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Database: UniProt
Entry: A0A085GP11_9GAMM
LinkDB: A0A085GP11_9GAMM
Original site: A0A085GP11_9GAMM 
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
//
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