MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000250|UniProtKB:P0AF18}; Short=GlcNAc 6-P deacetylase {ECO:0000250|UniProtKB:P0AF18}; EC=3.5.1.25 {ECO:0000250|UniProtKB:P0AF18}; |
 |
|
| MyHits synonyms | NAGA_VIBCH , O32445 , Q9KTA9 , 34906344A3F92A0F |
 Legends: 1, ACT_SITE Proton donor/acceptor. {ECO:0000250|UniProtKB:P0AF18}; 2, Divalent metal cation. {ECO:0000269|Ref.3}; 3, Divalent metal cation; via tele nitrogen. {ECO:0000269|Ref.3}; 4, BINDING Substrate. {ECO:0000269|Ref.3}; 5, CONFLICT T -> I (in Ref. 1; BAA22834). {ECO:0000305}; 6, REGION Substrate binding. {ECO:0000269|Ref.3}; 7, STRAND {ECO:0000244|PDB:3IV8}; 8, HELIX {ECO:0000244|PDB:3IV8}; 9, TURN {ECO:0000244|PDB:3IV8}; 10, HELIX {ECO:0000244|PDB:3EGJ}; 11, TURN {ECO:0000244|PDB:3EGJ}.
| |
ID NAGA_VIBCH Reviewed; 378 AA.
AC O32445; Q9KTA9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 12-APR-2017, entry version 104.
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=VC_0994;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC Vibrionaceae; Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NON-O1 / 1148A;
RX PubMed=9301118; DOI=10.1271/bbb.61.1349;
RA Yamano N., Oura N., Wang J., Fujishima S.;
RT "Cloning and sequencing of the genes for N-acetylglucosamine use that
RT construct divergent operons (nagE-nagAC) from Vibrio cholerae non-
RT O1.";
RL Biosci. Biotechnol. Biochem. 61:1349-1353(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A.,
RA Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L.,
RA Ermolaeva M.D., Vamathevan J.J., Bass S., Qin H., Dragoi I.,
RA Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D.,
RA Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R.,
RA Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) IN COMPLEXES WITH NICKEL AND
RP FRUCTOSE-6-PHOSPHATE, COFACTOR, AND SUBUNIT.
RG Center for structural genomics of infectious diseases (CSGID);
RT "X-ray crystal structure of N-acetylglucosamine-6-phosphate
RT deacetylase from Vibrio cholerae complexed with fructose 6-
RT phosphate.";
RL Submitted (AUG-2009) to the PDB data bank.
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:0000269|Ref.3};
CC Note=Binds 1 divalent metal cation per subunit. Ni(2+) ion is seen
CC in the structure. {ECO:0000269|Ref.3};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation;
CC D-fructose 6-phosphate from N-acetylneuraminate: step 4/5.
CC {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the NagA family. {ECO:0000305}.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D87820; BAA22834.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF94155.1; -; Genomic_DNA.
DR PIR; E82254; E82254.
DR PIR; JC5649; JC5649.
DR RefSeq; NP_230640.1; NC_002505.1.
DR RefSeq; WP_000271133.1; NC_002505.1.
DR PDB; 3EGJ; X-ray; 2.90 A; A/B=1-378.
DR PDB; 3IV8; X-ray; 2.53 A; A/B/C/D=1-378.
DR PDBsum; 3EGJ; -.
DR PDBsum; 3IV8; -.
DR ProteinModelPortal; O32445; -.
DR SMR; O32445; -.
DR STRING; 243277.VC0994; -.
DR DNASU; 2614247; -.
DR EnsemblBacteria; AAF94155; AAF94155; VC_0994.
DR GeneID; 2614247; -.
DR KEGG; vch:VC0994; -.
DR PATRIC; 20081086; VBIVibCho83274_0947.
DR eggNOG; ENOG4105CE4; Bacteria.
DR eggNOG; COG1820; LUCA.
DR KO; K01443; -.
DR OMA; PAGANMD; -.
DR BioCyc; MetaCyc:MONOMER-16875; -.
DR BioCyc; VCHO:VC0994-MONOMER; -.
DR UniPathway; UPA00629; UER00683.
DR EvolutionaryTrace; O32445; -.
DR Proteomes; UP000000584; Chromosome 1.
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:0006044; P:N-acetylglucosamine metabolic process; ISS:TIGR.
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; -; 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; Nickel; Reference proteome.
FT CHAIN 1 378 N-acetylglucosamine-6-phosphate
FT deacetylase.
FT /FTId=PRO_0000170918.
FT REGION 139 140 Substrate binding. {ECO:0000269|Ref.3}.
FT REGION 216 217 Substrate binding. {ECO:0000269|Ref.3}.
FT REGION 245 248 Substrate binding. {ECO:0000269|Ref.3}.
FT REGION 303 305 Substrate binding. {ECO:0000269|Ref.3}.
FT ACT_SITE 270 270 Proton donor/acceptor.
