ID F7RQE3_9GAMM Unreviewed; 708 AA. AC F7RQE3; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-DEC-2022, entry version 63. DE RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000256|HAMAP-Rule:MF_01617}; DE Includes: DE RecName: Full=Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase {ECO:0000256|HAMAP-Rule:MF_01617}; DE EC=4.2.1.17 {ECO:0000256|HAMAP-Rule:MF_01617}; DE EC=5.1.2.3 {ECO:0000256|HAMAP-Rule:MF_01617}; DE Includes: DE RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01617}; DE EC=1.1.1.35 {ECO:0000256|HAMAP-Rule:MF_01617}; GN Name=fadJ {ECO:0000256|HAMAP-Rule:MF_01617}; GN ORFNames=SOHN41_02592 {ECO:0000313|EMBL:EGM69502.1}; OS Shewanella sp. HN-41. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=327275 {ECO:0000313|EMBL:EGM69502.1, ECO:0000313|Proteomes:UP000002956}; RN [1] {ECO:0000313|EMBL:EGM69502.1, ECO:0000313|Proteomes:UP000002956} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HN-41 {ECO:0000313|EMBL:EGM69502.1, RC ECO:0000313|Proteomes:UP000002956}; RX PubMed=21868804; DOI=10.1128/JB.05578-11; RA Kim D.H., Jiang S., Lee J.H., Cho Y.J., Chun J., Choi S.H., Park H.S., RA Hur H.G.; RT "Draft Genome Sequence of Shewanella sp. Strain HN-41, Which Produces RT Arsenic-Sulfide Nanotubes."; RL J. Bacteriol. 193:5039-5040(2011). 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:0000256|HAMAP- CC 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:0000256|HAMAP-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:0000256|ARBA:ARBA00023693, ECO:0000256|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:0000256|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:0000256|HAMAP- CC Rule:MF_01617}; CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC {ECO:0000256|ARBA:ARBA00005005, ECO:0000256|HAMAP-Rule:MF_01617}. CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadJ) and two beta chains CC (FadI). {ECO:0000256|HAMAP-Rule:MF_01617}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01617}. CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA CC hydratase/isomerase family. {ECO:0000256|HAMAP-Rule:MF_01617}. CC -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA CC dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_01617}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EGM69502.1}. 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; AFOZ01000031; EGM69502.1; -; Genomic_DNA. DR RefSeq; WP_007649402.1; NZ_AFOZ01000031.1. DR AlphaFoldDB; F7RQE3; -. DR STRING; 327275.SOHN41_02592; -. DR EnsemblBacteria; EGM69502; EGM69502; SOHN41_02592. DR UniPathway; UPA00659; -. DR Proteomes; UP000002956; Unassembled WGS sequence. 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 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 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 TIGRFAMs; TIGR02440; FadJ; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01617}; KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP- KW Rule:MF_01617}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01617, ECO:0000313|EMBL:EGM69502.1}; KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, ECO:0000256|HAMAP- KW Rule:MF_01617}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP- KW Rule:MF_01617}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01617}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP- KW Rule:MF_01617}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01617}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01617}. FT DOMAIN 313..491 FT /note="3HCDH_N" FT /evidence="ECO:0000259|Pfam:PF02737" FT DOMAIN 494..587 FT /note="3HCDH" FT /evidence="ECO:0000259|Pfam:PF00725" FT DOMAIN 620..705 FT /note="3HCDH" FT /evidence="ECO:0000259|Pfam:PF00725" FT REGION 1..188 FT /note="Enoyl-CoA hydratase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01617" FT REGION 308..708 FT /note="3-hydroxyacyl-CoA dehydrogenase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01617" FT SITE 116 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01617" FT SITE 138 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01617" SQ SEQUENCE 708 AA; 76271 MW; 2E5A2019A2EADCE2 CRC64; MEKTFNLTRR DDGIAILTMD VPGETMNTLK AQFGPEISEI LAEIKRDSSI RGLVLISGKK DSFVAGADIS MLDACKTASD AKALSQQGHV VFNELEALTI PVVAAIHGAC LGGGLELALA CHQRVCSDDG KTMLGVPEVQ LGLLPGGGGT QRLPRLVGIT TALDMMLTGK QIRPKQALKM GLVNDVVPQT ILLQTAVEMA LAGKRASKPI KKSLVNQVLE GTSFGRNIIF DQATKQVEKK TQGNYPAPAK IIDCVRQGIA KGMQKGLEVE ASHFAELVIS KESEALRSIF FATTEMKKET GAEGATPRKV KKAVILGGGL MGGGIASVTT TKAKIPARVK DINEKGLSNA LAYAYKLLDK GVKRRHMTPA ARDNLMALMT TTTEYKGVKD ADIVVEAVFE DLALKHQMVK DIERECGEHT IFASNTSSLP ISQIAEAATR PENVIGLHYF SPVEKMPLVE VIAHAKTSPE TIATTVAFAR KQGKTPIVVQ DGAGFYVNRI LALYMNEAAQ LLLEGQSVEH LDKALVKFGF PVGPITLLDE VGIDVGAKIS PILEKELGER FKAPAAFDKL LGDDRKGRKN GKGFYQYGQK DSSKKAKVVD ESVYGVLGIK PGTNKDAKAV AERCVVQMLN EAVRCLDEGI IASPRDGDIG AIFGIGFPPF LGGPFHYIDT LGAANLVRIL EGYQSQLGDR FEPCERLKAM AQENRRFF //