Entry bact:NAGA_ECOLI

ID   NAGA_ECOLI              Reviewed;         382 AA.
AC   P0AF18; P15300;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   12-APR-2017, entry version 93.
DE   RecName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000303|PubMed:2190615};
DE            Short=GlcNAc 6-P deacetylase {ECO:0000303|PubMed:9143339};
DE            EC=3.5.1.25 {ECO:0000269|PubMed:16630633, ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:17567048, ECO:0000269|PubMed:4861885, ECO:0000269|PubMed:9143339};
GN   Name=nagA; OrderedLocusNames=b0677, JW0663;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=2668691; DOI=10.1111/j.1365-2958.1989.tb00197.x;
RA   Plumbridge J.;
RT   "Sequence of the nagBACD operon in Escherichia coli K12 and pattern of
RT   transcription within the nag regulon.";
RL   Mol. Microbiol. 3:505-515(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=K12;
RX   PubMed=2190615;
RA   Peri K.G., Goldie H., Waygood E.B.;
RT   "Cloning and characterization of the N-acetylglucosamine operon of
RT   Escherichia coli.";
RL   Biochem. Cell Biol. 68:123-137(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
RA   Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA   Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA   Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA   Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA   Yano M., Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=K12;
RX   PubMed=4861885; DOI=10.1042/bj1050121;
RA   White R.J., Pasternak C.A.;
RT   "The purification and properties of N-acetylglucosamine 6-phosphate
RT   deacetylase from Escherichia coli.";
RL   Biochem. J. 105:121-125(1967).
RN   [7]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=K12;
RX   PubMed=8349539; DOI=10.1128/jb.175.16.4951-4956.1993;
RA   Plumbridge J.A., Cochet O., Souza J.M., Altamirano M.M.,
RA   Calcagno M.L., Badet B.;
RT   "Coordinated regulation of amino sugar-synthesizing and -degrading
RT   enzymes in Escherichia coli K-12.";
RL   J. Bacteriol. 175:4951-4956(1993).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, CIRCULAR DICHROISM, AND REACTION MECHANISM.
RC   STRAIN=K12;
RX   PubMed=9143339; DOI=10.1006/abbi.1997.9780;
RA   Souza J.M., Plumbridge J.A., Calcagno M.L.;
RT   "N-acetylglucosamine-6-phosphate deacetylase from Escherichia coli:
RT   purification and molecular and kinetic characterization.";
RL   Arch. Biochem. Biophys. 340:338-346(1997).
RN   [9]
RP   CRYSTALLIZATION.
RC   STRAIN=K12;
RX   PubMed=10771446; DOI=10.1107/S0907444900003668;
RA   Ferreira F.M., Mendoza-Hernandez G., Calcagno M.L., Minauro F.,
RA   Delboni L.F., Oliva G.;
RT   "Crystallization and preliminary crystallographic analysis of N-
RT   acetylglucosamine 6-phosphate deacetylase from Escherichia coli.";
RL   Acta Crystallogr. D 56:670-672(2000).
RN   [10]
RP   INDUCTION.
RC   STRAIN=K12;
RX   PubMed=12813061; DOI=10.1128/JB.185.13.3696-3702.2003;
RA   Minagawa S., Ogasawara H., Kato A., Yamamoto K., Eguchi Y., Oshima T.,
RA   Mori H., Ishihama A., Utsumi R.;
RT   "Identification and molecular characterization of the Mg2+ stimulon of
RT   Escherichia coli.";
RL   J. Bacteriol. 185:3696-3702(2003).
RN   [11]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ENZYME
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF
RP   GLN-59; ASN-61; GLU-131; HIS-143; HIS-251 AND ASP-273, AND REACTION
RP   MECHANISM.
RC   STRAIN=K12;
RX   PubMed=17567047; DOI=10.1021/bi700543x;
RA   Hall R.S., Xiang D.F., Xu C., Raushel F.M.;
RT   "N-Acetyl-D-glucosamine-6-phosphate deacetylase: substrate activation
RT   via a single divalent metal ion.";
RL   Biochemistry 46:7942-7952(2007).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF APOENZYME, FUNCTION,
RP   CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, AND SUBUNIT.