FT {ECO:0000250|UniProtKB:P0AF18}.
FT METAL 128 128 Divalent metal cation.
FT {ECO:0000269|Ref.3}.
FT METAL 192 192 Divalent metal cation; via tele nitrogen.
FT {ECO:0000269|Ref.3}.
FT METAL 213 213 Divalent metal cation; via tele nitrogen.
FT {ECO:0000269|Ref.3}.
FT BINDING 224 224 Substrate. {ECO:0000269|Ref.3}.
FT CONFLICT 79 79 T -> I (in Ref. 1; BAA22834).
FT {ECO:0000305}.
FT STRAND 2 10 {ECO:0000244|PDB:3IV8}.
FT STRAND 15 24 {ECO:0000244|PDB:3IV8}.
FT STRAND 27 33 {ECO:0000244|PDB:3IV8}.
FT HELIX 34 36 {ECO:0000244|PDB:3IV8}.
FT STRAND 42 53 {ECO:0000244|PDB:3IV8}.
FT STRAND 55 60 {ECO:0000244|PDB:3IV8}.
FT TURN 68 70 {ECO:0000244|PDB:3IV8}.
FT HELIX 74 86 {ECO:0000244|PDB:3IV8}.
FT STRAND 89 98 {ECO:0000244|PDB:3IV8}.
FT HELIX 101 117 {ECO:0000244|PDB:3IV8}.
FT STRAND 119 122 {ECO:0000244|PDB:3IV8}.
FT STRAND 125 128 {ECO:0000244|PDB:3IV8}.
FT HELIX 134 136 {ECO:0000244|PDB:3IV8}.
FT TURN 142 144 {ECO:0000244|PDB:3IV8}.
FT HELIX 150 158 {ECO:0000244|PDB:3IV8}.
FT TURN 159 161 {ECO:0000244|PDB:3IV8}.
FT STRAND 162 168 {ECO:0000244|PDB:3IV8}.
FT HELIX 170 172 {ECO:0000244|PDB:3EGJ}.
FT HELIX 175 183 {ECO:0000244|PDB:3IV8}.
FT STRAND 187 190 {ECO:0000244|PDB:3IV8}.
FT HELIX 197 205 {ECO:0000244|PDB:3IV8}.
FT STRAND 210 213 {ECO:0000244|PDB:3IV8}.
FT STRAND 216 218 {ECO:0000244|PDB:3IV8}.
FT HELIX 227 234 {ECO:0000244|PDB:3IV8}.
FT STRAND 239 243 {ECO:0000244|PDB:3IV8}.
FT STRAND 245 249 {ECO:0000244|PDB:3IV8}.
FT HELIX 251 261 {ECO:0000244|PDB:3IV8}.
FT HELIX 262 264 {ECO:0000244|PDB:3IV8}.
FT STRAND 265 268 {ECO:0000244|PDB:3IV8}.
FT TURN 273 276 {ECO:0000244|PDB:3IV8}.
FT STRAND 280 286 {ECO:0000244|PDB:3IV8}.
FT STRAND 288 292 {ECO:0000244|PDB:3IV8}.
FT STRAND 295 297 {ECO:0000244|PDB:3IV8}.
FT TURN 299 301 {ECO:0000244|PDB:3EGJ}.
FT HELIX 310 319 {ECO:0000244|PDB:3IV8}.
FT HELIX 325 332 {ECO:0000244|PDB:3IV8}.
FT HELIX 334 340 {ECO:0000244|PDB:3IV8}.
FT TURN 343 345 {ECO:0000244|PDB:3IV8}.
FT STRAND 346 348 {ECO:0000244|PDB:3IV8}.
FT STRAND 357 360 {ECO:0000244|PDB:3IV8}.
FT STRAND 366 371 {ECO:0000244|PDB:3IV8}.
FT STRAND 374 377 {ECO:0000244|PDB:3IV8}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 51 374 ipfam:Amidohydro_1 [T]
SQ SEQUENCE 378 AA; 40956 MW; 34906344A3F92A0F CRC64;
MYALTNCKIY TGNDVLVKHA VIINGDKIEA VCPIESLPSE MNVVDLNGAN LSPGFIDLQL
NGCGGVMFND EITAETIDTM HKANLKSGCT SFLPTLITSS DENMRQAIAA AREYQAKYPN
QSLGLHLEGP YLNVMKKGIH SVDFIRPSDD TMIDTICANS DVIAKVTLAP ENNKPEHIEK
LVKAGIVVSI GHTNATYSEA RKSFESGITF ATHLFNAMTP MVGREPGVVG AIYDTPEVYA
GIIADGFHVD YANIRIAHKI KGEKLVLVTD ATAPAGAEMD YFIFVGKKVY YRDGKCVDEN
GTLGGSALTM IEAVQNTVEH VGIALDEALR MATLYPAKAI GVDEKLGRIK KGMIANLTVF
DRDFNVKATV VNGQYEQN
//
| |