HADI_CLODI
ID HADI_CLODI Reviewed; 266 AA.
AC Q5U925;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=2-hydroxyisocaproyl-CoA dehydratase activator {ECO:0000303|PubMed:15654892};
DE EC=3.-.-.- {ECO:0000305};
GN Name=hadI {ECO:0000303|PubMed:15654892}; Synonyms=fldI_1, lcdC;
GN ORFNames=BN1095_530010, BN1096_180047, BN1097_160049, CD630DERM_03960,
GN ERS445050_03311, PCZ31_0395;
OS Clostridioides difficile (Peptoclostridium difficile).
OG Plasmid 2.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=1496;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND COFACTOR.
RC STRAIN=DSMZ 1296;
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 Clostridium
RT difficile.";
RL FEBS J. 272:550-561(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Monot M.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13307;
RG Pathogen Informatics;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z31;
RA Pereira F.L., Oliveira Junior C.A., Silva R.O.S., Dorela F.A.,
RA Carvalho A.F., Almeida G.M.F., Leal C.A.G., Lobato F.C.F.,
RA Figueiredo H.C.P.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH ATP; ATP ANALOG AND
RP IRON-SULFUR (4FE-4S), FUNCTION, COFACTOR, SUBUNIT, AND REACTION MECHANISM.
RC PLASMID=2;
RX PubMed=22827463; DOI=10.1021/bi300571z;
RA Knauer S.H., Buckel W., Dobbek H.;
RT "On the ATP-dependent activation of the radical enzyme (R)-2-
RT hydroxyisocaproyl-CoA dehydratase.";
RL Biochemistry 51:6609-6622(2012).
CC -!- FUNCTION: Involved in the reductive branch of L-leucine fermentation.
CC Required for the activation of (R)-2-hydroxyisocaproyl-CoA dehydratase.
CC The reduced activator transfers one electron to the dehydratase
CC concomitant with hydrolysis of ATP. This protein is extremely sensitive
CC towards oxygen. {ECO:0000269|PubMed:15654892,
CC ECO:0000269|PubMed:22827463}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:15654892, ECO:0000269|PubMed:22827463};
CC Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000269|PubMed:15654892,
CC ECO:0000269|PubMed:22827463};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22827463}.
CC -!- MISCELLANEOUS: Only in the reduced state, HadI exhibits significant
CC ATPase activity, which appears to be essential for unidirectional
CC electron transfer. {ECO:0000269|PubMed:22827463}.
CC -!- SIMILARITY: Belongs to the HadI activator family. {ECO:0000305}.
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DR EMBL; AY772815; AAV40818.1; -; Genomic_DNA.
DR EMBL; LK932467; CDS83472.1; -; Genomic_DNA.
DR EMBL; LK932350; CDS83578.1; -; Genomic_DNA.
DR EMBL; LK933216; CDT50868.1; -; Genomic_DNA.
DR EMBL; LN614756; CEJ96914.1; -; Genomic_DNA.
DR EMBL; LN831031; CKH72430.1; -; Genomic_DNA.
DR EMBL; CP013196; ALP02349.1; -; Genomic_DNA.
DR RefSeq; WP_009888223.1; NZ_WUUI01000021.1.
DR PDB; 4EHT; X-ray; 1.95 A; A/B=1-266.
DR PDB; 4EHU; X-ray; 1.60 A; A/B=1-266.
DR PDB; 4EIA; X-ray; 3.00 A; A=1-266.
DR PDBsum; 4EHT; -.
DR PDBsum; 4EHU; -.
DR PDBsum; 4EIA; -.
DR AlphaFoldDB; Q5U925; -.
DR SMR; Q5U925; -.
DR GeneID; 66352921; -.
DR KEGG; pdf:CD630DERM_03960; -.
DR BioCyc; MetaCyc:MON-20613; -.
DR BRENDA; 4.2.1.157; 1473.
DR BRENDA; 5.6.1.9; 1473.
DR SABIO-RK; Q5U925; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase 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; 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 3D-structure; 4Fe-4S; ATP-binding; Hydrolase; Iron; Iron-sulfur;
KW Metal-binding; Nucleotide-binding; Plasmid.
FT CHAIN 1..266
FT /note="2-hydroxyisocaproyl-CoA dehydratase activator"
FT /id="PRO_0000435664"
FT BINDING 10..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22827463"
FT BINDING 102..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22827463"
FT BINDING 125
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:22827463"
FT BINDING 134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22827463"
FT BINDING 164
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:22827463"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22827463"
FT BINDING 241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22827463"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:4EHU"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:4EHU"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:4EHU"
FT STRAND 23..31
FT /evidence="ECO:0007829|PDB:4EHU"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:4EHT"
FT HELIX 38..50
FT /evidence="ECO:0007829|PDB:4EHU"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:4EHU"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:4EHU"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:4EHU"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:4EHU"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:4EHU"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:4EHU"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:4EHU"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:4EHU"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:4EHU"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:4EHU"
FT HELIX 147..151
FT /evidence="ECO:0007829|PDB:4EHU"
FT HELIX 165..177
FT /evidence="ECO:0007829|PDB:4EHU"
FT HELIX 182..204
FT /evidence="ECO:0007829|PDB:4EHU"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:4EHU"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:4EHU"
FT HELIX 220..230
FT /evidence="ECO:0007829|PDB:4EHU"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:4EHU"
FT HELIX 243..261
FT /evidence="ECO:0007829|PDB:4EHU"
SQ SEQUENCE 266 AA; 28423 MW; 7D763B2C5C5A24EE CRC64;
MYTMGLDIGS TASKGVILKN GEDIVASETI SSGTGTTGPS RVLEKLYGKT GLAREDIKKV
VVTGYGRMNY SDADKQISEL SCHARGVNFI IPETRTIIDI GGQDAKVLKL DNNGRLLNFL
MNDKCAAGTG RFLDVMAKII EVDVSELGSI SMNSQNEVSI SSTCTVFAES EVISHLSENA
KIEDIVAGIH TSVAKRVSSL VKRIGVQRNV VMVGGVARNS GIVRAMAREI NTEIIVPDIP
QLTGALGAAL YAFDEAKESQ KEVKNI
