FADB_PSEOL
ID FADB_PSEOL Reviewed; 715 AA.
AC Q93Q12;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
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};
OS Pseudomonas oleovorans.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas;
OC Pseudomonas oleovorans/pseudoalcaligenes group.
OX NCBI_TaxID=301;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29347 / CIP 105816 / NRRL B-14683 / TF4-1L;
RX PubMed=12115060; DOI=10.1007/s00203-002-0444-0;
RA Fiedler S., Steinbuchel A., Rehm B.H.;
RT "The role of the fatty acid beta-oxidation multienzyme complex from
RT Pseudomonas oleovorans in polyhydroxyalkanoate biosynthesis: molecular
RT characterization of the fadBA operon from P. oleovorans and of the enoyl-
RT CoA hydratase genes phaJ from P. oleovorans and Pseudomonas putida.";
RL Arch. Microbiol. 178:149-160(2002).
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}.
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DR EMBL; AF288535; AAK83058.1; -; Genomic_DNA.
DR AlphaFoldDB; Q93Q12; -.
DR SMR; Q93Q12; -.
DR UniPathway; UPA00659; -.
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 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 Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF48179; SSF48179; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR TIGRFAMs; TIGR02437; FadB; 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_0000109277"
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; 77268 MW; F67EE0D424E39307 CRC64;
MIYQGKAITV KALESGIVEL KFDLKGESVN KFNRLTLNEL RQAVDAIQAD ASVKGVIVSS
GKDVFIVGAD ITEFVDNFKL PEAELVAGNL EANRIFNAFE DLEVPTVAAI SGIALGGGLE
MCLAADYRVM STSAKIGLPE VKLGIYPGFG GTVRLPRLIG SDNAIEWIAA GKENRAEDAL
KVGAVDAVVA PELLMAGALD LVKRAISGEL DYKAKRQPKL EKLKLNAIEQ MMAFETAKGF
VAGQAGPNYP APVEAIKTIQ KAANFGRDKA LEVEAAGFAK LAKTSVAESL IGLFLNDQEL
KRKAKAHDEI AHDAKQAAVL GAGIMGGGIA YQSAVKGTPI LMKDIREEAI QLGLNEASKL
LGNRVEKGRL TPAKMAEALN AIRPTLSYGD FANVDIVVEA VVENPKVKQA VLAEVETQVK
DDAILASNTS TISINLLAKA LKRPENFVGM HFFNPVHMMP LVEVIRGEKS SEVAVATTVA
YAKKMGKNPI VVNDCPGFLV NRVLFPYFGG FAKLVSAGVD FVRIDKVMEK FGWPMGPAYL
MDVVGIDTGH HGRDVMAEGF PDRMKDERRS AVDALYEANR LGQKNGKGFY AYETDKRGKP
KKVADASVLD VLKPIVFEQR EVTDEDIINW MMIPLCLETV RCLEDGIVET AAEADMGLVY
GIGFPPFRGG ALRYIDSIGV AEFVALADQY ADLGPLYHPT AKLREMAKNG QRFFN
