ID FADB_ENT38 Reviewed; 729 AA. AC A4WFX4; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 16-JUN-2009, entry version 18. 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=Ent638_3949; OS Enterobacter sp. (strain 638). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Enterobacter. OX NCBI_TaxID=399742; 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., Kiss H., Brettin T., Bruce D., RA Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L., RA Vangronsveld J., van der Lelie D., Richardson P.; RT "Complete sequence of chromosome of Enterobacter sp. 638."; 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; CP000653; ABP62604.1; -; Genomic_DNA. DR RefSeq; YP_001178655.1; -. DR GeneID; 5114669; -. DR GenomeReviews; CP000653_GR; Ent638_3949. DR KEGG; ent:Ent638_3949; -. DR NMPDR; fig|399742.4.peg.3750; -. DR OMA; A4WFX4; 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; 2. 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 1 729 Fatty acid oxidation complex subunit FT alpha. FT /FTId=PRO_1000069562. FT REGION 1 189 Enoyl-CoA hydratase/isomerase (By FT similarity). FT REGION 311 729 3-hydroxyacyl-CoA dehydrogenase (By FT similarity). SQ SEQUENCE 729 AA; 79714 MW; D68AC01654407B8F CRC64; MLYKGDTLYV DWLEDGIAEL VFDAPGSVNK LDTATVASLG HALDVLEKQS DLKGLLLRSE KAAFIVGADI TEFLSLFQVP EEQLSQWLHF ANSVFNRLED LPVPTISAVN GYALGGGCEC VLATDYRLAT PDLRIGLPET KLGIMPGFGG SVRMPRMLGA DSALEIIAAG KDVGADQALK IGLIDGIVKA EKLRDGAISI LRQAINGDLD WKAKRQRKLE PLKLSKIEAT MSFTIAKGMV MQTAGKHYPA PITAVKTIEA AARLGREEAL KLENQSFVPL AHTNEARALV GIFLNDQFVK GKAKQLTKNV EMPKQAAVLG AGIMGGGIAY QSAWKGVPVI MKDINDKSLT LGMTEAAKLL NKQLERGKID GLKLSGVIST IHPTLEYSGF DRVDVVVEAV VENPKIKKAV LAETEDKVRP DTVLASNTST IPIGELASVL KRPENFCGMH FFNPVHRMPL VEVIRGEKTS DETIAKVVAW ASKMGKTPIV VNDCPGFFVN RVLFPYFAGF SQLLRDGADF RKVDKVMEKQ FGWPMGPAYL LDVVGIDTAH HAQAVMAAGF PQRMQKDYRD AIDALFDANR FGQKNGLGFW RYKEDSKGKP KKEDDTAVES LLADVSQPTR DFSDEEIIAR MMIPMVNEVV RCLEEGIIAS PAEADMALVY GLGFPPFHGG AFRWLDTLGS AKYLDMAQQY QQLGPLYEVP DGLRNKARHN EPYYPPVEPA RPVGALKTA //