ID FADB_SHEHH Reviewed; 717 AA. AC B0TLB9; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 16-JUN-2009, entry version 11. 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=5.3.3.8; DE EC=5.1.2.3; DE Includes: DE RecName: Full=3-hydroxyacyl-CoA dehydrogenase; DE EC=1.1.1.35; GN Name=fadB; OrderedLocusNames=Shal_0016; OS Shewanella halifaxensis (strain HAW-EB4). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=458817; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Zhao J.-S., Richardson P.; RT "Complete sequence of Shewanella halifaxensis HAW-EB4."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000931; ABZ74592.1; -; Genomic_DNA. DR RefSeq; YP_001672251.1; -. DR GeneID; 5904871; -. DR GenomeReviews; CP000931_GR; Shal_0016. DR KEGG; shl:Shal_0016; -. DR OMA; B0TLB9; ANNGSYY. DR GO; GO:0016507; C:fatty acid beta-oxidation multienzyme complex; IEA:InterPro. DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:HAMAP. DR GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:HAMAP. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:HAMAP. DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:HAMAP. DR GO; GO:0009062; P:fatty acid catabolic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR HAMAP; MF_01621; -; 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; 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; 1. DR Pfam; PF00725; 3HCDH; 1. DR Pfam; PF02737; 3HCDH_N; 1. DR Pfam; PF00378; ECH; 1. DR TIGRFAMs; TIGR02437; FadB; 1. DR PROSITE; PS00067; 3HCDH; 1. DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 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 1 717 Fatty acid oxidation complex subunit FT alpha. FT /FTId=PRO_1000088083. FT REGION 1 189 Enoyl-CoA hydratase/isomerase (By FT similarity). FT REGION 311 717 3-hydroxyacyl-CoA dehydrogenase (By FT similarity). SQ SEQUENCE 717 AA; 77430 MW; F2D56F4583E4BF12 CRC64; MIYQSPTIEV ELLEDNIAHL CFKAQGSVNK FDRETIDSLN AALDSIKQDT SIKALMLSSA KDAFIVGADI TEFLGLFAEE DAVLQSWLEQ ANVVFNKLED LPFPTLSAIN GFALGAGCET ILATDFRIAD TTARIGLPET KLGIIPGFGG TVRLPRVIGA DNALEWITSG KDQRPDAALK VGAIDAVVAP EQLRPAALRM LKDAMAEKLD WQTRRAKKLA PLTLPKLEAM MSFATAKGMV FKIAGKHYPA PMAVISVIEQ AAQCGRAEAL QIEHQAFIKL AKTEVAQALI GIFLNDQLVK GKAKKAGKLA KKVNSAAVLG AGIMGGGIAY QSASKGTPIV MKDIAQPALD LGLGEAAKLL TAQVKRGRST PAKMATVLNN ITPALDYAPV KDTDIIVEAV VEHPKVKSMV LAEVEEHVSE DAIITSNTST ISINLLAKSL KKPERFCGMH FFNPVHKMPL VEVIRGENSS DETVASVVAY ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SGLLADGADF AAIDKVMEKQ FGWPMGPAYL LDVVGLDTGH HAQAVMAEGF PDRMGKSGKD AIDVMFEAER FGQKNNKGFY QYSVDHRGKP KKDLDPTSYE LLQAEFGEQK AFESDEIIAR TMIPMIIETV RCLEEGIIAS PAEADMGLVY GLGFPPFRGG VFRYLDTIGV ANFVALADKY AHLGGLYQVT DTMRELAANN GSYYQQA //