(data stored in ACNUC7421 zone)

SWISSPROT: FADB_ACIAD

ID   FADB_ACIAD              Reviewed;         717 AA.
AC   Q6FF68;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   08-MAY-2019, entry version 112.
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=ACIAD0335;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S.,
RA   Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P.,
RA   Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp.
RT   ADP1, a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
CC   -!- FUNCTION: Involved in the aerobic and anaerobic degradation of
CC       long-chain fatty acids via beta-oxidation cycle. Catalyzes the
CC       formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA.
CC       It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as
CC       substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+)
CC         + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01621};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-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)-hydroxyacyl-CoA = a (3E)-enoyl-CoA +
CC         H2O; 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)-hydroxybutanoyl-CoA = (3R)-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
CC       chains (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-
CC       hydroxyacyl-CoA dehydrogenase family. {ECO:0000255|HAMAP-
CC       Rule:MF_01621}.
DR   EMBL; CR543861; CAG67289.1; -; Genomic_DNA.
DR   RefSeq; WP_004920538.1; NC_005966.1.
DR   SMR; Q6FF68; -.
DR   STRING; 62977.ACIAD0335; -.
DR   PRIDE; Q6FF68; -.
DR   EnsemblBacteria; CAG67289; CAG67289; ACIAD0335.
DR   KEGG; aci:ACIAD0335; -.
DR   eggNOG; ENOG4105DYT; Bacteria.
DR   eggNOG; COG1250; LUCA.
DR   HOGENOM; HOG000261344; -.
DR   KO; K01825; -.
DR   OMA; IDLCMIL; -.
DR   OrthoDB; 977512at2; -.
DR   BioCyc; ASP62977:ACIAD_RS01570-MONOMER; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000000430; 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:dodecenoyl-CoA delta-isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-UniRule.
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;
DR   PRODOM; Q6FF68.
DR   SWISS-2DPAGE; Q6FF68.
KW   Complete proteome; Fatty acid metabolism; Isomerase;
KW   Lipid degradation; Lipid metabolism; Lyase; Multifunctional enzyme;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN         1    717       Fatty acid oxidation complex subunit
FT                                alpha.
FT                                /FTId=PRO_0000109264.
FT   NP_BIND     402    404       NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   REGION        1    190       Enoyl-CoA hydratase/isomerase.
FT                                {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   REGION      313    717       3-hydroxyacyl-CoA dehydrogenase.
FT                                {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   ACT_SITE    452    452       For 3-hydroxyacyl-CoA dehydrogenase
FT                                activity. {ECO:0000255|HAMAP-
FT                                Rule:MF_01621}.
FT   BINDING     298    298       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01621}.
FT   BINDING     326    326       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   BINDING     345    345       NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   BINDING     409    409       NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   BINDING     431    431       NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   BINDING     455    455       NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   BINDING     502    502       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01621}.
FT   SITE        120    120       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   SITE        140    140       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_01621}.
SQ   SEQUENCE   717 AA;  77985 MW;  C0981AB69CA14483 CRC64;
     MIHAGNAITV QMLSDGIAEF RFDLQGESVN KFNRATIEDF QAAIEAVKNH PEVKGLIVTS
     AKSTFIVGAD ITEFGQNFAQ GEKAIVEWAL PVHDIFNSFE DLDIPKVAAI NGMALGGGFE
     MCLVCDYRVM SDQAQVGLPE IKLGIFPGFG GTVRLSRLIG IDNAVEWIAM AAPKKPAAAL
     KDGAVDAVVS ADKLQEAAID LVKQALAGRV DWKAKRQEKL NPVKLNPLEQ MMAFNTAKGA
     VLAKANPAQY PAPKLMLDSL QAGASLGRDE ALKVETEGFA KAAITPQAEA LIGLFLNDQI
     IKKTSKKHEK GAHPVNQAAV LGAGIMGGGI AYQAASKGTP IIMKDIGNPQ LALGMQEANG
     LLTKQVERKK LTPAKMGETL ARIRPTLSYD EFKEVDIVIE AVTENPKIKE AVLADTEAKV
     RDNTIIASNT STISITRLAK ALKRPENFVG MHFFNPVHMM PLVEVIRGEQ TSEEAVATTV
     VLAQKMGKTP IVVNDCPGFL VNRVLFPYFG AFDLLLKDGA DFQQIDKVME KFGWPMGPAY
     LMDVVGIDTG VHGAEVMAEG FPDRMKPDYK GSIQTMYEAK RLGQKNDVGF YKYELDKKGK
     KAKTVDSTAY EVIAPVVTSE KREFDAQEII DRMMLALCNE TVRCLEDNIV ATPAEADMAM
     IMGIGFPPFR GGPCRYIDQT GVAEYVALCN KYAHLGKAYE APQLLRDMAE NNKKFYG
//

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