RC   STRAIN=K12;
RX   PubMed=16630633; DOI=10.1016/j.jmb.2006.03.024;
RA   Ferreira F.M., Mendoza-Hernandez G., Castaneda-Bueno M., Aparicio R.,
RA   Fischer H., Calcagno M.L., Oliva G.;
RT   "Structural analysis of N-acetylglucosamine-6-phosphate deacetylase
RT   apoenzyme from Escherichia coli.";
RL   J. Mol. Biol. 359:308-321(2006).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF APOENZYME; WILD-TYPE IN
RP   COMPLEX WITH ZINC AND MUTANT ASN-273 IN COMPLEX WITH TRANSITION STATE
RP   INHIBITOR AND ZINC, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF
RP   ASP-273, COFACTOR, SUBUNIT, AND ACTIVE SITE.
RC   STRAIN=K12;
RX   PubMed=17567048; DOI=10.1021/bi700544c;
RA   Hall R.S., Brown S., Fedorov A.A., Fedorov E.V., Xu C., Babbitt P.C.,
RA   Almo S.C., Raushel F.M.;
RT   "Structural diversity within the mononuclear and binuclear active
RT   sites of N-acetyl-D-glucosamine-6-phosphate deacetylase.";
RL   Biochemistry 46:7953-7962(2007).
CC   -!- FUNCTION: Involved in the first step in the biosynthesis of amino-
CC       sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group
CC       of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield
CC       glucosamine 6-phosphate and acetate. In vitro, can also hydrolyze
CC       substrate analogs such as N-thioacetyl-D-glucosamine-6-phosphate,
CC       N-trifluoroacetyl-D-glucosamine-6-phosphate, N-acetyl-D-
CC       glucosamine-6-sulfate, N-acetyl-D-galactosamine-6-phosphate, and
CC       N-formyl-D-glucosamine-6-phosphate. {ECO:0000269|PubMed:16630633,
CC       ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:17567048,
CC       ECO:0000269|PubMed:2190615, ECO:0000269|PubMed:4861885,
CC       ECO:0000269|PubMed:9143339}.
CC   -!- CATALYTIC ACTIVITY: N-acetyl-D-glucosamine 6-phosphate + H(2)O =
CC       D-glucosamine 6-phosphate + acetate. {ECO:0000269|PubMed:16630633,
CC       ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:17567048,
CC       ECO:0000269|PubMed:4861885, ECO:0000269|PubMed:9143339}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:16630633,
CC         ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:17567048};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000269|PubMed:16630633,
CC         ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:17567048};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:16630633,
CC         ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:17567048};
CC       Name=Cd(2+); Xref=ChEBI:CHEBI:48775;
CC         Evidence={ECO:0000269|PubMed:16630633,
CC         ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:17567048};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000269|PubMed:16630633,
CC         ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:17567048};
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000269|PubMed:16630633,
CC         ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:17567048};
CC       Note=Binds 1 divalent metal cation per subunit. The highest
CC       efficient metals are Zn(2+) and Co(2+), followed by Mn(2+),
CC       Cd(2+), Fe(2+) and Ni(2+). {ECO:0000269|PubMed:16630633,
CC       ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:17567048};
CC   -!- ENZYME REGULATION: Inhibited by high substrate concentration and
CC       by products glucosamine 6-phosphate and acetate. Completely
CC       inactivated by the treatment with 5,5'-dithio-bis(2-nitrobenzoate)
CC       or 2,2'-dithio-pyridine (2-DPDS). Inhibited by 1,10-phenanthroline
CC       and EDTA. {ECO:0000269|PubMed:16630633,
CC       ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:4861885,
CC       ECO:0000269|PubMed:9143339}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.3 mM for N-acetyl-glucosamine 6-phosphate (at 30 degrees
CC         Celsius and pH 7.5) {ECO:0000269|PubMed:17567047,
CC         ECO:0000269|PubMed:4861885, ECO:0000269|PubMed:9143339};
