ID   HVOR_PROVU              Reviewed;          20 AA.
AC   Q9R4Y1;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=2-oxo-acid reductase;
DE            EC=1.1.99.30;
DE   AltName: Full=(2R)-hydroxycarboxylate-viologen-oxidoreductase;
DE            Short=HVOR;
DE   Flags: Fragment;
OS   Proteus vulgaris.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Proteus.
OX   NCBI_TaxID=585;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR
RP   LOCATION, SUBUNIT, AND ACTIVITY REGULATION.
RX   PubMed=8026480; DOI=10.1111/j.1432-1033.1994.tb18954.x;
RA   Trautwein T., Krauss F., Lottspeich F., Simon H.;
RT   "The (2R)-hydroxycarboxylate-viologen-oxidoreductase from Proteus vulgaris
RT   is a molybdenum-containing iron-sulphur protein.";
RL   Eur. J. Biochem. 222:1025-1032(1994).
CC   -!- FUNCTION: Oxidoreductase with an extremely broad substrate specificity
CC       that can reduce reversibly 2-oxocarboxylates to (2R)-
CC       hydroxycarboxylates. {ECO:0000269|PubMed:8026480}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + a (2R)-2-hydroxycarboxylate = a 2-oxocarboxylate + AH2;
CC         Xref=Rhea:RHEA:23664, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:35179, ChEBI:CHEBI:58314; EC=1.1.99.30;
CC         Evidence={ECO:0000269|PubMed:8026480};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000269|PubMed:8026480};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000269|PubMed:8026480};
CC   -!- COFACTOR:
CC       Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC         Evidence={ECO:0000269|PubMed:8026480};
CC       Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC       {ECO:0000269|PubMed:8026480};
CC   -!- ACTIVITY REGULATION: Is inhibited by cyanide. Is sensitive to oxygen.
CC       {ECO:0000269|PubMed:8026480}.
CC   -!- SUBUNIT: Forms various types of homooligomers.
CC       {ECO:0000269|PubMed:8026480}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8026480}.
CC   -!- SIMILARITY: Belongs to the AOR/FOR family. {ECO:0000305}.
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DR   PIR; S45637; S45637.
DR   AlphaFoldDB; Q9R4Y1; -.
DR   STRING; 585.DR95_1848; -.
DR   eggNOG; COG2414; Bacteria.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0033719; F:2-oxo-acid reductase activity; IDA:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR   GO; GO:0030151; F:molybdenum ion binding; IDA:UniProtKB.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   4Fe-4S; Cell membrane; Direct protein sequencing; Iron; Iron-sulfur;
KW   Membrane; Metal-binding; Molybdenum; Oxidoreductase.
FT   CHAIN           1..>20
FT                   /note="2-oxo-acid reductase"
FT                   /id="PRO_0000408495"
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2146 MW;  D12A6CFC51207C63 CRC64;
     MINGWTGNIL RINLTTGAIS