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 02-SEP-2026, entry version 109. 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; Bacillati; Bacillota; 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}. 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; AJ250267; CAB60035.2; -; Genomic_DNA. DR PIR; S34765; S34765. DR RefSeq; WP_155758543.1; NZ_JAFJZZ010000001.1. DR PDB; 1U8V; X-ray; 1.60 A; A/B/C/D=1-490. DR AlphaFoldDB; P55792; -. DR SMR; P55792; -. DR DrugBank; DB03147; Flavin adenine dinucleotide. DR KEGG; ag:CAB60035; -. DR BioCyc; MetaCyc:MONOMER-13485; -. DR BRENDA; 4.2.1.120; 1455. DR EvolutionaryTrace; P55792; -. DR GO; GO:0043721; F:4-hydroxybutanoyl-CoA dehydratase activity; IEA:UniProtKB-EC. 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 Gene3D; 1.10.3140.10; 4-hydroxybutyryl-coa dehydratase, domain 1; 1. DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1. DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 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_sf. 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; 4-HYDROXYPHENYLACETATE 3-MONOOXYGENASE-RELATED; 1. DR PANTHER; PTHR36117:SF3; 4-HYDROXYPHENYLACETATE 3-MONOOXYGENASE-RELATED; 1. DR Pfam; PF03241; HpaB; 1. DR Pfam; PF11794; HpaB_N; 1. DR PIRSF; PIRSF000331; HpaA_HpaB; 1. DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1. DR PDBsum; 1U8V; -. 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 74..76 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 395..397 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 450..455 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 //