ID A0A073KFG4_9BACI Unreviewed; 380 AA.
AC A0A073KFG4;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000313|EMBL:KEK25989.1};
GN ORFNames=BAGA_01770 {ECO:0000313|EMBL:KEK25989.1};
OS Bacillus gaemokensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=574375 {ECO:0000313|EMBL:KEK25989.1, ECO:0000313|Proteomes:UP000027778};
RN [1] {ECO:0000313|EMBL:KEK25989.1, ECO:0000313|Proteomes:UP000027778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15801 {ECO:0000313|EMBL:KEK25989.1,
RC ECO:0000313|Proteomes:UP000027778};
RA Lai Q., Liu Y., Shao Z.;
RT "Draft genome sequence of Bacillus gaemokensis JCM 15801 (MCCC 1A00707).";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRSR:PIRSR038994-3};
CC Note=Binds 1 divalent metal cation per subunit.
CC {ECO:0000256|PIRSR:PIRSR038994-3};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC NagA family. {ECO:0000256|ARBA:ARBA00010716,
CC ECO:0000256|PIRNR:PIRNR038994}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEK25989.1}.
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DR EMBL; JOTM01000001; KEK25989.1; -; Genomic_DNA.
DR RefSeq; WP_033672881.1; NZ_LTAQ01000001.1.
DR AlphaFoldDB; A0A073KFG4; -.
DR STRING; 574375.AZF08_01845; -.
DR eggNOG; COG1820; Bacteria.
DR OrthoDB; 9776488at2; -.
DR Proteomes; UP000027778; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008448; F:N-acetylglucosamine-6-phosphate deacetylase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IEA:InterPro.
DR CDD; cd00854; NagA; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 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 NCBIfam; TIGR00221; nagA; 1.
DR PANTHER; PTHR11113; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1.
DR PANTHER; PTHR11113:SF16; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR PIRSF; PIRSF038994; NagA; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|PIRNR:PIRNR038994};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR038994};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR038994-3}.
FT DOMAIN 53..363
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT ACT_SITE 271
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-1"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
SQ SEQUENCE 380 AA; 41623 MW; 9FBFADE49907BB54 CRC64;
MKTQVVINAN IYTGQEVMES GFIRYAEKIE EIGLMAQYVS QENETVFDAE GKIVIPGMID
VHIHGGYDID AMDANSDGLV TLGKEMLKEG VTTYFPTTMT QAPEAIEAAL HAAKEAKEKG
AHFEYIHLEG PYVSKKRAGA QPLEHIVPAN IEQFKQWQEA SGNLIKLVTY APEEEGAEAF
EQYLAETGVV GTIGHTDAID ADLKNRNITH ATHLYNQMRG LHHREPGVVG HVLLNPDVMV
EVITDGIHIH PDMVKLAYKL KGPKKVSVIT DAMRAKGLED GLYELGGQPV HVKDGSARLE
DGTLAGSILK MDQAFRNVIE FTGCSVEEAV LMTSVNQAEE FGLTNKGALV AGKDADFVVM
TEDLHVYDTV RLGIHMKEGK
//