CC         KM=0.8 mM for N-acetyl-glucosamine 6-phosphate (at 37 degrees
CC         Celsius and pH 8.0) {ECO:0000269|PubMed:17567047,
CC         ECO:0000269|PubMed:4861885, ECO:0000269|PubMed:9143339};
CC         KM=20 mM for glucosamine 6-phosphate (at 30 degrees Celsius and
CC         pH 7.5) {ECO:0000269|PubMed:17567047,
CC         ECO:0000269|PubMed:4861885, ECO:0000269|PubMed:9143339};
CC         KM=20 mM for acetate (at 30 degrees Celsius and pH 7.5)
CC         {ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:4861885,
CC         ECO:0000269|PubMed:9143339};
CC         KM=0.08 mM for N-acetyl-D-glucosamine-6-phosphate (at 30 degrees
CC         Celsius and pH 7.5 using Zn-reconstituted form of the enzyme)
CC         {ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:4861885,
CC         ECO:0000269|PubMed:9143339};
CC         KM=1.24 mM for N-acetyl-D-galactosamine-6-phosphate (at 30
CC         degrees Celsius and pH 7.5 using Zn-reconstituted form of the
CC         enzyme) {ECO:0000269|PubMed:17567047,
CC         ECO:0000269|PubMed:4861885, ECO:0000269|PubMed:9143339};
CC         Note=kcat is 102 sec(-1) for the deacetylation of N-acetyl-D-
CC         glucosamine-6-phosphate by the Zn-enzyme. The Cd-NagA catalyzes
CC         the hydrolysis of N-thioacetyl-D-glucosamine-6-phosphate
CC         substrate about an order of magnitude better than does the Zn-
CC         substituted enzyme. The N-trifluoroacetyl substituted substrate
CC         is hydrolyzed 26 times faster than the natural substrate, but
CC         the N-formyl substrate is hydrolyzed more slowly by a factor of
CC         5. {ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:4861885,
CC         ECO:0000269|PubMed:9143339};
CC       pH dependence:
CC         Optimum pH is 8.5. {ECO:0000269|PubMed:17567047,
CC         ECO:0000269|PubMed:4861885, ECO:0000269|PubMed:9143339};
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation;
CC       D-fructose 6-phosphate from N-acetylneuraminate: step 4/5.
CC       {ECO:0000305|PubMed:2190615}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16630633,
CC       ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:17567048,
CC       ECO:0000269|PubMed:9143339}.
CC   -!- INDUCTION: By N-acetylglucosamine. Induced by low extracellular
CC       levels of magnesium via the PhoQ/PhoP two-component regulatory
CC       system. {ECO:0000269|PubMed:12813061}.
CC   -!- DISRUPTION PHENOTYPE: Synthesizes high levels of glucosamine-6-
CC       phosphate deaminase and over half of the amount of glucosamine-6-
CC       phosphate synthase compared to wild-type.
CC       {ECO:0000269|PubMed:8349539}.
CC   -!- SIMILARITY: Belongs to the NagA family. {ECO:0000305}.
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DR   EMBL; X14135; CAA32353.1; -; Genomic_DNA.
DR   EMBL; AF052007; AAC09325.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73771.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35320.1; -; Genomic_DNA.
DR   PIR; A37018; A37018.
DR   RefSeq; NP_415203.1; NC_000913.3.
DR   RefSeq; WP_000271153.1; NZ_LN832404.1.
DR   PDB; 1YMY; X-ray; 2.60 A; A/B=1-382.
DR   PDB; 1YRR; X-ray; 2.00 A; A/B=1-382.
DR   PDB; 2P50; X-ray; 2.20 A; A/B/C/D=1-382.
DR   PDB; 2P53; X-ray; 2.10 A; A/B=1-382.
DR   PDBsum; 1YMY; -.
DR   PDBsum; 1YRR; -.
DR   PDBsum; 2P50; -.
DR   PDBsum; 2P53; -.
DR   ProteinModelPortal; P0AF18; -.
DR   SMR; P0AF18; -.
DR   BioGrid; 4261208; 12.
DR   DIP; DIP-10297N; -.
DR   IntAct; P0AF18; 5.
DR   STRING; 511145.b0677; -.
DR   EPD; P0AF18; -.
DR   PaxDb; P0AF18; -.
DR   PRIDE; P0AF18; -.
DR   EnsemblBacteria; AAC73771; AAC73771; b0677.
DR   EnsemblBacteria; BAA35320; BAA35320; BAA35320.
DR   GeneID; 945289; -.
DR   KEGG; ecj:JW0663; -.
DR   KEGG; eco:b0677; -.
DR   PATRIC; 32116539; VBIEscCol129921_0702.
DR   EchoBASE; EB0626; -.
DR   EcoGene; EG10632; nagA.
DR   eggNOG; ENOG4105CE4; Bacteria.
