(data stored in ACNUC7421 zone)

SWISSPROT: FADB_ACIBY

ID   FADB_ACIBY              Reviewed;         717 AA.
AC   B0VE45;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   08-MAY-2019, entry version 78.
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=ABAYE3470;
OS   Acinetobacter baumannii (strain AYE).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509173;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AYE;
RX   PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA   Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S.,
RA   Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S.,
RA   Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M.,
RA   Raoult D., Medigue C., Weissenbach J., Cruveiller S.;
RT   "Comparative analysis of Acinetobacters: three genomes for three
RT   lifestyles.";
RL   PLoS ONE 3:E1805-E1805(2008).
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; CU459141; CAM88259.1; -; Genomic_DNA.
DR   RefSeq; WP_000580942.1; NC_010410.1.
DR   SMR; B0VE45; -.
DR   PRIDE; B0VE45; -.
DR   EnsemblBacteria; CAM88259; CAM88259; ABAYE3470.
DR   KEGG; aby:ABAYE3470; -.
DR   HOGENOM; HOG000261344; -.
DR   KO; K01825; -.
DR   OMA; KMGKNPI; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000002446; 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; B0VE45.
DR   SWISS-2DPAGE; B0VE45.
KW   Complete proteome; Fatty acid metabolism; Isomerase;
KW   Lipid degradation; Lipid metabolism; Lyase; Multifunctional enzyme;
KW   NAD; Oxidoreductase.
FT   CHAIN         1    717       Fatty acid oxidation complex subunit
FT                                alpha.
FT                                /FTId=PRO_1000186030.
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;  77874 MW;  C8F7CAC439DE6C1B CRC64;
     MIHAGNAITV QMLADGIAEF RFDLQGESVN KFNRATIEDF KAAIAAVKAN NDIKGLVVTS
     GKSTFIVGAD ITEFGQNFAQ GEKAIVDWLM PVHEIFNSFE DLDLPKVAAI NGMALGGGFE
     MCLVCDYRVM SEAAQVGLPE IKLGIYPGFG GSVRLSRLIG IDNAVEWMAM ATPKKPAAAL
     KDGAVDAVVA ADKLLDAATD LVKQAISGRL NWKAKRQEKL EAVKLNPLEQ MMAFNTAKGA
     VLAKANPAQY PAPKLLLDSL QAGASLARDE ALKAEAEGFA KAAVTPQAEA LIGLFINDQV
     VKKASKQHEK GAHPVNQAAV LGAGIMGGGI AYQAASKGTP IIMKDIGNPQ LALGMKEANN
     LLTKQVERKK MKPVQMGETL ARIRPTLSYE EFKEVDIVIE AVTENPKVKE IVLAETEKNV
     RENTIIASNT STISITRLAK ALQRPENFVG MHFFNPVHMM PLVEVIRGEK TSEEAIATTV
     VLAQKMGKTP IVVNDCPGFL VNRVLFPYFG AFDLLVKDGA DFQQIDNVMS KFGWPMGPAY
     LIDVVGIDTG VHGAEVMAEG FPDRMKPDYK GAIEAMYEAK RLGQKNDVGF YKYELDKKGK
     KAKTVDPTAY EVIAPFVTGE KREFDNQEII DRMMLALCNE TVRCLEDNIV ATASEADMAM
     IMGIGFPPFR GGPCRYIDQT GVAEYVALCD KYAHLGKAYE APQMLRDMAA NNKKFYG
//

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