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Database: UniProt
Entry: A0A069CUY2_WEIOS
LinkDB: A0A069CUY2_WEIOS
Original site: A0A069CUY2_WEIOS 
ID   A0A069CUY2_WEIOS        Unreviewed;       390 AA.
AC   A0A069CUY2;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=N-acetylglucosamine-6-phosphate deacetylase {ECO:0000313|EMBL:GAK31625.1};
GN   ORFNames=WOSG25_120160 {ECO:0000313|EMBL:GAK31625.1};
OS   Weissella oryzae (strain DSM 25784 / JCM 18191 / LMG 30913 / SG25).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; Weissella.
OX   NCBI_TaxID=1329250 {ECO:0000313|EMBL:GAK31625.1, ECO:0000313|Proteomes:UP000030643};
RN   [1] {ECO:0000313|Proteomes:UP000030643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25784 / JCM 18191 / LMG 30913 / SG25
RC   {ECO:0000313|Proteomes:UP000030643};
RX   PubMed=25013139; DOI=10.1128/genomea.00667-14;
RA   Tanizawa Y., Fujisawa T., Mochizuki T., Kaminuma E., Suzuki Y.,
RA   Nakamura Y., Tohno M.;
RT   "Draft genome sequence of Weissella oryzae SG25T, isolated from fermented
RT   rice grains.";
RL   Genome Announc. 2:0-0(2014).
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}.
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DR   EMBL; DF820495; GAK31625.1; -; Genomic_DNA.
DR   RefSeq; WP_027699579.1; NZ_DF820495.1.
DR   AlphaFoldDB; A0A069CUY2; -.
DR   STRING; 1329250.WOSG25_120160; -.
DR   eggNOG; COG1820; Bacteria.
DR   OrthoDB; 9776488at2; -.
DR   Proteomes; UP000030643; 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:UP000030643}.
FT   DOMAIN          55..368
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   ACT_SITE        275
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-1"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-3"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         198
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"
FT   BINDING         220..221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
FT   BINDING         308..310
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038994-2"
SQ   SEQUENCE   390 AA;  42405 MW;  1BB5A5680C7F58AE CRC64;
     MTTVLTHATF YTGEADPAVI KDGYVRFNQQ IEAIGTMADY VPAAGDEVIN LTGKVIVPGF
     IDVHTHGAYG FDTMDGNQDD LVKMVRSQIT EGITTVFPTT MTQSTESISQ AMRAINAAAA
     EEPAIVGVHL EGPFVSPHYK GAQPEQYIIA PSADLVAQWN ELSGNRVRLI TYAPEEADDL
     AGFEEYLLAH NIIGSIGHSN ASREFLQNNS KANHITHLYN AQRPMKHRDP GVTGHAMLED
     SIRTELIVDG FHVAPDMVKL AYKLKSAKRI DLITDSMRAK GLGDGVSELG GQTVYVKDKQ
     ARLEDGTLAG SVLEFDDAFR NIINFTGASI QEAVEMAAVN QAVEFGLTQK GTLRIGKDAD
     MNVFDGNLSL LATYSMGRHF SKQDLVIKEA
//
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