HDVD_CLOAM
ID HDVD_CLOAM Reviewed; 490 AA.
AC P55792; Q9RM87;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 3.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=4-hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA-Delta-isomerase;
DE Short=4-BUDH;
DE EC=4.2.1.120;
DE EC=5.3.3.3;
DE AltName: Full=Gamma-aminobutyrate metabolism dehydratase/isomerase;
GN Name=abfD;
OS Clostridium aminobutyricum.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=33953;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13726 / DSM 2634;
RX PubMed=11041350; DOI=10.1007/s002030000195;
RA Gerhardt A., Cinkaya I., Linder D., Huisman G., Buckel W.;
RT "Fermentation of 4-aminobutyrate by Clostridium aminobutyricum: cloning of
RT two genes involved in the formation and dehydration of 4-hydroxybutyryl-
RT CoA.";
RL Arch. Microbiol. 174:189-199(2000).
RN [2]
RP SEQUENCE REVISION TO 43; 167 AND 357.
RA Zhang J.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 1-30, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND REACTION MECHANISM.
RC STRAIN=ATCC 13726 / DSM 2634;
RX PubMed=8344309; DOI=10.1111/j.1432-1033.1993.tb18049.x;
RA Scherf U., Buckel W.;
RT "Purification and properties of an iron-sulfur and FAD-containing 4-
RT hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA delta 3-delta 2-isomerase
RT from Clostridium aminobutyricum.";
RL Eur. J. Biochem. 215:421-429(1993).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR AND FAD,
RP COFACTOR, AND REACTION MECHANISM.
RX PubMed=15496473; DOI=10.1073/pnas.0403952101;
RA Martins B.M., Dobbek H., Cinkaya I., Buckel W., Messerschmidt A.;
RT "Crystal structure of 4-hydroxybutyryl-CoA dehydratase: radical catalysis
RT involving a [4Fe-4S] cluster and flavin.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15645-15649(2004).
CC -!- FUNCTION: Catalyzes the reversible conversion of 4-hydroxybutyryl-CoA
CC to crotonyl-CoA. The mechanism of the reaction seems to go through
CC three steps: (1) the FAD-dependent oxidation of 4-hydroxybutyryl-CoA to
CC 4-hydroxycrotonyl-CoA; (2) the hydroxyl group is substituted by a
CC hydride derived from the now reduced FAD in an SN2' reaction leading to
CC vinylacetyl-CoA; (3) isomerization to yield crotonyl-CoA.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybutanoyl-CoA = (2E)-butenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:26530, ChEBI:CHEBI:15377, ChEBI:CHEBI:57332,
CC ChEBI:CHEBI:58574; EC=4.2.1.120;
CC Evidence={ECO:0000269|PubMed:8344309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=vinylacetyl-CoA = (2E)-butenoyl-CoA; Xref=Rhea:RHEA:10572,
CC ChEBI:CHEBI:57332, ChEBI:CHEBI:57396; EC=5.3.3.3;
CC Evidence={ECO:0000269|PubMed:8344309};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per subunit.;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for 4-hydroxybutanoyl-CoA {ECO:0000269|PubMed:8344309};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15496473,
CC ECO:0000269|PubMed:8344309}.
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DR EMBL; AJ250267; CAB60035.2; -; Genomic_DNA.
DR PIR; S34765; S34765.
DR PDB; 1U8V; X-ray; 1.60 A; A/B/C/D=1-490.
DR PDBsum; 1U8V; -.
DR AlphaFoldDB; P55792; -.
DR SMR; P55792; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR PRIDE; P55792; -.
DR KEGG; ag:CAB60035; -.
DR BioCyc; MetaCyc:MON-13485; -.
DR BRENDA; 4.2.1.120; 1455.
DR EvolutionaryTrace; P55792; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0043721; F:4-hydroxybutanoyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0050393; F:vinylacetyl-CoA delta-isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR InterPro; IPR004925; HpaB/PvcC/4-BUDH.
DR InterPro; IPR024719; HpaB/PvcC/4-BUDH_C.
DR InterPro; IPR024674; HpaB/PvcC/4-BUDH_N.
DR PANTHER; PTHR36117; PTHR36117; 1.
DR Pfam; PF03241; HpaB; 1.
DR Pfam; PF11794; HpaB_N; 1.
DR PIRSF; PIRSF000331; HpaA_HpaB; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Direct protein sequencing; FAD; Flavoprotein; Iron;
KW Iron-sulfur; Isomerase; Lyase; Metal-binding; Multifunctional enzyme;
KW Oxidoreductase.
FT CHAIN 1..490
FT /note="4-hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA-
FT Delta-isomerase"
FT /id="PRO_0000083940"
FT BINDING 99
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:15496473"
FT BINDING 103
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:15496473"
FT BINDING 149..156
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15496473"
FT BINDING 188..190
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15496473"
FT BINDING 292
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:15496473"
FT BINDING 299
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:15496473"
FT BINDING 325
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15496473"
FT BINDING 386..390
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:15496473"
FT HELIX 5..12
FT /evidence="ECO:0007829|PDB:1U8V"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:1U8V"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 36..50
FT /evidence="ECO:0007829|PDB:1U8V"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:1U8V"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1U8V"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:1U8V"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 79..96
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 103..123
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 127..141
FT /evidence="ECO:0007829|PDB:1U8V"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1U8V"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:1U8V"
FT STRAND 177..186
FT /evidence="ECO:0007829|PDB:1U8V"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 208..213
FT /evidence="ECO:0007829|PDB:1U8V"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:1U8V"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 236..240
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:1U8V"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:1U8V"
FT STRAND 258..268
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:1U8V"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 281..318
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 324..349
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 363..373
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 376..388
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 391..394
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 398..401
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 414..421
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 430..444
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 449..452
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 454..458
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 463..473
FT /evidence="ECO:0007829|PDB:1U8V"
FT HELIX 476..487
FT /evidence="ECO:0007829|PDB:1U8V"
SQ SEQUENCE 490 AA; 54422 MW; EDC1E40336806E38 CRC64;
MLMTAEQYIE SLRKLNTRVY MFGEKIENWV DHPMIRPSIN CVAMTYELAQ DPQYADLMTT
KSNLIGKTIN RFANLHQSTD DLRKKVKMQR LLGQKTASCF QRCVGMDAFN AVFSTTYEID
QKYGTNYHKN FTEYLKYIQE NDLIVDGAMT DPKGDRGLAP SAQKDPDLFL RIVEKREDGI
VVRGAKAHQT GSINSHEHII MPTIAMTEAD KDYAVSFACP SDADGLFMIY GRQSCDTRKM
EEGADIDLGN KQFGGQEALV VFDNVFIPND RIFLCQEYDF AGMMVERFAG YHRQSYGGCK
VGVGDVVIGA AALAADYNGA QKASHVKDKL IEMTHLNETL YCCGIACSAE GYPTAAGNYQ
IDLLLANVCK QNITRFPYEI VRLAEDIAGG LMVTMPSEAD FKSETVVGRD GETIGDFCNK
FFAAAPTCTT EERMRVLRFL ENICLGASAV GYRTESMHGA GSPQAQRIMI ARQGNINAKK
ELAKAIAGIK
