ID HADB_PEPDI Reviewed; 408 AA. AC Q5U924; DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 1. DT 13-APR-2016, entry version 44. DE RecName: Full=(R)-2-hydroxyisocaproyl-CoA dehydratase alpha subunit {ECO:0000303|PubMed:15654892}; DE EC=4.2.1.157 {ECO:0000269|PubMed:15654892}; GN Name=hadB {ECO:0000303|PubMed:15654892}; GN ORFNames=CD630DERM_03970, ERS445050_03310; OS Peptoclostridium difficile (Clostridium difficile). OG Plasmid 2. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=1496; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION, RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, RP COFACTOR, SUBUNIT, AND REACTION MECHANISM. RX PubMed=15654892; DOI=10.1111/j.1742-4658.2004.04498.x; RA Kim J., Darley D., Buckel W.; RT "2-hydroxyisocaproyl-CoA dehydratase and its activator from RT Clostridium difficile."; RL FEBS J. 272:550-561(2005). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=630Derm; RA Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A., RA Brescovit A.D., Santos A.J.; RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases. RN [3] RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR RP (4FE-4S) AND SUBSTRATE ANALOG, FUNCTION, COFACTOR, SUBUNIT, AND RP REACTION MECHANISM. RC PLASMID=2; RX PubMed=21366233; DOI=10.1021/ja1076537; RA Knauer S.H., Buckel W., Dobbek H.; RT "Structural basis for reductive radical formation and electron RT recycling in (R)-2-hydroxyisocaproyl-CoA dehydratase."; RL J. Am. Chem. Soc. 133:4342-4347(2011). CC -!- FUNCTION: Involved in the reductive branch of L-leucine CC fermentation. Catalyzes the irreversible beta/alpha-elimination of CC water from (R)-2-hydroxyisocaproyl-CoA to yield isocaprenoyl-CoA. CC This beta/alpha-dehydration depends on the reductive formation of CC ketyl radicals on the substrate generated by injection of a single CC electron from the ATP-dependent activator protein HadI. The enzyme CC is specific for the R-isomer. {ECO:0000269|PubMed:15654892, CC ECO:0000269|PubMed:21366233}. CC -!- CATALYTIC ACTIVITY: (R)-2-hydroxy-4-methylpentanoyl-CoA = 4- CC methylpent-2-enoyl-CoA + H(2)O. {ECO:0000269|PubMed:15654892}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000269|PubMed:15654892, CC ECO:0000269|PubMed:21366233}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:15654892, CC ECO:0000269|PubMed:21366233}; CC -!- ENZYME REGULATION: Activated by HadI. CC {ECO:0000269|PubMed:15654892}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.05 mM for (R)-2-hydroxyisocaproyl-CoA CC {ECO:0000269|PubMed:15654892}; CC -!- SUBUNIT: Part of the heterodimeric complex HadBC composed of (R)- CC 2-hydroxyisocaproyl-CoA dehydratase alpha (HadB) and beta (HadC) CC subunit. {ECO:0000269|PubMed:15654892, CC ECO:0000269|PubMed:21366233}. CC -!- SIMILARITY: Belongs to the FldB/FldC dehydratase alpha subunit CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY772816; AAV40819.1; -; Genomic_DNA. DR EMBL; LN614756; CEJ96915.1; -; Genomic_DNA. DR EMBL; LN831031; CKH72398.1; -; Genomic_DNA. DR PDB; 3O3M; X-ray; 1.82 A; A/C=1-408. DR PDB; 3O3N; X-ray; 2.30 A; A/C=1-408. DR PDB; 3O3O; X-ray; 2.00 A; A=1-408. DR PDBsum; 3O3M; -. DR PDBsum; 3O3N; -. DR PDBsum; 3O3O; -. DR STRING; 272563.CD0397; -. DR KEGG; pdf:CD630DERM_03970; -. DR eggNOG; ENOG4105CMH; Bacteria. DR eggNOG; COG1775; LUCA. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB. DR GO; GO:0016836; F:hydro-lyase activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006551; P:leucine metabolic process; IDA:UniProtKB. DR InterPro; IPR010327; FldB/FldC_alpha/beta. DR Pfam; PF06050; HGD-D; 1. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; KW Lyase; Metal-binding; Plasmid. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:15654892}. FT CHAIN 2 408 (R)-2-hydroxyisocaproyl-CoA dehydratase FT alpha subunit. FT /FTId=PRO_0000435662. FT METAL 84 84 Iron-sulfur (4Fe-4S). FT {ECO:0000269|PubMed:21366233}. FT METAL 117 117 Iron-sulfur (4Fe-4S). FT {ECO:0000269|PubMed:21366233}. FT METAL 346 346 Iron-sulfur (4Fe-4S). FT {ECO:0000269|PubMed:21366233}. FT BINDING 55 55 Substrate. {ECO:0000269|PubMed:21366233}. SQ SEQUENCE 408 AA; 46334 MW; 702A372CB6796AB5 CRC64; MSEKKEARVV INDLLAEQYA NAFKAKEEGR PVGWSTSVFP QELAEVFDLN VLYPENQAAG VAAKKGSLEL CEIAESKGYS IDLCAYARTN FGLLENGGCE ALDMPAPDFL LCCNNICNQV IKWYENISRE LDIPLIMIDT TFNNEDEVTQ SRIDYIKAQF EEAIKQLEII SGKKFDPKKF EEVMKISAEN GRLWKYSMSL PADSSPSPMN GFDLFTYMAV IVCARGKKET TEAFKLLIEE LEDNMKTGKS SFRGEEKYRI MMEGIPCWPY IGYKMKTLAK FGVNMTGSVY PHAWALQYEV NDLDGMAVAY STMFNNVNLD RMTKYRVDSL VEGKCDGAFY HMNRSCKLMS LIQYEMQRRA AEETGLPYAG FDGDQADPRA FTNAQFETRI QGLVEVMEER KKLNRGEI //