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}; |
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| MyHits synonyms | NAGA_HAEIN , P44537 , A502DF70BC03965A |
 Legends: 1, ACT_SITE Proton donor/acceptor. {ECO:0000250|UniProtKB:P0AF18}; 2, Divalent metal cation. {ECO:0000250|UniProtKB:P0AF18}; 3, Divalent metal cation; via tele nitrogen. {ECO:0000250|UniProtKB:P0AF18}; 4, BINDING Substrate. {ECO:0000250|UniProtKB:P0AF18}; 5, REGION Substrate binding. {ECO:0000250|UniProtKB:P0AF18}.
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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 12-APR-2017, entry version 102.
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}.
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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 SMR; 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; -; 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 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
//
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