(data stored in ACNUC7421 zone)

HOGENOM: ALISL_2_PE2734

ID   ALISL_2_PE2734                       STANDARD;      PRT;   726 AA.
AC   ALISL_2_PE2734; B6EGU2;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Fatty acid oxidation complex subunit alpha;Includes:
DE   RecName: Full=Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA
DE   isomerase/3-hydroxybutyryl-CoA epimerase; EC=4.2.1.17; EC=5.1.2.3;
DE   EC=5.3.3.8;Includes: RecName: Full=3-hydroxyacyl-CoA dehydrogenase;
DE   EC=1.1.1 35; (ALISL_2.PE2734).
GN   Name=fadB; OrderedLocusNames=VSAL_I2974;
OS   ALIIVIBRIO SALMONICIDA LFI1238.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ALISL_2.PE2734.
CC       Aliivibrio salmonicida LFI1238 chromosome 1, complete genome.
CC       pAACI03, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:FADB_ALISL
CC   -!- FUNCTION: Catalyzes the formation of an hydroxyacyl-CoA by
CC       addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA
CC       epimerase and 3-hydroxyacyl-CoA dehydrogenase activities (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
CC       + NADH.
CC   -!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-
CC       CoA + H(2)O.
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxybutanoyl-CoA = (R)-3-
CC       hydroxybutanoyl-CoA.
CC   -!- CATALYTIC ACTIVITY: (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-
CC       CoA.
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains (fadB) and two beta
CC       chains (fadA) (By similarity).
CC   -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC       hydratase/isomerase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the 3-
CC       hydroxyacyl-CoA dehydrogenase family.
CC   -!- GENE_FAMILY: HOG000261344 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B6EGU2; -.
DR   EMBL; FM178379; CAQ80658.1; -; Genomic_DNA.
DR   RefSeq; YP_002264299.1; NC_011312.1.
DR   ProteinModelPortal; B6EGU2; -.
DR   STRING; B6EGU2; -.
DR   GeneID; 6988472; -.
DR   GenomeReviews; FM178379_GR; VSAL_I2974.
DR   KEGG; vsa:VSAL_I2974; -.
DR   OMA; FGEQKAF; -.
DR   ProtClustDB; PRK11730; -.
DR   GO; GO:0016507; C:fatty acid beta-oxidation multienzyme complex; IEA:InterPro.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:EC.
DR   GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:EC.
DR   GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
DR   GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:EC.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:EC.
DR   GO; GO:0009062; P:fatty acid catabolic process; IEA:InterPro.
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_C-like.
DR   InterPro; IPR001753; Crotonase_core.
DR   InterPro; IPR013328; DH_multihelical.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   InterPro; IPR012799; FadB.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:1.10.1040.10; Opine_DH; 2.
DR   Pfam; PF00725; 3HCDH; 2.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH; 1.
DR   SUPFAM; SSF48179; 6DGDH_C_like; 2.
DR   TIGRFAMs; TIGR02437; FadB; 1.
DR   PROSITE; PS00067; 3HCDH; 1.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
DR   HOGENOMDNA; ALISL_2.PE2734; -.
KW   Complete proteome; Fatty acid metabolism; Isomerase;
KW   Lipid degradation; Lipid metabolism; Lyase; Multifunctional enzyme;
KW   NAD; Oxidoreductase.
SQ   SEQUENCE   726 AA;  UNKNOWN MW;  UNKNOWN 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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