ID FADB_PSEFR Reviewed; 715 AA. AC P28793; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 27-MAR-2024, entry version 151. DE RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000255|HAMAP-Rule:MF_01621}; DE Includes: DE RecName: Full=Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase {ECO:0000255|HAMAP-Rule:MF_01621}; DE EC=4.2.1.17 {ECO:0000255|HAMAP-Rule:MF_01621}; DE EC=5.1.2.3 {ECO:0000255|HAMAP-Rule:MF_01621}; DE EC=5.3.3.8 {ECO:0000255|HAMAP-Rule:MF_01621}; DE Includes: DE RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01621}; DE EC=1.1.1.35 {ECO:0000255|HAMAP-Rule:MF_01621}; GN Name=fadB {ECO:0000255|HAMAP-Rule:MF_01621}; Synonyms=faoA; OS Pseudomonas fragi. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=296; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=B-0771; RX PubMed=1607366; DOI=10.1093/oxfordjournals.jbchem.a123722; RA Sato S., Hayashi M., Imamura S., Ozeki Y., Kawaguchi A.; RT "Primary structures of the genes, faoA and faoB, from Pseudomonas fragi B- RT 0771 which encode the two subunits of the HDT multienzyme complex involved RT in fatty acid beta-oxidation."; RL J. Biochem. 111:8-15(1992). RN [2] RP INDUCTION. RX PubMed=8206878; DOI=10.1093/oxfordjournals.jbchem.a124330; RA Sato S., Ozeki Y., Kawaguchi A.; RT "Transcription of the faoAB operon which encodes the HDT multienzyme RT complex involved in fatty acid beta-oxidation in Pseudomonas fragi RT B-0771."; RL J. Biochem. 115:286-292(1994). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEXES WITH NAD AND RP ACYL-COENZYME A, AND SUBUNIT. RX PubMed=15229654; DOI=10.1038/sj.emboj.7600298; RA Ishikawa M., Tsuchiya D., Oyama T., Tsunaka Y., Morikawa K.; RT "Structural basis for channelling mechanism of a fatty acid beta-oxidation RT multienzyme complex."; RL EMBO J. 23:2745-2754(2004). CC -!- FUNCTION: Involved in the aerobic and anaerobic degradation of long- CC chain fatty acids via beta-oxidation cycle. Catalyzes the formation of CC 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use CC D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. CC {ECO:0000255|HAMAP-Rule:MF_01621}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + CC NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O; CC Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318, CC ChEBI:CHEBI:58856; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01621}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O; CC Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521, CC ChEBI:CHEBI:137480; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01621}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA; CC Xref=Rhea:RHEA:21760, ChEBI:CHEBI:57315, ChEBI:CHEBI:57316; CC EC=5.1.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; CC Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489; CC EC=5.3.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; CC Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097; CC EC=5.3.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC {ECO:0000255|HAMAP-Rule:MF_01621}. CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta chains CC (FadA). {ECO:0000255|HAMAP-Rule:MF_01621, ECO:0000269|PubMed:15229654}. CC -!- INTERACTION: CC P28793; P28790: fadA; NbExp=4; IntAct=EBI-1039318, EBI-1039311; CC -!- INDUCTION: By palmitic acid. {ECO:0000269|PubMed:8206878}. CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA CC hydratase/isomerase family. {ECO:0000255|HAMAP-Rule:MF_01621}. CC -!- SIMILARITY: In the C-terminal section; belongs to the 3-hydroxyacyl-CoA CC dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_01621}. 