ID   Y2135_AQUAE             Reviewed;         211 AA.
AC   O67893;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Uncharacterized protein aq_2135;
DE            EC=3.-.-.-;
GN   OrderedLocusNames=aq_2135;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q16775};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q16775};
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC       Glyoxalase II family. {ECO:0000305}.
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DR   EMBL; AE000657; AAC07862.1; -; Genomic_DNA.
DR   PIR; A70483; A70483.
DR   RefSeq; NP_214462.1; NC_000918.1.
DR   RefSeq; WP_010881398.1; NC_000918.1.
DR   AlphaFoldDB; O67893; -.
DR   SMR; O67893; -.
DR   STRING; 224324.aq_2135; -.
DR   EnsemblBacteria; AAC07862; AAC07862; aq_2135.
DR   KEGG; aae:aq_2135; -.
DR   eggNOG; COG0491; Bacteria.
DR   HOGENOM; CLU_030571_5_3_0; -.
DR   InParanoid; O67893; -.
DR   OMA; GAWGTNC; -.
DR   OrthoDB; 1581636at2; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.15.10; -; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SUPFAM; SSF56281; SSF56281; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..211
FT                   /note="Uncharacterized protein aq_2135"
FT                   /id="PRO_0000192359"
FT   BINDING         54
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q16775"
FT   BINDING         56
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q16775"
FT   BINDING         58
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q16775"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q16775"
FT   BINDING         129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q16775"
FT   BINDING         148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q16775"
FT   BINDING         148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q16775"
FT   BINDING         189
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q16775"
SQ   SEQUENCE   211 AA;  22959 MW;  A6F3368FD665A68B CRC64;
     MIIKVIPVGP IAVNCSVVAD EKSGEAIIID PGAEAEKILE AVKDFKVVGI VATHGHIDHV
     GQVGKLKELF DVPFYMNPLD KFLINDEIWS GFASYIGAVP CPEPDVEISE GDVIRVGDVE
     FKVLHTPGHT PGLCCLYEEK RRVLIAGDLL FKGSVGRWDL PGGNLVELKK SVKRVLTELP
     QDTLVICGHY DETTIGQERA FNPFAGELLN G