ID FADJ_ECO57 Reviewed; 714 AA. AC Q8XCP2; Q7ABX5; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 04-NOV-2026, entry version 150. 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=Z3604, ECs3224; OS Escherichia coli O157:H7. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83334; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; RX PubMed=11206551; DOI=10.1038/35054089; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J., RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., RA Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC; RX PubMed=11258796; DOI=10.1093/dnares/8.1.11; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S., RA Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and RT genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(2001). 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 + NADH + CC H(+); 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; AE005174; AAG57469.1; -; Genomic_DNA. DR EMBL; BA000007; BAB36647.1; -; Genomic_DNA. DR PIR; A85876; A85876. DR PIR; H91031; H91031. DR RefSeq; NP_311251.1; NC_002695.2. DR RefSeq; WP_000426148.1; NZ_CP012802.1. DR AlphaFoldDB; Q8XCP2; -. DR SMR; Q8XCP2; -. DR STRING; 155864.Z3604; -. DR GeneID; 915679; -. DR KEGG; ece:Z3604; -. DR KEGG; ecs:ECs_3224; -. DR PATRIC; fig|386585.9.peg.3366; -. DR eggNOG; COG1024; Bacteria. DR eggNOG; COG1250; Bacteria. DR HOGENOM; CLU_009834_16_1_6; -. DR OMA; AACHHAQ; -. DR UniPathway; UPA00659; -. DR Proteomes; UP000000558; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0018812; F:3-hydroxyacyl-CoA dehydratase activity; IEA:RHEA. DR GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016509; F:long-chain (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity; IEA:TreeGrafter. DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro. DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniRule. DR CDD; cd06558; crotonase-like; 1. DR FunFam; 1.10.1040.50:FF:000003; Fatty acid oxidation complex subunit alpha; 1. DR FunFam; 3.90.226.10:FF:000011; Fatty acid oxidation complex subunit alpha; 1. DR FunFam; 3.40.50.720:FF:000009; Fatty oxidation complex, alpha subunit; 1. DR Gene3D; 1.10.1040.50; -; 1. DR Gene3D; 3.90.226.10; 2-enoyl-CoA Hydratase, Chain A, domain 1; 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; IPR001753; Enoyl-CoA_hydra/iso. DR InterPro; IPR050136; FA_oxidation_alpha_subunit. DR InterPro; IPR012802; FadJ. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR NCBIfam; TIGR02440; FadJ; 1. DR NCBIfam; NF008363; 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. 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..714 FT /note="Fatty acid oxidation complex subunit alpha" FT /id="PRO_0000109299" FT REGION 1..190 FT /note="Enoyl-CoA hydratase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617" FT REGION 306..714 FT /note="3-hydroxyacyl-CoA dehydrogenase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617" FT SITE 118 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617" FT SITE 140 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617" SQ SEQUENCE 714 AA; 76983 MW; D164EE27CE22CC35 CRC64; MEMTSAFTLN VRLDNIAIIT IDVPGEKMNT LKAEFASQVR AIIKQLRENK ELRGVVFVSA KPDNFIAGAD INMIGNCKTA QEAEALARQG QQLMAEIHAL PIPVIAAIHG ACLGGGLELA LACHGRVCTD DPKTVLGLPE VQLGLLPGSG GTQRLPRLIG VSTALEMILT GKQLRAKQAL KLGLVDDVVP HSILLEAAVE LAKKDRPSSR PLPVRERILA GPLGRAQLFK MVGKKTEHKT QGNYPATERI LEVVETGLAQ GTSSGYDAEA RAFGELAMTP QSQALRSIFF ASTEVKKDPG SDAPPAPLNS VGILGGGLMG GGIAYVTACK AGIPVRIKDI NPQGINHALK YSWDQLEGKV RRRHLKASER DKQLALISGT TDYRGFAHRD LIIEAVFENL ELKQQMVAEV EQNCAAHTIF ASNTSSLPIG DIAAHATRPE QVIGLHFFSP VEKMPLVEII PHAGTSAQTI ATTVKLAKKQ GKTPIVVRDK AGFYVNRILA PYINEAIRML TEGERVAHID AALVKFGFPV GPIQLLDEVG IDTGTKIIPV LEAAYGERFS APANVVSSIL NDDRKGRKNG RGFYLYGQKG RKSKKQVDPA IYPLIGAQGQ GRLSAPQVAE RCVMLMLNEA VRCVDEQVIR SVRDGDIGAV FGIGFPPFLG GPFRYIDSLG AGEVVAIMQR LATQYGSRFT PCERLVEMGA RGESFWKTTA TDLQ //