ID FADJ_PECAS Reviewed; 731 AA. AC Q6D2L7; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 27-MAR-2024, entry version 118. DE RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000255|HAMAP-Rule:MF_01617}; DE Includes: DE RecName: Full=Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase {ECO:0000255|HAMAP-Rule:MF_01617}; DE EC=4.2.1.17 {ECO:0000255|HAMAP-Rule:MF_01617}; DE EC=5.1.2.3 {ECO:0000255|HAMAP-Rule:MF_01617}; DE Includes: DE RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01617}; DE EC=1.1.1.35 {ECO:0000255|HAMAP-Rule:MF_01617}; GN Name=fadJ {ECO:0000255|HAMAP-Rule:MF_01617}; GN OrderedLocusNames=ECA3078; OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia OS carotovora subsp. atroseptica). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Pectobacteriaceae; Pectobacterium. OX NCBI_TaxID=218491; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCRI 1043 / ATCC BAA-672; RX PubMed=15263089; DOI=10.1073/pnas.0402424101; RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J., RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K., RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J., RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H., RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S., RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.; RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora RT subsp. atroseptica and characterization of virulence factors."; RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004). CC -!- FUNCTION: Catalyzes the formation of a hydroxyacyl-CoA by addition of CC water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- CC hydroxyacyl-CoA dehydrogenase activities. {ECO:0000255|HAMAP- CC Rule:MF_01617}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O; CC Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318, CC ChEBI:CHEBI:58856; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01617}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O; CC Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521, CC ChEBI:CHEBI:137480; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01617}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + CC NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01617}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA; CC Xref=Rhea:RHEA:21760, ChEBI:CHEBI:57315, ChEBI:CHEBI:57316; CC EC=5.1.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01617}; CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC {ECO:0000255|HAMAP-Rule:MF_01617}. CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadJ) and two beta chains CC (FadI). {ECO:0000255|HAMAP-Rule:MF_01617}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01617}. CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA CC hydratase/isomerase family. {ECO:0000255|HAMAP-Rule:MF_01617}. CC -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA CC dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_01617}. 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; BX950851; CAG75977.1; -; Genomic_DNA. DR RefSeq; WP_011094602.1; NC_004547.2. DR AlphaFoldDB; Q6D2L7; -. DR SMR; Q6D2L7; -. DR STRING; 218491.ECA3078; -. DR KEGG; eca:ECA3078; -. DR PATRIC; fig|218491.5.peg.3111; -. DR eggNOG; COG1024; Bacteria. DR eggNOG; COG1250; Bacteria. DR HOGENOM; CLU_009834_16_1_6; -. DR OrthoDB; 5389341at2; -. DR UniPathway; UPA00659; -. DR Proteomes; UP000007966; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-UniRule. DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro. DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway. DR CDD; cd06558; crotonase-like; 1. DR Gene3D; 1.10.1040.50; -; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_01617; FadJ; 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-like_C_sf. DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf. DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS. DR InterPro; IPR001753; Enoyl-CoA_hydra/iso. DR InterPro; IPR012802; FadJ. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR02440; FadJ; 1. DR PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 1. DR PANTHER; PTHR43612:SF3; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL; 1. DR Pfam; PF00725; 3HCDH; 2. DR Pfam; PF02737; 3HCDH_N; 1. DR Pfam; PF00378; ECH_1; 1. DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2. DR SUPFAM; SSF52096; ClpP/crotonase; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00067; 3HCDH; 1. DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1. PE 3: Inferred from homology; KW Cytoplasm; Fatty acid metabolism; Isomerase; Lipid degradation; KW Lipid metabolism; Lyase; Multifunctional enzyme; NAD; Oxidoreductase; KW Reference proteome. FT CHAIN 1..731 FT /note="Fatty acid oxidation complex subunit alpha" FT /id="PRO_0000109297" FT REGION 15..204 FT /note="Enoyl-CoA hydratase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617" FT REGION 320..729 FT /note="3-hydroxyacyl-CoA dehydrogenase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617" FT SITE 132 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617" FT SITE 154 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617" SQ SEQUENCE 731 AA; 80047 MW; DAAB4DA0B42ECCB3 CRC64; MNDQQPFSVT ASPTTEKTSA FSLTIRPDNI GVISIDVPGE RVNTLKSEFA EQILSVFELA RQHATLRGLI FISAKPDSFI AGADITMLNK CSSAEQAENL AKQGQETFDQ IAALPFPVVA AIHGACLGGG LELALACDYR VCSLDEKTVL GLPEVQLGLL PGSGGTQRLP RLIGLDSALD LILTGRHLRA GQALRQGLVD EAVPHDILLD TAVEILKKGK RKAVPLGWRS RLLNSPGIRH LLFKMVKRKT RAKTHGNYPA TEKIIQVVRR GIEKGREEGY RHEARAFGKL VMTPESAALR HLFFATNALK KTSGAASEAK PIHRVGILGG GLMGGGIASV TATRGQLPVR IKDINEQGIN HALKYNWQLL TKRVQSKRMK PTERQRLMTL ISGSTDYRGF EHADIVIEAV FEDLALKRQM ITEIEDHAAP HTIFASNTSS LPIHQIAEGA RRPQLVVGLH YFSPVDKMPL VEVIPHAHTS AETVATTVAL ARKQGKTAIV VGDSAGFYVN RILAPYINEA AYCLLEGEPI ESIDYALVRF GFPVGPLALL DEVGIDVATK IVPVLSEELG DRFTSPPAFD AILKDGRKGR KNGKGFYRYN KTRRFWHSGK EVDSSVYPLL DVTPKAHIDP ALISQRAVMM MLNEAARCLD EGVIQCARDG DIGAVFGIGF PPFLGGPFHY MDRLGMETVV KTLLVLQQQY GDRFAPCERL LTMREGQRTF YPPADKDNSI S //