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; D10390; BAA01227.1; -; Genomic_DNA. DR PIR; JX0199; JX0199. DR RefSeq; WP_016780046.1; NZ_SDUZ01000007.1. DR PDB; 1WDK; X-ray; 2.50 A; A/B=1-715. DR PDB; 1WDL; X-ray; 3.50 A; A/B=1-715. DR PDB; 1WDM; X-ray; 3.80 A; A/B=1-715. DR PDB; 2D3T; X-ray; 3.40 A; A/B=1-715. DR PDBsum; 1WDK; -. DR PDBsum; 1WDL; -. DR PDBsum; 1WDM; -. DR PDBsum; 2D3T; -. DR AlphaFoldDB; P28793; -. DR SMR; P28793; -. DR DIP; DIP-29089N; -. DR IntAct; P28793; 1. DR STRING; 296.B6D87_06985; -. DR DrugBank; DB08249; 3,6,9,12,15-PENTAOXATRICOSAN-1-OL. DR GeneID; 72389476; -. DR eggNOG; COG1024; Bacteria. DR eggNOG; COG1250; Bacteria. DR OrthoDB; 5389341at2; -. DR UniPathway; UPA00659; -. DR EvolutionaryTrace; P28793; -. DR GO; GO:0036125; C:fatty acid beta-oxidation multienzyme complex; IEA:InterPro. DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-UniRule. DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro. DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway. DR CDD; cd06558; crotonase-like; 1. DR Gene3D; 1.10.1040.50; -; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_01621; FadB; 1. DR InterPro; IPR006180; 3-OHacyl-CoA_DH_CS. DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd. DR InterPro; IPR006108; 3HC_DH_C. DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf. DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf. DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS. DR InterPro; IPR001753; Enoyl-CoA_hydra/iso. DR InterPro; IPR012799; FadB. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR02437; FadB; 1. DR PANTHER; PTHR43612:SF8; FATTY ACID OXIDATION COMPLEX SUBUNIT ALPHA; 1. DR PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 1. DR Pfam; PF00725; 3HCDH; 1. DR Pfam; PF02737; 3HCDH_N; 1. DR Pfam; PF00378; ECH_1; 1. DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2. DR SUPFAM; SSF52096; ClpP/crotonase; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00067; 3HCDH; 1. DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Fatty acid metabolism; Isomerase; KW Lipid degradation; Lipid metabolism; Lyase; Multifunctional enzyme; NAD; KW Oxidoreductase. FT CHAIN 1..715 FT /note="Fatty acid oxidation complex subunit alpha" FT /id="PRO_0000109276" FT REGION 1..190 FT /note="Enoyl-CoA hydratase/isomerase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT REGION 312..715 FT /note="3-hydroxyacyl-CoA dehydrogenase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT ACT_SITE 451 FT /note="For 3-hydroxyacyl-CoA dehydrogenase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT BINDING 297 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:15229654" FT BINDING 325 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:15229654" FT BINDING 344 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:15229654" FT BINDING 401..403 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:15229654" FT BINDING 408 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:15229654" FT BINDING 430 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:15229654" FT BINDING 454 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:15229654" FT BINDING 501 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:15229654" FT BINDING 660 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:15229654" FT SITE 120 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT SITE 140 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01621" FT STRAND 6..12 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 14..16 FT /evidence="ECO:0007829|PDB:1WDK" FT STRAND 17..22 FT /evidence="ECO:0007829|PDB:1WDK" FT STRAND 27..29 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 34..49 FT /evidence="ECO:0007829|PDB:1WDK" FT STRAND 55..67 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 71..77 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 82..100 FT /evidence="ECO:0007829|PDB:1WDK" FT STRAND 106..110 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 117..123 FT /evidence="ECO:0007829|PDB:1WDK" FT STRAND 125..131 FT /evidence="ECO:0007829|PDB:1WDK" FT STRAND 135..137 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 139..143 FT /evidence="ECO:0007829|PDB:1WDK" FT TURN 148..150 FT /evidence="ECO:0007829|PDB:2D3T" FT HELIX 151..159 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 161..170 FT /evidence="ECO:0007829|PDB:1WDK" FT