ID FADB_SALTI STANDARD; PRT; 729 AA. AC Q8Z3C6; DT 15-JUN-2002 (Rel. 41, Created) DT 15-JUN-2002 (Rel. 41, Last sequence update) DT 15-JUN-2002 (Rel. 41, Last annotation update) DE Fatty oxidation complex alpha subunit [Includes: Enoyl-CoA hydratase DE (EC 4.2.1.17); Delta(3)-cis-delta(2)-trans-enoyl-CoA isomerase DE (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35); 3- DE hydroxybutyryl-CoA epimerase (EC 5.1.2.3)]. GN FADB OR STY3577. OS Salmonella typhi. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=601; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CT18; RX MEDLINE=21534947; PubMed=11677608; RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., RA Churcher C., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., RA Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J., RA Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., RA Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., RA Quail M., Rutherford K., Simmonds M., Skelton J., Stevens K., RA Whitehead S., Barrell B.G.; RT "Complete genome sequence of a multiple drug resistant Salmonella RT enterica serovar Typhi CT18."; RL Nature 413:848-852(2001). CC -!- FUNCTION: FadB and fadA are the alpha and beta subunits of the CC multifunctional enzyme complex of the fatty acid degradation CC cycle (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: 3-cis-dodecenoyl-CoA = 2-trans-dodecenoyl-CoA. CC -!- PATHWAY: Fatty acid beta-oxidation cycle; third step. CC -!- SUBUNIT: Tetramer of two alpha chains and two beta chains (By CC similarity). CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE 3- CC HYDROXYACYL-COA DEHYDROGENASE FAMILY. CC -!- SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO THE ENOYL-COA CC HYDRATASE/ISOMERASE FAMILY. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL627278; CAD07910.1; -. DR InterPro; IPR006108; 3HCDH_C. DR InterPro; IPR001753; EnCoA_hydrtse. DR Pfam; PF00725; 3HCDH; 2. DR Pfam; PF02737; 3HCDH_N; 1. DR Pfam; PF00378; ECH; 1. DR PROSITE; PS00067; 3HCDH; 1. DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1. KW Fatty acid metabolism; Multifunctional enzyme; Oxidoreductase; NAD; KW Lyase; Isomerase; Complete proteome. SQ SEQUENCE 729 AA; 79642 MW; C34C68ECFF35713C CRC64; MLYKGDTLYL DWLEDGIAEL VFDAPGSVNK LDTATVASLG QALEVLEKQH DLKGLLLRSN KAAFIVGADI TEFLSLFLVP EEQLSQWLHF ANSVFNRLED LPVPTLAAVN GYALGGGCEC VLATDYRLAT PDLRIGLPET KLGIMPGFGG SVRLPRMLGA DSALEIIAAG KDVGAEHALK IGLVDGVVKQ EKLIEGAIAV LRQAITGDLD WRAKRQPKLE PLKLSKIEAA MSFTIAKGMV AQTAGKHYPA PMTAVKTIEA AARFGREEAL NLENKSFVPL AHTNEARALV GIFLNDQYVK GKAKKLTKDI ETPKQAAVLG AGIMGGGIAY QSAWKGVPVI MKDINDKSLN LGMTEAAKLL NKQLERGKID GLKLAGVIST IHPTLDYAGF DRVDVVVEAV VENPKVKKAV LAETEQKVRP ETVLASNTST IPIGELASAL ERPENFCGMH FFNPVHRMPL VEIIRGEKSS DETIAKVVAW ASKMGKTPIV VNNCPGFFVN RVLFPYFAGF SQLLRDGADF RKVDKVMEKQ FGWPMGPAYL LDVVGIDTAH HAQAVMAAGF PQRMQKEYRD AIDALFDASR FGQKNGLGFW RYKEDSKGKP KKEEDAAVDD LLASVSQTKR DFSDDEIIAR MMIPMINEVV RCLEEGIIAS PAEADMALVY GLGFPPFHGG AFRWLDTQGS AKYLDMAQQY QHLGPLYEVP EGLRDKTRHN EPYYPPVEPA RPVGSLKTA //