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 03-AUG-2022, entry version 120.
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., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., 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 of
CC amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group
CC of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-
CC phosphate and acetate. {ECO:0000250|UniProtKB:P0AF18}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-D-glucosamine 6-phosphate = acetate + D-
CC glucosamine 6-phosphate; Xref=Rhea:RHEA:22936, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:57513, ChEBI:CHEBI:58725; EC=3.5.1.25;
CC Evidence={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; D-
CC 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 metallo-dependent hydrolases superfamily.
CC 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 AlphaFoldDB; P44537; -.
DR SMR; P44537; -.
DR STRING; 71421.HI_0140; -.
DR PRIDE; P44537; -.
DR EnsemblBacteria; AAC21812; AAC21812; HI_0140.
DR KEGG; hin:HI_0140; -.
DR PATRIC; fig|71421.8.peg.142; -.
DR eggNOG; COG1820; Bacteria.
DR HOGENOM; CLU_032482_2_2_6; -.
DR OMA; HAFNAMP; -.
DR PhylomeDB; P44537; -.
DR BioCyc; HINF71421:G1GJ1-152-MON; -.
DR UniPathway; UPA00629; UER00683.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0047419; F:N-acetylgalactosamine-6-phosphate deacetylase activity; IEA:UniProtKB-EC.
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 PANTHER; PTHR11113:SF14; PTHR11113:SF14; 1.
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; Hydrolase; Metal-binding; Reference proteome.
FT CHAIN 1..381
FT /note="N-acetylglucosamine-6-phosphate deacetylase"
FT /id="PRO_0000170917"
FT ACT_SITE 271
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 129
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 140..141
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 193
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 214
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 217..218
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 246..249
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 306..308
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
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
