ID FADB_SHEPC Reviewed; 716 AA. AC A4Y1B6; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 16-JUN-2009, entry version 17. 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=Sputcn32_0013; OS Shewanella putrefaciens (strain CN-32 / ATCC BAA-453). OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=319224; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Romine M.F., Fredrickson J., Tiedje J., Richardson P.; RT "Complete sequence of Shewanella putrefaciens CN-32."; RL Submitted (APR-2007) 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; CP000681; ABP73749.1; -; Genomic_DNA. DR RefSeq; YP_001181548.1; -. DR GeneID; 5081488; -. DR GenomeReviews; CP000681_GR; Sputcn32_0013. DR KEGG; spc:Sputcn32_0013; -. DR OMA; A4Y1B6; 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:0005488; F: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; 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 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; FALSE_NEG. 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_1000069577. FT REGION 1 189 Enoyl-CoA hydratase/isomerase (By FT similarity). FT REGION 311 716 3-hydroxyacyl-CoA dehydrogenase (By FT similarity). SQ SEQUENCE 716 AA; 76716 MW; 472D39B10A1E9325 CRC64; MIYQSPTIQV ELLEDNIAKL CFNAPGSVNK FDRETLASLD AALDSIKQNS NIKALVLTSS KDTFIVGADI TEFLGLFAQD DAVLLSWVEQ ANAVFNKLED LPFPTASAIK GFALGGGCET ILATDFRIAD TTAKIGLPET KLGIIPGFGG TVRLPRVIGA DNALEWISTG NDQRAEDALK VGAVDAVVAP EALEAAAIQM LKDAVAEKLD WQARRNRKLS ALTLPKLEAM MSFTTAKGMV FAVAGKHYPA PMAAVSVIEQ ASTKGRAEAL QIEHQAFIKL AKTDVAKALI GIFLNDQLVK GKAKKAGKLA KEVKNAAVLG AGIMGGGIAY QSASKGTPIV MKDIAQPALD LGLNEAAKLL SAQVARGRST PEKMAKVLNN ITPSLDYAAL KHSDVVVEAV VEHPKIKAQV LAEVEGYVSE DAIIASNTST ISINLLAKSM KKPERFCGMH FFNPVHKMPL VEVIRGEHSS EETIASVVAY ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF NGLLAEGGDF AAIDKVMEKQ FGWPMGPAYL LDVVGLDTGH HAQAVMAEGF PDRMGKSGTD AIDVMFENKR LGQKNGKGFY VYSVDSRGKP KKDVDPTSYG LLKDAFGELK TFEADDIIAR TMIPMIIETV RCLEEGIVAS PAEADMGLVY GLGFPPFRGG VFRYLDTMGV ANFVALADKY AHLGGLYQVT DAMRTKATNN GSYYQA //