ID   FADB_PSEF5              Reviewed;         715 AA.
AC   Q4KFC4;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 118.
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};
GN   OrderedLocusNames=PFL_1940;
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
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}.
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; CP000076; AAY91227.1; -; Genomic_DNA.
DR   RefSeq; WP_011060260.1; NC_004129.6.
DR   AlphaFoldDB; Q4KFC4; -.
DR   SMR; Q4KFC4; -.
DR   STRING; 220664.PFL_1940; -.
DR   GeneID; 57474984; -.
DR   KEGG; pfl:PFL_1940; -.
DR   PATRIC; fig|220664.5.peg.1979; -.
DR   eggNOG; COG1024; Bacteria.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_009834_16_3_6; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000008540; Chromosome.
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   3: Inferred from homology;
KW   Fatty acid metabolism; Isomerase; Lipid degradation; Lipid metabolism;
KW   Lyase; Multifunctional enzyme; NAD; Oxidoreductase.
FT   CHAIN           1..715
FT                   /note="Fatty acid oxidation complex subunit alpha"
FT                   /id="PRO_0000109275"
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:0000255|HAMAP-Rule:MF_01621"
FT   BINDING         325
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT   BINDING         344
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT   BINDING         401..403
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT   BINDING         408
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT   BINDING         430
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT   BINDING         454
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT   BINDING         501
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
FT   BINDING         660
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01621"
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"
SQ   SEQUENCE   715 AA;  77124 MW;  0043AE4C28EE5168 CRC64;
     MIYEGKAITV KALESGIVEL NFDLKGESVN KFNRLTLNEL RQAVDTIKAD ASIKGVIVSS
     GKDVFIVGAD ITEFVDNFKL PDAELVAGNL EANKIFSDFE DLNVPTVAAI NGIALGGGLE
     MCLAADYRVM AASAKIGLPE VKLGIYPGFG GTVRLPRLIG ADNAIEWIAA GKENRAEDAL
     KVGAVDAVVA PDKLKDAALA LVKRAISGEF DYKAKRQPKL EKLKLNAIEQ MMAFETAKGF
     VAGQAGPNYP APVEAIKTIQ KAANFGRDKA LEVEAAGFVK LAKTSAAQSL IGLFLNDQEL
     KKKAKAYDEI AKDVKQAAVL GAGIMGGGIA YQSASKGTPI LMKDINEHGI EQGLAEAAKL
     LVGRVDKGRM TAAKMAEVLN GIRPTLSYGD FGNVDLVVEA VVENPKVKQI VLAEVEGQVK
     EDTILASNTS TISISLLAKA LKRPENFVGM HFFNPVHMMP LVEVIRGEKS SELAVATTVA
     YAKKMGKNPI VVNDCPGFLV NRVLFPYFGG FAKLVSAGVD FVRIDKIMEK FGWPMGPAYL
     MDVVGIDTGH HGRDVMAEGF PDRMKDDRRS AVDVLYEAKR LGQKNGKGFY AYETDKKGKQ
     KKVADPSVLE VLKPIVYEQR EVTDEDIINW MMIPLCLETV RCLEDGIVET AAEADMGLVY
     GIGFPPFRGG ALRYIDSIGV AEFVALADQY ADLGALYHPT AKLREMAKNG QSFFG
//