ID FADB_PSEPG Reviewed; 715 AA. AC B0KH74; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 18-MAR-2008, sequence version 1. DT 16-JUN-2009, entry version 10. 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=PputGB1_1676; OS Pseudomonas putida (strain GB-1). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=76869; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., RA Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.; RT "Complete sequence of Pseudomonas putida GB-1."; 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; CP000926; ABY97579.1; -; Genomic_DNA. DR RefSeq; YP_001667915.1; -. DR GeneID; 5869456; -. DR GenomeReviews; CP000926_GR; PputGB1_1676. DR KEGG; ppg:PputGB1_1676; -. DR OMA; B0KH74; QFANSIF. 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 1 715 Fatty acid oxidation complex subunit FT alpha. FT /FTId=PRO_1000088080. FT REGION 1 190 Enoyl-CoA hydratase/isomerase (By FT similarity). FT REGION 312 715 3-hydroxyacyl-CoA dehydrogenase (By FT similarity). SQ SEQUENCE 715 AA; 77366 MW; DE811EBF9BF0B890 CRC64; MIYEGKAITV KALESGIVEL KFDLKGESVN KFNRLTLNEL RQAVEAIQAD ASVKGVIVSS GKDVFIVGAD ITEFVDNFKL PEAELVAGNL EANRIFNAFE DLEVPTVAAI NGIALGGGLE MCLAADYRVM SNSAKIGLPE VKLGIYPGFG GTVRLPRLIG SDNAIEWIAA GKENRAEDAL KVGAVDAVVA PELLLAGALD LIKRAISGEL DYKAKRQPKL EKLKLNAIEQ MMAFETAKGF VAGQAGPNYP APVEAIKSIQ KAANFGRDKA LEVEAAGFAK LAKTSVAESL IGLFLNDQEL KRKAKAHDEI AHDVKQAAVL GAGIMGGGIA YQSAVKGTPI LMKDIREEAI QLGLNEASKL LGNRVEKGRL TPAKMAEALN AIRPTLSYGD FANVDIVVEA VVENPKVKQA VLAEVEGQVK DDAILASNTS TISINLLAKA LKRPENFVGM HFFNPVHMMP LVEVIRGEKS SEVAVATTVA YAKKMGKNPI VVNDCPGFLV NRVLFPYFGG FAKLVSAGVD FVRIDKVMEK FGWPMGPAYL MDVVGIDTGH HGRDVMAEGF PDRMKDERRS AVDALYEANR LGQKNGKGFY AYETDKRGKP KKVFDATVLD VLKPIVFEQR EVTDEDIINW MMVPLCLETV RCLEDGIVET AAEADMGLVY GIGFPPFRGG ALRYIDSIGV AEFVALADQY ADLGPLYHPT AKLREMAKNG QRFFN //