ID FADJ_PHOPR Reviewed; 715 AA. AC Q6LTK3; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 28-JAN-2026, entry version 124. 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=PBPRA0962; OS Photobacterium profundum (strain SS9). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=298386; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1253 / SS9; RX PubMed=15746425; DOI=10.1126/science.1103341; RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M., RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C., RA Bartlett D.H., Valle G.; RT "Life at depth: Photobacterium profundum genome sequence and expression RT analysis."; RL Science 307:1459-1461(2005). 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; CR378666; CAG19373.1; -; Genomic_DNA. DR RefSeq; WP_011217707.1; NC_006370.1. DR AlphaFoldDB; Q6LTK3; -. DR SMR; Q6LTK3; -. DR STRING; 298386.PBPRA0962; -. DR KEGG; ppr:PBPRA0962; -. DR eggNOG; COG1024; Bacteria. DR eggNOG; COG1250; Bacteria. DR HOGENOM; CLU_009834_16_1_6; -. DR UniPathway; UPA00659; -. DR Proteomes; UP000000593; Chromosome 1. 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; 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; PRK11154.1; 1. DR PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 1. DR PANTHER; PTHR43612:SF3; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL; 1. DR Pfam; PF00725; 3HCDH; 1. 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..715 FT /note="Fatty acid oxidation complex subunit alpha" FT /id="PRO_0000109302" FT REGION 8..197 FT /note="Enoyl-CoA hydratase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617" FT REGION 313..715 FT /note="3-hydroxyacyl-CoA dehydrogenase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617" FT SITE 125 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617" FT SITE 147 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617" SQ SEQUENCE 715 AA; 77342 MW; BEDB6D9C220C07A5 CRC64; MTQHESANSQ PSAFSLTFGD NGVAWLKIDV PNERMNTLQS AFVDQVTDVL AQLKDKKDIK GMVVYSGKPD NFIAGADIRM LAACQTADEA QQLAAKGQEL FGQLEALPFH VVAAIHGPCL GGGLELALAC HSRVCSDDDK TRLGLPEVQL GLLPGSGGTQ RLPRLIGVAN ALDMILTGKQ LRAKKAKNLG LVEEAVPLSI LLDIAEKQAL KGKPKRKGSF QEWAMGGNAL GRSVVFDQAA KKTHEKTRGN YPAADAILDV IKYGLQHGMK KGLDQEAKRF GELVMTSESA ALRSIFFATT AMKKESGSDA LPATIKKVGV LGGGLMGGGI SHVTATKAGY PVRIKDISND GIKNALVYNF KLLDKQRKRR IISKAELQNK MFSITGGTTF TGFTNVDVVI EAVFEDINLK HQMVKDIEQQ TSDYTIFASN TSSLPIHQIA AAAERPENVV GLHYFSPVEK MPLVEVIPHQ GTENGSATSE QTIATVVALA KKQGKTPIVV ADKAGFYVNR ILAPYMNEAA AVLLSGEPIE HIDRSLLDFG FPVGPITLLD EVGVDIGAKI SPILLAELGE RFKAPDVFDL LLSDDRKGRK SGKGFYLYNT KKKEVDKSVY KLLSLEPEQK AAGQDIALRC TLMMLNEAAR CLDEGVIKSA RDGDIGAIFG IGFPPFLGGP FRYMDTLGAK RVVEMLKDHT DKYGGRFTPC DKLVAMANEE QSFYS //