STRAND 173..175 FT /evidence="ECO:0007829|PDB:1WDL" FT HELIX 176..181 FT /evidence="ECO:0007829|PDB:1WDK" FT STRAND 184..189 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 191..193 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 194..206 FT /evidence="ECO:0007829|PDB:1WDK" FT STRAND 207..210 FT /evidence="ECO:0007829|PDB:2D3T" FT HELIX 212..216 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 217..220 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 227..245 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 250..262 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 267..282 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 285..308 FT /evidence="ECO:0007829|PDB:1WDK" FT STRAND 315..320 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 323..335 FT /evidence="ECO:0007829|PDB:1WDK" FT STRAND 340..343 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 347..365 FT /evidence="ECO:0007829|PDB:1WDK" FT TURN 366..368 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 372..381 FT /evidence="ECO:0007829|PDB:1WDK" FT STRAND 382..388 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 391..393 FT /evidence="ECO:0007829|PDB:1WDK" FT STRAND 395..399 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 405..416 FT /evidence="ECO:0007829|PDB:1WDK" FT STRAND 424..427 FT /evidence="ECO:0007829|PDB:1WDK" FT STRAND 430..432 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 434..437 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 438..440 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 444..446 FT /evidence="ECO:0007829|PDB:1WDK" FT STRAND 447..451 FT /evidence="ECO:0007829|PDB:1WDK" FT TURN 456..458 FT /evidence="ECO:0007829|PDB:1WDK" FT STRAND 461..466 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 472..484 FT /evidence="ECO:0007829|PDB:1WDK" FT STRAND 488..494 FT /evidence="ECO:0007829|PDB:1WDK" FT TURN 496..499 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 500..516 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 521..531 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 537..544 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 546..559 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 561..564 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 571..577 FT /evidence="ECO:0007829|PDB:1WDK" FT TURN 583..586 FT /evidence="ECO:0007829|PDB:1WDK" FT STRAND 587..592 FT /evidence="ECO:0007829|PDB:1WDK" FT STRAND 599..603 FT /evidence="ECO:0007829|PDB:1WDL" FT HELIX 607..612 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 613..615 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 624..644 FT /evidence="ECO:0007829|PDB:1WDK" FT STRAND 647..650 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 651..661 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 666..668 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 671..678 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 680..689 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 690..693 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 695..697 FT /evidence="ECO:0007829|PDB:1WDK" FT HELIX 701..708 FT /evidence="ECO:0007829|PDB:1WDK" SQ SEQUENCE 715 AA; 77137 MW; F22727CDEF7F3DB5 CRC64; MIYEGKAITV TALESGIVEL KFDLKGESVN KFNRLTLNEL RQAVDAIKAD ASVKGVIVSS GKDVFIVGAD ITEFVENFKL PDAELIAGNL EANKIFSDFE DLNVPTVAAI NGIALGGGLE MCLAADFRVM ADSAKIGLPE VKLGIYPGFG GTVRLPRLIG VDNAVEWIAS GKENRAEDAL KVSAVDAVVT ADKLGAAALD LIKRAISGEL DYKAKRQPKL EKLKLNAIEQ MMAFETAKGF VAGQAGPNYP APVEAIKTIQ KAANFGRDKA LEVEAAGFAK LAKTSASNCL IGLFLNDQEL KKKAKVYDKI AKDVKQAAVL GAGIMGGGIA YQSASKGTPI LMKDINEHGI EQGLAEAAKL LVGRVDKGRM TPAKMAEVLN GIRPTLSYGD FGNVDLVVEA VVENPKVKQA VLAEVENHVR EDAILASNTS TISISLLAKA LKRPENFVGM HFFNPVHMMP LVEVIRGEKS SDLAVATTVA YAKKMGKNPI VVNDCPGFLV NRVLFPYFGG FAKLVSAGVD FVRIDKVMEK FGWPMGPAYL MDVVGIDTGH HGRDVMAEGF PDRMKDDRRS AIDALYEAKR LGQKNGKGFY AYEADKKGKQ KKLVDSSVLE VLKPIVYEQR DVTDEDIINW MMIPLCLETV RCLEDGIVET AAEADMGLVY GIGFPLFRGG ALRYIDSIGV AEFVALADQY AELGALYHPT AKLREMAKNG QSFFG //