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Database: UniProt
Entry: Q08A39
LinkDB: Q08A39
Original site: Q08A39 
ID   FADB_SHEFN              Reviewed;         716 AA.
AC   Q08A39;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   11-JUN-2014, entry version 63.
DE   RecName: Full=Fatty acid oxidation complex subunit alpha;
DE   Includes:
DE     RecName: Full=Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase;
DE              EC=4.2.1.17;
DE              EC=5.1.2.3;
DE              EC=5.3.3.8;
DE   Includes:
DE     RecName: Full=3-hydroxyacyl-CoA dehydrogenase;
DE              EC=1.1.1.35;
GN   Name=fadB; OrderedLocusNames=Sfri_0013;
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T.,
RA   Nealson K.H., Newman D., Tiedje J.M., Zhou J., Romine M.F.,
RA   Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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 (By 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.
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DR   EMBL; CP000447; ABI69876.1; -; Genomic_DNA.
DR   RefSeq; YP_748714.1; NC_008345.1.
DR   ProteinModelPortal; Q08A39; -.
DR   SMR; Q08A39; 1-714.
DR   STRING; 318167.Sfri_0013; -.
DR   EnsemblBacteria; ABI69876; ABI69876; Sfri_0013.
DR   GeneID; 4277696; -.
DR   KEGG; sfr:Sfri_0013; -.
DR   PATRIC; 23493733; VBISheFri14343_0013.
DR   eggNOG; COG1250; -.
DR   HOGENOM; HOG000261344; -.
DR   KO; K01825; -.
DR   OMA; NPIVVND; -.
DR   OrthoDB; EOG6M9F0M; -.
DR   BioCyc; SFRI318167:GIXS-13-MONOMER; -.
DR   UniPathway; UPA00659; -.
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-HAMAP.
DR   GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0050662; F:coenzyme binding; IEA:InterPro.
DR   GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1040.10; -; 2.
DR   Gene3D; 3.40.50.720; -; 1.
DR   Gene3D; 3.90.226.10; -; 1.
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; IPR029045; ClpP/crotonase-like_dom.
DR   InterPro; IPR001753; Crotonase_core_superfam.
DR   InterPro; IPR013328; DH_multihelical.
DR   InterPro; IPR012799; FadB.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH; 1.
DR   SUPFAM; SSF48179; SSF48179; 2.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR02437; FadB; 1.
DR   PROSITE; PS00067; 3HCDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Fatty acid metabolism; Isomerase;
KW   Lipid degradation; Lipid metabolism; Lyase; Multifunctional enzyme;
KW   NAD; Oxidoreductase.
FT   CHAIN         1    716       Fatty acid oxidation complex subunit
FT                                alpha.
FT                                /FTId=PRO_1000069575.
FT   NP_BIND     400    402       NAD (By similarity).
FT   NP_BIND     427    429       NAD (By similarity).
FT   REGION        1    189       Enoyl-CoA hydratase/isomerase (By
FT                                similarity).
FT   REGION      311    716       3-hydroxyacyl-CoA dehydrogenase (By
FT                                similarity).
FT   ACT_SITE    450    450       For 3-hydroxyacyl-CoA dehydrogenase
FT                                activity (By similarity).
FT   BINDING     296    296       Substrate (By similarity).
FT   BINDING     324    324       NAD; via amide nitrogen (By similarity).
FT   BINDING     343    343       NAD (By similarity).
FT   BINDING     407    407       NAD (By similarity).
FT   BINDING     453    453       NAD (By similarity).
FT   BINDING     500    500       Substrate (By similarity).
FT   BINDING     660    660       Substrate (By similarity).
FT   SITE        119    119       Important for catalytic activity (By
FT                                similarity).
FT   SITE        139    139       Important for catalytic activity (By
FT                                similarity).
SQ   SEQUENCE   716 AA;  76897 MW;  28434AB7ABC1166C CRC64;
     MIYQSPTIQV ELLEDNIAKL CFNAQGSVNK FDRETIASLD AALDSIKQNT NIKALLLTSA
     KSTFIVGADI TEFLTLFQQD DATLLAWVEQ ANAVFNKLED LPFPTASAIN GFALGGGCET
     ILATDLRVAD TNARIGLPET KLGLIPGFGG TVRLPRVIGA DNALEWITTA KDQRPEDALK
     VGAIDAVVAP ENLEAAAIQM LHDALNGSLD WQARRTKKQS PLQLPKLEAM MSFATAKGMV
     FSVAGKHYPA PMAAVNVVEQ AAGLDRDGAL KVEALAFIKL AKTDVAQALI GIFLNDQFVK
     GKAKKAGKLA KDVNQAAVLG AGIMGGGIAY QSASKGTPIV MKDIAQPALE LGLNEAAKIL
     TTQVARGRST PEKMAKVLNN ITPSLDYAAI KNSDIVVEAV VEHPKVKATV LAEVEGYVSE
     DAIIASNTST ISINLLAKSL KKPERFCGMH FFNPVHKMPL VEIIRGEHSS EETIATVVAY
     ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SGLLAEGADF AAVDKVMEKQ FGWPMGPAYL
     LDVVGLDTGH HAQAVMAEGF PDRMGKNGKD AIDIMFENKR LGQKNTKGFY AYSVDRRGKP
     KKDIDPTSYE LLSAEFGELK AFESDDIIAR CMIPMIIETV RCLEEGIIAS PAEGDMGLVY
     GIGFPPFRGG VFRYLDTMGV ANFVALADKY AHLGGLYQVT DAMRALAANN GSYYQA
//
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