NAGA_VIBFU
ID NAGA_VIBFU Reviewed; 399 AA.
AC P96166;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000250|UniProtKB:O34450};
DE Short=GlcNAc 6-P deacetylase {ECO:0000250|UniProtKB:O34450};
DE EC=3.5.1.25 {ECO:0000250|UniProtKB:P0AF18};
GN Name=manD;
OS Vibrio furnissii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=29494;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SR1514;
RX PubMed=8969210; DOI=10.1074/jbc.271.52.33468;
RA Bouma C.L., Roseman S.;
RT "Sugar transport by the marine chitinolytic bacterium Vibrio furnissii.
RT Molecular cloning and analysis of the mannose/glucose permease.";
RL J. Biol. Chem. 271:33468-33475(1996).
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:O34450}.
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:O34450};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000250|UniProtKB:O34450};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC fructose 6-phosphate from N-acetylneuraminate: step 4/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O34450}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC NagA family. {ECO:0000305}.
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DR EMBL; U65015; AAC44683.1; -; Genomic_DNA.
DR AlphaFoldDB; P96166; -.
DR SMR; P96166; -.
DR UniPathway; UPA00629; UER00683.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
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:0042803; F:protein homodimerization 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 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.
FT CHAIN 1..399
FT /note="N-acetylglucosamine-6-phosphate deacetylase"
FT /id="PRO_0000170919"
FT ACT_SITE 279
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O34450"
FT BINDING 65
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O34450"
FT BINDING 67
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O34450"
FT BINDING 135
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O34450"
FT BINDING 135
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O34450"
FT BINDING 146..147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O34450"
FT BINDING 201
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O34450"
FT BINDING 222
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O34450"
FT BINDING 225..226
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O34450"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF18"
FT BINDING 254..257
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O34450"
FT BINDING 279
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O34450"
FT BINDING 312..314
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O34450"
SQ SEQUENCE 399 AA; 43122 MW; 82B1B9C3E5C99A37 CRC64;
MESKSHAHCF RAQRVLHGKQ WQQDAVVTVD ENGTISAIES YDGQRHADAI PLGPVDLMPG
LIDSHVHGSQ GCDVMDATHD SLNTMSRYFA TLGVTAFVAT TVTAPVAKIR AALAQVAKSK
HDGVDGAEIL GAYLEGPYFT EKNKGAHPTQ WFRELAVEEL EDWISYSDNQ LLKVALAPEK
TGALDAIRYL DAHGIHVMLG HSDADYEQVK AALAAGAKGI VHCYNGMRGL HHRDPGVVGA
GLLHPHCFVE MIADGHHVHP AAIDVAHRCC GSRMTLITDA MRATGMPDGQ YTLGEYQVDM
KQGVVMTSSG GLAGSTLTLL RGVKNIHRWL NVPIEQAWLM ASYTPAESLG IQHQLGSLEV
GKYASMVAVS SDFSIEKTWV KGRLVFDAAT SPRQEALCI
