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
//