ID   A0A1Y4TH47_9FIRM        Unreviewed;       385 AA.
AC   A0A1Y4TH47;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000313|EMBL:OUQ41568.1};
GN   ORFNames=B5E65_11640 {ECO:0000313|EMBL:OUQ41568.1};
OS   Gemmiger sp. An120.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Gemmiger.
OX   NCBI_TaxID=1965549 {ECO:0000313|EMBL:OUQ41568.1, ECO:0000313|Proteomes:UP000195783};
RN   [1] {ECO:0000313|Proteomes:UP000195783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An120 {ECO:0000313|Proteomes:UP000195783};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
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|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:OUQ41568.1}.
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; NFLN01000014; OUQ41568.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4TH47; -.
DR   OrthoDB; 9776488at2; -.
DR   Proteomes; UP000195783; 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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR038994};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR038994-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195783}.
FT   DOMAIN          51..381
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   ACT_SITE        274
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-1"
FT   BINDING         130
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT   BINDING         196
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT   BINDING         217
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
SQ   SEQUENCE   385 AA;  40274 MW;  722FF7979DA82D07 CRC64;
     MNNTWLIRGG TVCTPDGMQQ ADLLVDNGCI TAVGEGLTAP GAQEVDATGL LVMPGFIDIH
     THGAVGVDMN GADKEGLAKV SAFFASQGVT GFLPTLLTDS HEALLQYVHT IGMAAPEITD
     GAAVLGIHME GPYLCAEYKG AMPEHLLQTP DFSKFMQYQK ASGGRIRRMT VSPEVEGVSH
     FIPKAVAEGV SISIGHSGAD YDTAWEAIRS GAACATHTFN AMKLLHQHFP AISGAVLESD
     IYAEAICDGI HLHPGTVRIL LKAKGLDRVI AITDSIMAAG LGDGRFKLGV NDVIVKNGDA
     ILADGGSRAG STLTMSRAFA NLRRFTGLPA FELAKLLSAN PADLLGLGGR KGRILPGYDA
     DLTLITDEGA VSATFVEGRQ VYSAG
//