ID   2ENR_CLOTY              Reviewed;          30 AA.
AC   P11887;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   02-JUN-2021, entry version 47.
DE   RecName: Full=2-enoate reductase;
DE            EC=1.3.1.31;
DE   Flags: Fragment;
OS   Clostridium tyrobutyricum.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1519;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=4005048; DOI=10.1515/bchm3.1985.366.1.463;
RA   Kuno S., Bacher A., Simon H.;
RT   "Structure of enoate reductase from a Clostridium tyrobutyricum (C. spec.
RT   La1).";
RL   Biol. Chem. Hoppe-Seyler 366:463-472(1985).
CC   -!- FUNCTION: Involved in fermentation of amino acids (Stickland reaction)
CC       such as leucine, isoleucine, valine and phenylalanine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=butanoate + NAD(+) = (2E)-2-butenoate + H(+) + NADH;
CC         Xref=Rhea:RHEA:10200, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968,
CC         ChEBI:CHEBI:35899, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.31;
CC   -!- COFACTOR:
CC       Name=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC   -!- SUBUNIT: Dodecamer; tetramer of trimers.
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DR   PIR; A22498; A22498.
DR   GO; GO:0047540; F:2-enoate reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Flavoprotein; Iron; Iron-sulfur; Metal-binding;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..>30
FT                   /note="2-enoate reductase"
FT                   /id="PRO_0000064360"
FT   NON_TER         30
SQ   SEQUENCE   30 AA;  3303 MW;  AD96FB5BB2080920 CRC64;
     MKNKSLFEVI KIGKVEVXXK IXMAVMGAFG