ID FADB_SALTI Reviewed; 729 AA. AC Q8Z3C6; DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 29-APR-2015, entry version 97. DE RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000255|HAMAP-Rule:MF_01621}; DE Includes: DE RecName: Full=Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase {ECO:0000255|HAMAP-Rule:MF_01621}; DE EC=4.2.1.17 {ECO:0000255|HAMAP-Rule:MF_01621}; DE EC=5.1.2.3 {ECO:0000255|HAMAP-Rule:MF_01621}; DE EC=5.3.3.8 {ECO:0000255|HAMAP-Rule:MF_01621}; DE Includes: DE RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01621}; DE EC=1.1.1.35 {ECO:0000255|HAMAP-Rule:MF_01621}; GN Name=fadB {ECO:0000255|HAMAP-Rule:MF_01621}; GN OrderedLocusNames=STY3577, t3315; OS Salmonella typhi. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=90370; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CT18; RX PubMed=11677608; DOI=10.1038/35101607; RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., RA Churcher C.M., 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.A., Rutherford K.M., 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). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700931 / Ty2; RX PubMed=12644504; DOI=10.1128/JB.185.7.2330-2337.2003; RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., RA Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.; RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 RT and CT18."; RL J. Bacteriol. 185:2330-2337(2003). CC -!- FUNCTION: Involved in the aerobic and anaerobic degradation of CC long-chain fatty acids via beta-oxidation cycle. Catalyzes the CC formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. CC It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as CC substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. CC -!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA CC + NADH. {ECO:0000255|HAMAP-Rule:MF_01621}. CC -!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl- CC CoA + H(2)O. {ECO:0000255|HAMAP-Rule:MF_01621}. CC -!- CATALYTIC ACTIVITY: (S)-3-hydroxybutanoyl-CoA = (R)-3- CC hydroxybutanoyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01621}. CC -!- CATALYTIC ACTIVITY: (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl- CC CoA. {ECO:0000255|HAMAP-Rule:MF_01621}. CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC {ECO:0000255|HAMAP-Rule:MF_01621}. CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta CC chains (FadA). {ECO:0000255|HAMAP-Rule:MF_01621}. CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA CC hydratase/isomerase family. {ECO:0000255|HAMAP-Rule:MF_01621}. CC -!- SIMILARITY: In the C-terminal section; belongs to the 3- CC hydroxyacyl-CoA dehydrogenase family. {ECO:0000255|HAMAP- CC Rule:MF_01621}. 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; AL513382; CAD07910.1; -; Genomic_DNA. DR EMBL; AE014613; AAO70843.1; -; Genomic_DNA. DR RefSeq; NP_457769.1; NC_003198.1. DR RefSeq; NP_806983.1; NC_004631.1. DR ProteinModelPortal; Q8Z3C6; -. DR SMR; Q8Z3C6; 1-714. DR STRING; 220341.STY3577; -. DR EnsemblBacteria; AAO70843; AAO70843; t3315. DR EnsemblBacteria; CAD07910; CAD07910; CAD07910. DR GeneID; 1249832; -. DR KEGG; sty:STY3577; -. DR PATRIC; 18545260; VBISalEnt120419_3644. DR eggNOG; COG1250; -. DR HOGENOM; HOG000261344; -. DR KO; K01825; -. DR OMA; NPIVVND; -. DR OrthoDB; EOG6M9F0M; -. DR UniPathway; UPA00659; -. DR Proteomes; UP000000541; Chromosome. DR Proteomes; UP000002670; Chromosome. DR GO; GO:0036125; C:fatty acid beta-oxidation multienzyme complex; IEA:InterPro. DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.1040.10; -; 2. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.226.10; -; 2. DR HAMAP; MF_01621; FadB; 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; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR013328; 6PGD_dom_2. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR001753; Crotonase_core_superfam. DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS. DR InterPro; IPR012799; FadB. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00725; 3HCDH; 2. DR Pfam; PF02737; 3HCDH_N; 1. DR Pfam; PF00378; ECH; 1. DR SUPFAM; SSF48179; SSF48179; 2. DR SUPFAM; SSF52096; SSF52096; 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_0000109286. FT NP_BIND 400 402 NAD. {ECO:0000255|HAMAP-Rule:MF_01621}. FT NP_BIND 427 429 NAD. {ECO:0000255|HAMAP-Rule:MF_01621}. FT REGION 1 189 Enoyl-CoA hydratase/isomerase. FT {ECO:0000255|HAMAP-Rule:MF_01621}. FT REGION 311 729 3-hydroxyacyl-CoA dehydrogenase. FT {ECO:0000255|HAMAP-Rule:MF_01621}. FT ACT_SITE 450 450 For 3-hydroxyacyl-CoA dehydrogenase FT activity. {ECO:0000255|HAMAP- FT Rule:MF_01621}. FT BINDING 296 296 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01621}. FT BINDING 324 324 NAD; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01621}. FT BINDING 343 343 NAD. {ECO:0000255|HAMAP-Rule:MF_01621}. FT BINDING 407 407 NAD. {ECO:0000255|HAMAP-Rule:MF_01621}. FT BINDING 453 453 NAD. {ECO:0000255|HAMAP-Rule:MF_01621}. FT BINDING 500 500 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01621}. FT BINDING 660 660 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01621}. FT SITE 119 119 Important for catalytic activity. FT {ECO:0000255|HAMAP-Rule:MF_01621}. FT SITE 139 139 Important for catalytic activity. FT {ECO:0000255|HAMAP-Rule:MF_01621}. 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 //