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Database: UniProt
Entry: A0A1W2CCP7_9RHOB
LinkDB: A0A1W2CCP7_9RHOB
Original site: A0A1W2CCP7_9RHOB 
ID   A0A1W2CCP7_9RHOB        Unreviewed;       382 AA.
AC   A0A1W2CCP7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000313|EMBL:SMC82963.1};
GN   ORFNames=SAMN06295998_10772 {ECO:0000313|EMBL:SMC82963.1};
OS   Primorskyibacter flagellatus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Primorskyibacter.
OX   NCBI_TaxID=1387277 {ECO:0000313|EMBL:SMC82963.1, ECO:0000313|Proteomes:UP000192330};
RN   [1] {ECO:0000313|EMBL:SMC82963.1, ECO:0000313|Proteomes:UP000192330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12644 {ECO:0000313|EMBL:SMC82963.1,
RC   ECO:0000313|Proteomes:UP000192330};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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|PIRNR:PIRNR038994}.
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DR   EMBL; FWYD01000007; SMC82963.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W2CCP7; -.
DR   STRING; 1387277.SAMN06295998_10772; -.
DR   Proteomes; UP000192330; 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   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:SF16; 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};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR038994-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192330}.
FT   DOMAIN          41..365
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         122
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         190
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT   BINDING         211
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT   BINDING         214..215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         246
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         305..307
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
SQ   SEQUENCE   382 AA;  39821 MW;  A02056DBE7C01D8D CRC64;
     MRQEATYSGR DFHSGEGRAL HVRGGVIEKI TDCAAEGLPL LSPGFVDLQV NGFAGHDLND
     GQLTPETVEA LSEALAAVGV AAYLPTLITA SETELCQRLS AIHTAQQTMP FSQGMIAGVH
     VEGPSISPKD GPRGAHPLAH VRPPSIEEFN RWQQASGGLV RMVTLAPEVV GACQYIQALS
     AKGICVALGH CDATETDIER SAAAGACLAT HLGNGIAATL PRHPNAIWSQ LSDDRLAASL
     ILDGHHLPRS TARAMVRAKG IERTILVSDS VKFAGMPAGR YTSPIGGEVD VGEDGRVSIA
     GTAYLAGSGS CLLDIICRYQ SFTGFPTAEA LTMATTNPAR MIGRNAALAP GAPATFLLLD
     TTEADTAVRP VEILHNGASV LP
//
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