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FADB_PSEFR
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   03-AUG-2022, entry version 144.
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; Proteobacteria; 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_NQKM01000042.1.
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; 1136138.JH604622_gene1072; -.
DR   DrugBank; DB08249; 3,6,9,12,15-PENTAOXATRICOSAN-1-OL.
DR   PRIDE; P28793; -.
DR   GeneID; 67381810; -.
DR   eggNOG; COG1024; Bacteria.
DR   eggNOG; COG1250; Bacteria.
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   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   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
 
 
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