ID A0A085GP11_9GAMM Unreviewed; 386 AA.
AC A0A085GP11;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000313|EMBL:KFC85456.1};
DE EC=3.-.-.- {ECO:0000313|EMBL:KFC85456.1};
DE EC=3.5.1.25 {ECO:0000313|EMBL:KFC85456.1};
GN ORFNames=GEAM_0421 {ECO:0000313|EMBL:KFC85456.1};
OS Ewingella americana ATCC 33852.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Ewingella.
OX NCBI_TaxID=910964 {ECO:0000313|EMBL:KFC85456.1, ECO:0000313|Proteomes:UP000028640};
RN [1] {ECO:0000313|EMBL:KFC85456.1, ECO:0000313|Proteomes:UP000028640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33852 {ECO:0000313|EMBL:KFC85456.1,
RC ECO:0000313|Proteomes:UP000028640};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (MAY-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:KFC85456.1}.
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DR EMBL; JMPJ01000018; KFC85456.1; -; Genomic_DNA.
DR RefSeq; WP_034787586.1; NZ_JMPJ01000018.1.
DR AlphaFoldDB; A0A085GP11; -.
DR STRING; 910964.GEAM_0421; -.
DR GeneID; 78382903; -.
DR eggNOG; COG1820; Bacteria.
DR OrthoDB; 9776488at2; -.
DR Proteomes; UP000028640; Unassembled WGS sequence.
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; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR003764; GlcNAc_6-P_deAcase.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11113; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1.
DR PANTHER; PTHR11113:SF14; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR PIRSF; PIRSF038994; NagA; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR038994};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR038994, ECO:0000313|EMBL:KFC85456.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR038994-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000028640}.
FT DOMAIN 42..362
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT ACT_SITE 269
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-1"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT BINDING 215..216
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT BINDING 306..308
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
SQ SEQUENCE 386 AA; 41968 MW; C5F171CC13C193DA CRC64;
MREVRLQGRE YQTGAAIEIT AVDGMIRQIA ALKEANESLP LIAPGLVDLQ VNGFGGVDFN
SFPFDEQDVE QVVQAMWQQG VTTFMPTVIT NADHEIEQMV TTLAKACQRS PRVEQSIAGI
HLEGPFLSLQ DGPRGAHQRG YIKAPDWALF QRWQDAAQGR IRLLTLSPEW PEADEFIRRC
VAEKVVVSIG HTSASAEQIA SAVQAGARMS THLGNGAHLT LPRHPNYIWE QLAQDDLWCA
MIADGEHLPL SVLKVFIRAK GEHAMLVSDV TSLAGMPPGR YHSHIGGEVL LSAEGRLSMA
DNPALLAGSA QCLLHGVNTL IKHGIATHVQ SLEMASLRPA SSMNLPTQQG LIVGAPLDAI
LLQQAADQTL VLRATYKNGV EVWRGE
//