DR   eggNOG; COG1820; LUCA.
DR   HOGENOM; HOG000275008; -.
DR   InParanoid; P0AF18; -.
DR   KO; K01443; -.
DR   OMA; PAGANMD; -.
DR   PhylomeDB; P0AF18; -.
DR   BioCyc; EcoCyc:NAG6PDEACET-MONOMER; -.
DR   BioCyc; MetaCyc:NAG6PDEACET-MONOMER; -.
DR   BRENDA; 3.5.1.25; 2026.
DR   SABIO-RK; P0AF18; -.
DR   UniPathway; UPA00629; UER00683.
DR   EvolutionaryTrace; P0AF18; -.
DR   PRO; PR:P0AF18; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006046; P:N-acetylglucosamine catabolic process; IDA:UniProtKB.
DR   GO; GO:0019262; P:N-acetylneuraminate catabolic process; IMP:EcoCyc.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR   CDD; cd00854; NagA; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR003764; GlcNAc_6-P_deAcase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   PIRSF; PIRSF038994; NagA; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR00221; nagA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Complete proteome; Hydrolase;
KW   Metal-binding; Reference proteome; Zinc.
FT   CHAIN         1    382       N-acetylglucosamine-6-phosphate
FT                                deacetylase.
FT                                /FTId=PRO_0000170915.
FT   REGION      142    143       Substrate binding.
FT                                {ECO:0000269|PubMed:17567048}.
FT   REGION      219    220       Substrate binding.
FT                                {ECO:0000269|PubMed:17567048}.
FT   REGION      248    251       Substrate binding.
FT                                {ECO:0000269|PubMed:17567048}.
FT   REGION      306    308       Substrate binding.
FT                                {ECO:0000269|PubMed:17567048}.
FT   ACT_SITE    273    273       Proton donor/acceptor.
FT                                {ECO:0000269|PubMed:17567048}.
FT   METAL       131    131       Zinc. {ECO:0000269|PubMed:17567048}.
FT   METAL       195    195       Zinc; via tele nitrogen.
FT                                {ECO:0000269|PubMed:17567048}.
FT   METAL       216    216       Zinc; via tele nitrogen.
FT                                {ECO:0000269|PubMed:17567048}.
FT   BINDING     227    227       Substrate. {ECO:0000269|PubMed:17567048}.
FT   MUTAGEN      59     59       Q->H: Large decrease in catalytic
FT                                activity and substrate affinity, and
FT                                increase in the average amount of Zn
FT                                bound to the protein, suggesting that an
FT                                additional metal ion can bind to this
FT                                mutant; when associated with H-61.
FT                                {ECO:0000269|PubMed:17567047,
FT                                ECO:0000269|PubMed:17567048}.
FT   MUTAGEN      61     61       N->H: Large decrease in catalytic
FT                                activity and substrate affinity, and
FT                                increase in the average amount of Zn
FT                                bound to the protein, suggesting that an
FT                                additional metal ion can bind to this
FT                                mutant; when associated with H-59.
FT                                {ECO:0000269|PubMed:17567047}.
FT   MUTAGEN     131    131       E->Q,A: Large reduction in the amount of
FT                                the metal cofactor bound to the enzyme.
FT                                {ECO:0000269|PubMed:17567047}.
FT   MUTAGEN     143    143       H->N: Dramatic decrease in catalytic
FT                                activity and moderate decrease in
FT                                substrate affinity, producing a 6000-fold
FT                                decrease in catalytic efficiency.
FT                                {ECO:0000269|PubMed:17567047}.
FT   MUTAGEN     143    143       H->Q: 180-fold decrease in catalytic
FT                                efficiency.
FT                                {ECO:0000269|PubMed:17567047}.
FT   MUTAGEN     251    251       H->N: 500-fold decrease in catalytic
FT                                efficiency.
FT                                {ECO:0000269|PubMed:17567047}.
FT   MUTAGEN     273    273       D->N,A: Loss of catalytic activity.
FT                                {ECO:0000269|PubMed:17567047}.
FT   STRAND        2     10       {ECO:0000244|PDB:1YRR}.
FT   STRAND       15     24       {ECO:0000244|PDB:1YRR}.
FT   STRAND       27     33       {ECO:0000244|PDB:1YRR}.
FT   HELIX        34     36       {ECO:0000244|PDB:1YRR}.
