ID   LCDB_ANAPI              Reviewed;         374 AA.
AC   G3KIM3;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Lactoyl-CoA dehydratase subunit beta;
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=lcdB;
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, 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, 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   -!- 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; JN244651; AEM62993.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3KIM3; -.
DR   SMR; G3KIM3; -.
DR   KEGG; ag:AEM62993; -.
DR   BioCyc; MetaCyc:BETALAC-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; 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..374
FT                   /note="Lactoyl-CoA dehydratase subunit beta"
FT                   /id="PRO_0000419610"
FT   NON_TER         1
SQ   SEQUENCE   374 AA;  41810 MW;  F62729DFEEBC5FD2 CRC64;
     MSRVEAILSQ LKDVAANPKK AMDDYKAETG KGAVGIMPIY SPEEMVHAAG YLPMGIWGAQ
     GKTISKARTY LPAFACSVMQ QVMELQCEGA YDDLSAVIFS VPCDTLKCLS QKWKGTSPVI
     VFTHPQNRGL EAANQFLVTE YELVKAQLES VLGVKISNAA LENSIAIYNE NRAVMREFVK
     VAADYPQVID AVSRHAVFKA RQFMLKEKHT ALVKELIAEI KATPVQPWDG KKVVVTGILL
     EPNELLDIFN EFKIAIVDDD LAQESRQIRV DVLDGEGGPL YRMAKAWQQM YGCSLATDTK
     KGRGRMLINK TIQTGADAIV VAMMKFCDPE EWDYPVMYRE FEEKGVKSLM IEVDQEVSSF
     EQIKTRLQSF VEML