ID Q5U924_PEPDI Unreviewed; 408 AA. AC Q5U924; DT 07-DEC-2004, integrated into UniProtKB/TrEMBL. DT 07-DEC-2004, sequence version 1. DT 17-FEB-2016, entry version 42. DE SubName: Full=2-hydroxyisocaproyl-CoA dehydratase {ECO:0000313|EMBL:AAV40819.1}; DE SubName: Full=Subunit of oxygen-sensitive 2-hydroxyisocaproyl-CoA dehydratase {ECO:0000313|EMBL:CKH72398.1}; DE EC=4.2.1.- {ECO:0000313|EMBL:CKH72398.1}; DE SubName: Full=Subunit of oxygen-sensitive2-hydroxyisocaproyl-CoA dehydratase B {ECO:0000313|EMBL:CEJ96915.1}; GN Name=hadB {ECO:0000313|EMBL:AAV40819.1}; GN ORFNames=CD630DERM_03970 {ECO:0000313|EMBL:CEJ96915.1}, GN ERS445050_03310 {ECO:0000313|EMBL:CKH72398.1}; OS Peptoclostridium difficile (Clostridium difficile). OG Plasmid 2 {ECO:0000313|EMBL:CKH72398.1}. OC Bacteria; Firmicutes; Clostridia; Clostridiales; OC Peptostreptococcaceae; Peptoclostridium. OX NCBI_TaxID=1496 {ECO:0000313|EMBL:AAV40819.1, ECO:0000313|Proteomes:UP000032805}; RN [1] {ECO:0000213|PDB:3O3M, ECO:0000213|PDB:3O3N, ECO:0000213|PDB:3O3O} RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR RP (4FE-4S). RC PLASMID=2 {ECO:0000313|EMBL:CKH72398.1}; 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). RN [2] {ECO:0000313|EMBL:CEJ96915.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=630Derm {ECO:0000313|EMBL:CEJ96915.1}; 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. 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; COG1775; LUCA. DR eggNOG; ENOG4105CMH; Bacteria. DR Proteomes; UP000032805; Chromosome 1. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. 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 3D-structure {ECO:0000213|PDB:3O3M, ECO:0000213|PDB:3O3N, KW ECO:0000213|PDB:3O3O}; KW 4Fe-4S {ECO:0000213|PDB:3O3M, ECO:0000213|PDB:3O3N, KW ECO:0000213|PDB:3O3O}; KW Complete proteome {ECO:0000313|Proteomes:UP000032805}; KW Iron {ECO:0000213|PDB:3O3M, ECO:0000213|PDB:3O3N, KW ECO:0000213|PDB:3O3O}; KW Iron-sulfur {ECO:0000213|PDB:3O3M, ECO:0000213|PDB:3O3N, KW ECO:0000213|PDB:3O3O}; Lyase {ECO:0000313|EMBL:CKH72398.1}; KW Metal-binding {ECO:0000213|PDB:3O3M, ECO:0000213|PDB:3O3N, KW ECO:0000213|PDB:3O3O}; Plasmid {ECO:0000313|EMBL:CKH72398.1}. FT METAL 84 84 Iron-sulfur (4Fe-4S). {ECO:0000213|PDB: FT 3O3M, ECO:0000213|PDB:3O3N, FT ECO:0000213|PDB:3O3O}. FT METAL 117 117 Iron-sulfur (4Fe-4S). {ECO:0000213|PDB: FT 3O3M, ECO:0000213|PDB:3O3N, FT ECO:0000213|PDB:3O3O}. FT METAL 346 346 Iron-sulfur (4Fe-4S). {ECO:0000213|PDB: FT 3O3M, ECO:0000213|PDB:3O3N, FT ECO:0000213|PDB:3O3O}. 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 //