Entry sw:NAGA_HAEIN

ID   NAGA_HAEIN              Reviewed;         381 AA.
AC   P44537;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   05-OCT-2016, entry version 100.
DE   RecName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000250|UniProtKB:P0AF18};
DE            Short=GlcNAc 6-P deacetylase {ECO:0000250|UniProtKB:P0AF18};
DE            EC=3.5.1.25 {ECO:0000250|UniProtKB:P0AF18};
GN   Name=nagA; OrderedLocusNames=HI_0140;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M.,
RA   Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA   Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA   Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA   Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA   Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Involved in the first committed step in the biosynthesis
CC       of amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-
CC       acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to
CC       yield glucosamine 6-phosphate and acetate.
CC       {ECO:0000250|UniProtKB:P0AF18}.
CC   -!- CATALYTIC ACTIVITY: N-acetyl-D-glucosamine 6-phosphate + H(2)O =
CC       D-glucosamine 6-phosphate + acetate.
CC       {ECO:0000250|UniProtKB:P0AF18}.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:P0AF18};
CC       Note=Binds 1 divalent metal cation per subunit.
CC       {ECO:0000250|UniProtKB:P0AF18};
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation;
CC       D-fructose 6-phosphate from N-acetylneuraminate: step 4/5.
CC       {ECO:0000250|UniProtKB:P0AF18}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0AF18}.
CC   -!- SIMILARITY: Belongs to the NagA family. {ECO:0000305}.
DR   EMBL; L42023; AAC21812.1; -; Genomic_DNA.
DR   PIR; E64050; E64050.
DR   RefSeq; NP_438309.1; NC_000907.1.
DR   RefSeq; WP_005694427.1; NC_000907.1.
DR   ProteinModelPortal; P44537; -.
DR   STRING; 71421.HI0140; -.
DR   EnsemblBacteria; AAC21812; AAC21812; HI_0140.
DR   GeneID; 951049; -.
DR   KEGG; hin:HI0140; -.
DR   PATRIC; 20188771; VBIHaeInf48452_0142.
DR   eggNOG; ENOG4105CE4; Bacteria.
DR   eggNOG; COG1820; LUCA.
DR   KO; K01443; -.
DR   OMA; NLYPARA; -.
DR   PhylomeDB; P44537; -.
DR   UniPathway; UPA00629; UER00683.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006046; P:N-acetylglucosamine catabolic process; ISS:UniProtKB.
DR   GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR   CDD; cd00854; NagA; 1.
DR   Gene3D; 2.30.40.10; -; 2.
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   3: Inferred from homology;
KW   Carbohydrate metabolism; Complete proteome; Hydrolase; Metal-binding;
KW   Reference proteome.
FT   CHAIN         1    381       N-acetylglucosamine-6-phosphate
FT                                deacetylase.
FT                                /FTId=PRO_0000170917.
FT   REGION      140    141       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P0AF18}.
FT   REGION      217    218       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P0AF18}.
FT   REGION      246    249       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P0AF18}.
FT   REGION      306    308       Substrate binding.
FT                                {ECO:0000250|UniProtKB:P0AF18}.
FT   ACT_SITE    271    271       Proton donor/acceptor.
FT                                {ECO:0000250|UniProtKB:P0AF18}.
FT   METAL       129    129       Divalent metal cation.
FT                                {ECO:0000250|UniProtKB:P0AF18}.
FT   METAL       193    193       Divalent metal cation; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P0AF18}.
FT   METAL       214    214       Divalent metal cation; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:P0AF18}.
FT   BINDING     226    226       Substrate.
FT                                {ECO:0000250|UniProtKB:P0AF18}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        52    378       ipfam:Amidohydro_1 [T]
SQ   SEQUENCE   381 AA;  41593 MW;  A502DF70BC03965A CRC64;
     MKYALINCVI YTKYDVLRDF AVIINGEIIE AVIPQAELET GIKTIDLQGN NLTAGFIDLQ
     LNGCGGVMFN DQTSVETLEI MQETNLKSGC TSFLPTFITA PDENIKSAVK IMREYLNKHK
     NQALGLHIEG PYLSIEKKGV HRPEYIREIT PEMKDFLCEN GDVITKMTIA AENPTINYTP
     DFVKAGIIVS VGHSNATYEV AKAAFHKGAT FATHLHNAMS PISSGREMGV VGAVLDSDVY
     TGIIVDGVHI NYGNVRIDKK IKGDKLCIVT DSIAAAGAPP ELESFTFVGK TIYIKEGRCY
     DANDTIAGAS ITMMESIKNA VEYVEIPLAE AIRMSNLYPA RAIGIDDRLG SVEKGKIANL
     AVFTPNYQVI GTVVNGKWKE N
//