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
//