ID FADJ_SHEAM Reviewed; 706 AA. AC A1S7L6; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 100. 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=Sama_2167; OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=326297; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1098 / SB2B; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J., RA Richardson P.; RT "Complete sequence of Shewanella amazonensis SB2B."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000507; ABM00373.1; -; Genomic_DNA. DR RefSeq; WP_011760280.1; NC_008700.1. DR AlphaFoldDB; A1S7L6; -. DR SMR; A1S7L6; -. DR STRING; 326297.Sama_2167; -. DR KEGG; saz:Sama_2167; -. DR eggNOG; COG1024; Bacteria. DR eggNOG; COG1250; Bacteria. DR HOGENOM; CLU_009834_16_1_6; -. DR OrthoDB; 5389341at2; -. DR UniPathway; UPA00659; -. DR Proteomes; UP000009175; 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; 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; 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. 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..706 FT /note="Fatty acid oxidation complex subunit alpha" FT /id="PRO_0000323525" FT REGION 1..188 FT /note="Enoyl-CoA hydratase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617" FT REGION 308..706 FT /note="3-hydroxyacyl-CoA dehydrogenase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617" FT SITE 116 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617" FT SITE 138 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01617" SQ SEQUENCE 706 AA; 75699 MW; C724364647D18D6F CRC64; MEKTFSLSRR DDGIALLTMD VPGETMNTLK AQFAPEITAI LQEIKADSSI KGLVLISGKA DSFVAGADIS MLDACETAED ARLLSRQGHH VFAELEGLNI PVVAAIHGAC LGGGLELALA CHQRVCSDSS KTMLGVPEVQ LGLLPGGGGT QRLPRLIGIA KALDLMLTGK QVRPKQAVKM GLVDDVVPES ILLDTAIEMA LAGKKTRKPL KQPLVTKLLE GTPVGRNIMF DQATKQVLKK TQGNYPSPLK IIDCVREGMA KGMEKGLEVE AAHFGALVAT PESAALRSIF FATTEMKKET GAGDAKPRKV AKAVVLGGGL MGGGIASVTT TKAKVPVRVK DISDKGLSNA LGYAYKLLDK GVKRRHMTSA ERDKLMALMT TTTEYRGVKD ADIVVEAVFE DLNLKHQMVR DIERECGEHT IFASNTSSLP ITQIAAAASR PENVIGLHYF SPVEKMPLVE VIAHEKTSPE TIATTVAFAR KQGKTPIVVK DCAGFYVNRI LALYMNEAAQ LLLEGQAVDH LDKALVKFGF PVGPMTLLDE VGIDVGAKIS PILEKELGER FKAPAAFDKL MADDRKGRKN GKGFYLYGKA AKKGKKVDES VYSLLGLTPA TGKEAGEIAE RCVVQMLNEA VRCLEEGIIA SPRDGDIGAI FGIGFPPFLG GPFRYMDTLG AAKMVRLLEG YQSKYGDRFA PAALLKAMAA EGKTFY //