ID   LCDC_ANAPI              Reviewed;         259 AA.
AC   G3KIM5;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=Activator of lactoyl-CoA dehydratase;
DE   AltName: Full=Lactoyl-CoA dehydratase component E I;
DE   Flags: Fragment;
GN   Name=lcdC;
OS   Anaerotignum propionicum (Clostridium propionicum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerotignum.
OX   NCBI_TaxID=28446;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2;
RA   Poehlein A., Schlien K., Daniel R., Gottschalk G., Buckel W.;
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION.
RX   PubMed=4055736; DOI=10.1016/s0021-9258(17)38854-3;
RA   Kuchta R.D., Abeles R.H.;
RT   "Lactate reduction in Clostridium propionicum. Purification and properties
RT   of lactyl-CoA dehydratase.";
RL   J. Biol. Chem. 260:13181-13189(1985).
RN   [3]
RP   FUNCTION.
RX   PubMed=1597194; DOI=10.1111/j.1432-1033.1992.tb16958.x;
RA   Hofmeister A.E., Buckel W.;
RT   "(R)-lactyl-CoA dehydratase from Clostridium propionicum. Stereochemistry
RT   of the dehydration of (R)-2-hydroxybutyryl-CoA to crotonyl-CoA.";
RL   Eur. J. Biochem. 206:547-552(1992).
RN   [4]
RP   FUNCTION IN THE ACRYLATE PATHWAY.
RX   PubMed=22810300; DOI=10.1007/s00253-012-4274-y;
RA   Kandasamy V., Vaidyanathan H., Djurdjevic I., Jayamani E.,
RA   Ramachandran K.B., Buckel W., Jayaraman G., Ramalingam S.;
RT   "Engineering Escherichia coli with acrylate pathway genes for propionic
RT   acid synthesis and its impact on mixed-acid fermentation.";
RL   Appl. Microbiol. Biotechnol. 97:1191-1200(2013).
CC   -!- FUNCTION: Required for the activation of lactoyl-CoA dehydratase. This
CC       protein is extremely sensitive towards oxygen.
CC       {ECO:0000269|PubMed:1597194, ECO:0000269|PubMed:22810300,
CC       ECO:0000269|PubMed:4055736}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR   EMBL; JN244653; AEM62995.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3KIM5; -.
DR   SMR; G3KIM5; -.
DR   BioCyc; MetaCyc:EICOMP-MON; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0018819; F:lactoyl-CoA dehydratase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR002731; ATPase_BadF.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR008275; CoA_E_activase.
DR   Pfam; PF01869; BcrAD_BadFG; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
DR   TIGRFAMs; TIGR00241; CoA_E_activ; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding.
FT   CHAIN           <1..259
FT                   /note="Activator of lactoyl-CoA dehydratase"
FT                   /id="PRO_0000419611"
FT   BINDING         125
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   259 AA;  27120 MW;  A179ACE5856C1436 CRC64;
     MYTLGIDVGS ASSKAVILKD GKDIVAAEVV QVGTGSSGPQ RALDKAFEVS GLKKEDISYT
     VATGYGRFNF SDADKQISEI SCHAKGIYFL VPTARTIIDI GGQDAKAIRL DDKGGIKQFF
     MNDKCAAGTG RFLEVMARVL ETTLDEMAEL DEQATDTAPI SSTCTVFAES EVISQLSNGV
     SRNNIIKGVH LSVASRACGL AYRGGLEKDV VMTGGVAKNA GVVRAVAGVL KTDVIVAPNP
     QTTGALGAAL YAYEAAQKK