(data stored in ACNUC7421 zone)

SWISSPROT: FADB_ALISL

ID   FADB_ALISL              Reviewed;         726 AA.
AC   B6EGU2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   08-MAY-2019, entry version 77.
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=VSAL_I2974;
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Aliivibrio.
OX   NCBI_TaxID=316275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238;
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S.,
RA   Bason N., Churcher C., Harris D., Norbertczak H., Quail M.A.,
RA   Sanders S., Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida
RT   strain LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(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; FM178379; CAQ80658.1; -; Genomic_DNA.
DR   RefSeq; WP_012551375.1; NC_011312.1.
DR   SMR; B6EGU2; -.
DR   STRING; 316275.VSAL_I2974; -.
DR   PRIDE; B6EGU2; -.
DR   EnsemblBacteria; CAQ80658; CAQ80658; VSAL_I2974.
DR   KEGG; vsa:VSAL_I2974; -.
DR   eggNOG; ENOG4105DYT; Bacteria.
DR   eggNOG; COG1024; LUCA.
DR   eggNOG; COG1250; LUCA.
DR   HOGENOM; HOG000261344; -.
DR   KO; K01825; -.
DR   OMA; IDLCMIL; -.
DR   OrthoDB; 977512at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000001730; Chromosome 1.
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; 2.
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; B6EGU2.
DR   SWISS-2DPAGE; B6EGU2.
KW   Complete proteome; Fatty acid metabolism; Isomerase;
KW   Lipid degradation; Lipid metabolism; Lyase; Multifunctional enzyme;
KW   NAD; Oxidoreductase.
FT   CHAIN         1    726       Fatty acid oxidation complex subunit
FT                                alpha.
FT                                /FTId=PRO_1000186031.
FT   NP_BIND     400    402       NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   REGION        1    189       Enoyl-CoA hydratase/isomerase.
FT                                {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   REGION      311    726       3-hydroxyacyl-CoA dehydrogenase.
FT                                {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   ACT_SITE    450    450       For 3-hydroxyacyl-CoA dehydrogenase
FT                                activity. {ECO:0000255|HAMAP-
FT                                Rule:MF_01621}.
FT   BINDING     296    296       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01621}.
FT   BINDING     324    324       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   BINDING     343    343       NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   BINDING     407    407       NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   BINDING     429    429       NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   BINDING     453    453       NAD. {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   BINDING     500    500       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01621}.
FT   BINDING     660    660       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01621}.
FT   SITE        119    119       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_01621}.
FT   SITE        139    139       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_01621}.
SQ   SEQUENCE   726 AA;  78731 MW;  E40B3EB8D2AFE361 CRC64;
     MIYQGENLSV DYIENGIAHL VFNAAGSVNK LNIATLRSLG EAIDVLYKQK DLQALLLSSG
     KSAFIVGADI TEFLGLFDTP EEELSDWLHQ ANVIFSRLED LPVPTLSAIT GFALGGGCEC
     VLATDFRLAD DTASIGLPET QLGIMPGWGG SVRLPRLIGA DPAMEVITTG KPKRAKDALK
     IGMVDGIVSR ETLIDASVSM LKQAIDGQLN WQQRREQKKA PIQLSPLEAA MSFNVAKGMI
     MKMAGKHYPA PLTAVKSIEQ SANMHRDDAL AIENKHFVAL TRTDVAKSLV GIFLNDQLVK
     SKAKQAVKNS EPVKNAAVLG AGIMGGGIAY QSASKGVPVL MKDIAQASLD LGMNEASKLL
     NKQLERGRLS GLKMAQVLSS ITPSLNYGGI ETKDVIVEAV VENPTIKAAV LAEVENEVNE
     HAILASNTST IPISLLAKSL KRPENFCGMH FFNPVHRMPL VEVIRGEKTS QQTIDRVVAY
     ASQMGKTPIV VNDCPGFFVN RVLFPYFAGF SLLLRDGGNY QQIDKVMEKE FGWPMGPAYL
     LDVVGIDTAH HAQAVMAQGF PERMAKNGRD VIDAMFEDDR YGQKNGIGFY AYALDKKGKP
     KKNIDEKTNA IIATITDSTQ PYTSEQISAR MMIPMINEVI RCLDEGIIAS PAEADMALVY
     GLGFPPFKGG VFRYLDSIGL DTYLDMAKEF EQLSPVYQVP DSIKQKAAAG ECYYPAPKSS
     VSSPSV
//

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