FT   STRAND       43     45       {ECO:0000244|PDB:1YRR}.
FT   STRAND       50     53       {ECO:0000244|PDB:1YRR}.
FT   STRAND       55     63       {ECO:0000244|PDB:1YRR}.
FT   STRAND       66     71       {ECO:0000244|PDB:1YRR}.
FT   TURN         72     74       {ECO:0000244|PDB:1YRR}.
FT   HELIX        77     89       {ECO:0000244|PDB:1YRR}.
FT   STRAND       92    100       {ECO:0000244|PDB:1YRR}.
FT   HELIX       104    120       {ECO:0000244|PDB:1YRR}.
FT   STRAND      123    125       {ECO:0000244|PDB:2P50}.
FT   STRAND      128    131       {ECO:0000244|PDB:1YRR}.
FT   HELIX       137    139       {ECO:0000244|PDB:2P53}.
FT   HELIX       145    147       {ECO:0000244|PDB:2P53}.
FT   HELIX       150    161       {ECO:0000244|PDB:1YRR}.
FT   TURN        162    165       {ECO:0000244|PDB:1YRR}.
FT   STRAND      166    171       {ECO:0000244|PDB:1YRR}.
FT   HELIX       173    175       {ECO:0000244|PDB:1YRR}.
FT   HELIX       178    186       {ECO:0000244|PDB:1YRR}.
FT   STRAND      190    193       {ECO:0000244|PDB:1YRR}.
FT   HELIX       200    209       {ECO:0000244|PDB:1YRR}.
FT   STRAND      213    216       {ECO:0000244|PDB:1YRR}.
FT   TURN        217    220       {ECO:0000244|PDB:1YRR}.
FT   HELIX       230    237       {ECO:0000244|PDB:1YRR}.
FT   STRAND      242    246       {ECO:0000244|PDB:1YRR}.
FT   STRAND      248    252       {ECO:0000244|PDB:1YRR}.
FT   HELIX       254    264       {ECO:0000244|PDB:1YRR}.
FT   HELIX       265    267       {ECO:0000244|PDB:1YRR}.
FT   STRAND      268    271       {ECO:0000244|PDB:1YRR}.
FT   TURN        276    279       {ECO:0000244|PDB:1YRR}.
FT   STRAND      283    287       {ECO:0000244|PDB:1YRR}.
FT   STRAND      290    294       {ECO:0000244|PDB:1YRR}.
FT   STRAND      298    301       {ECO:0000244|PDB:2P53}.
FT   STRAND      306    309       {ECO:0000244|PDB:1YRR}.
FT   HELIX       313    324       {ECO:0000244|PDB:1YRR}.
FT   HELIX       328    335       {ECO:0000244|PDB:1YRR}.
FT   HELIX       337    342       {ECO:0000244|PDB:1YRR}.
FT   TURN        346    348       {ECO:0000244|PDB:1YRR}.
FT   STRAND      349    351       {ECO:0000244|PDB:1YRR}.
FT   STRAND      360    363       {ECO:0000244|PDB:1YRR}.
FT   STRAND      369    374       {ECO:0000244|PDB:1YRR}.
FT   STRAND      377    381       {ECO:0000244|PDB:1YRR}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        50    379       ipfam:Amidohydro_1 [T]
SQ   SEQUENCE   382 AA;  40949 MW;  A10B015ADFC98FCA CRC64;
     MYALTQGRIF TGHEFLDDHA VVIADGLIKS VCPVAELPPE IEQRSLNGAI LSPGFIDVQL
     NGCGGVQFND TAEAVSVETL EIMQKANEKS GCTNYLPTLI TTSDELMKQG VRVMREYLAK
     HPNQALGLHL EGPWLNLVKK GTHNPNFVRK PDAALVDFLC ENADVITKVT LAPEMVPAEV
     ISKLANAGIV VSAGHSNATL KEAKAGFRAG ITFATHLYNA MPYITGREPG LAGAILDEAD
     IYCGIIADGL HVDYANIRNA KRLKGDKLCL VTDATAPAGA NIEQFIFAGK TIYYRNGLCV
     DENGTLSGSS LTMIEGVRNL VEHCGIALDE VLRMATLYPA RAIGVEKRLG TLAAGKVANL
     TAFTPDFKIT KTIVNGNEVV TQ
//