ID   A0A1G8CZQ0_9ACTN        Unreviewed;       379 AA.
AC   A0A1G8CZQ0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000313|EMBL:SDH50998.1};
GN   ORFNames=SAMN05421505_11745 {ECO:0000313|EMBL:SDH50998.1};
OS   Sinosporangium album.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Sinosporangium.
OX   NCBI_TaxID=504805 {ECO:0000313|EMBL:SDH50998.1, ECO:0000313|Proteomes:UP000198923};
RN   [1] {ECO:0000313|EMBL:SDH50998.1, ECO:0000313|Proteomes:UP000198923}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CPCC 201354 {ECO:0000313|EMBL:SDH50998.1,
RC   ECO:0000313|Proteomes:UP000198923};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FNCN01000017; SDH50998.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8CZQ0; -.
DR   STRING; 504805.SAMN05421505_11745; -.
DR   OrthoDB; 9776488at2; -.
DR   Proteomes; UP000198923; 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}; Hydrolase {ECO:0000256|PIRNR:PIRNR038994};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR038994-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198923}.
FT   DOMAIN          47..374
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   ACT_SITE        267
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         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         188
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT   BINDING         209
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT   BINDING         212..213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         301..303
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
SQ   SEQUENCE   379 AA;  39075 MW;  A6BD3BDAEA8731E8 CRC64;
     MSITLADARI VTTDGVHEGW LTIEDGRITH IGHGSAPGNG YRLSGRYVVP GFVDIHNHGG
     AGGSFPTGDQ EQAGKAVAFH TAHGTTTLIA SLVSGPTAAL TEAASSLAEL CEEGLLAGIH
     YEGPYISTRR CGAHDLAQLR SPEPAEVEQL IKAGRGHIRM LTIAPELPGA LDAIRTLASH
     GIIAALGHTD ATLDQTLAGV DAGATVATHL YNAMAPLHHR DPGPIAALLQ DERVTVELIN
     DGVHVHPAMM RLAFDAAGAS RTALITDAMT AAGMGDGRYD LGDMGVTVEG GVARLIEGGA
     IAGSTLTMDV AFRRSVREVG LSLTEAAVIA SLTPATVLGQ ADRIGSIAVG KQADLVILTD
     DLQVSGVMKR GSWVTEPTA
//