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Y529_GEOTN
ID   Y529_GEOTN              Reviewed;         178 AA.
AC   A4IKQ7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Putative metal-dependent hydrolase GTNG_0529 {ECO:0000255|HAMAP-Rule:MF_01256};
DE            EC=3.-.-.- {ECO:0000255|HAMAP-Rule:MF_01256};
GN   OrderedLocusNames=GTNG_0529;
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=420246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2;
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
CC   -!- FUNCTION: Possible metal-dependent hydrolase. {ECO:0000255|HAMAP-
CC       Rule:MF_01256}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01256};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01256};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01256}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01256}.
CC   -!- SIMILARITY: Belongs to the metal hydrolase YfiT family.
CC       {ECO:0000255|HAMAP-Rule:MF_01256}.
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DR   EMBL; CP000557; ABO65911.1; -; Genomic_DNA.
DR   RefSeq; WP_011886844.1; NC_009328.1.
DR   AlphaFoldDB; A4IKQ7; -.
DR   SMR; A4IKQ7; -.
DR   STRING; 420246.GTNG_0529; -.
DR   EnsemblBacteria; ABO65911; ABO65911; GTNG_0529.
DR   KEGG; gtn:GTNG_0529; -.
DR   eggNOG; COG2318; Bacteria.
DR   HOGENOM; CLU_105789_1_0_9; -.
DR   OMA; GWTIRQV; -.
DR   OrthoDB; 1812981at2; -.
DR   Proteomes; UP000001578; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.450; -; 1.
DR   HAMAP; MF_01256; YfiT_hydrol; 1.
DR   InterPro; IPR024775; DinB-like.
DR   InterPro; IPR034660; DinB/YfiT-like.
DR   InterPro; IPR023774; Put_metal_dep_hydrolase_YfiT.
DR   Pfam; PF12867; DinB_2; 1.
DR   SUPFAM; SSF109854; SSF109854; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..178
FT                   /note="Putative metal-dependent hydrolase GTNG_0529"
FT                   /id="PRO_1000067244"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01256"
FT   BINDING         161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01256"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01256"
SQ   SEQUENCE   178 AA;  20150 MW;  57EFB94D34298923 CRC64;
     MSTIDPIRYP IGTFQAPAQF RAEDVKEWIA AIRELPDALR AAVAGLNDEQ LNTPYRDGGW
     TVAQVVHHLA DASMNAFLRT KWGLTEDKPA IKPFEESEWA KTADARSLPI EPSLMLLEGL
     HVRWATLLES MTEADFQRLI CPEGAKQAMP LYVLTALYTW HGKHHTAQIM SLRKRKGW
 
 
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