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 B-
RT 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}.
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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
//
