ID   LCDA_ANAPI              Reviewed;         422 AA.
AC   G3KIM4;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=Lactoyl-CoA dehydratase subunit alpha;
DE            EC=4.2.1.54;
DE   AltName: Full=(R)-lactyl-CoA dehydratase component E II;
DE   AltName: Full=2-hydroxybutyroyl-CoA dehydratase;
DE   Flags: Fragment;
GN   Name=lcdA;
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, COFACTOR, ACTIVITY REGULATION, AND SUBUNIT.
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, COFACTOR, ACTIVITY REGULATION, AND SUBUNIT.
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: Involved in the acrylate pathway for the conversion of D-
CC       lactic acid to propionic acid. Catalyzes the reversible dehydration of
CC       Lactoyl-CoA and 2-hydroxybutyroyl-CoA to acryloyl-CoA and crotonyl-CoA,
CC       respectively. {ECO:0000269|PubMed:1597194, ECO:0000269|PubMed:22810300,
CC       ECO:0000269|PubMed:4055736}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-lactoyl-CoA = acryloyl-CoA + H2O; Xref=Rhea:RHEA:34691,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57367, ChEBI:CHEBI:70980; EC=4.2.1.54;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-hydroxybutanoyl-CoA = (2E)-butenoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:47176, ChEBI:CHEBI:15377, ChEBI:CHEBI:57332,
CC         ChEBI:CHEBI:87474;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 1 [4Fe-4S] cluster.;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC   -!- COFACTOR:
CC       Name=riboflavin; Xref=ChEBI:CHEBI:57986;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- ACTIVITY REGULATION: Activated by the LcdC protein.
CC       {ECO:0000269|PubMed:1597194, ECO:0000269|PubMed:4055736}.
CC   -!- SUBUNIT: Heterodimer of an alpha (LcdA) and a beta (LcdB) subunit.
CC       {ECO:0000269|PubMed:1597194, ECO:0000269|PubMed:4055736}.
CC   -!- MISCELLANEOUS: The elimination of water from 2-hydroxybutyryl-CoA or
CC       lactoyl-CoA occurs in a syn mode.
CC   -!- SIMILARITY: Belongs to the FldB/FldC dehydratase alpha/beta subunit
CC       family. {ECO:0000305}.
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DR   EMBL; JN244652; AEM62994.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3KIM4; -.
DR   SMR; G3KIM4; -.
DR   KEGG; ag:AEM62994; -.
DR   BioCyc; MetaCyc:ALPHALAC-MON; -.
DR   BRENDA; 4.2.1.54; 1504.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0018819; F:lactoyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR010327; FldB/FldC_alpha/beta.
DR   Pfam; PF06050; HGD-D; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Flavoprotein; FMN; Iron; Iron-sulfur; Lyase; Metal-binding.
FT   CHAIN           <1..422
FT                   /note="Lactoyl-CoA dehydratase subunit alpha"
FT                   /id="PRO_0000419609"
FT   NON_TER         1
SQ   SEQUENCE   422 AA;  47390 MW;  69E4D23F1CCCE42C CRC64;
     MSLTQGMKAK QLLAYFQGKA DQDAREAKAR GELVCWSASV APPEFCVTMG IAMIYPETHA
     AGIGARKGAM DMLEVADRKG YNVDCCSYGR VNMGYMECLK EAAITGVKPE VLVNSPAADV
     PLPDLVITCN NICNTLLKWY ENLAAELDIP CIVIDVPFNH TMPIPEYAKA YIADQFRNAI
     SQLEVICGRP FDWKKFKEVK DQTQRSVYHW NRIAEMAKYK PSPLNGFDLF NYMALIVACR
     SLDYAEITFK AFADELEENL KAGIYAFKGA EKTRFQWEGI AVWPHLGHTF KSMKNLNSIM
     TGTAYPALWD LHYDANDESM HSMAEAYTRI YINTCLQNKV EVLLGIMEKG QVDGTVYHLN
     RSCKLMSFLN VETAEIIKEK NGLPYVSIDG DQTDPRVFSP AQFDTRVQAL VEMMEANMAA
     AE