ID A0A085A9M8_9ENTR Unreviewed; 716 AA. AC A0A085A9M8; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 02-DEC-2020, entry version 39. 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 ECO:0000313|EMBL:KFC06923.1}; GN ORFNames=GTGU_02248 {ECO:0000313|EMBL:KFC06923.1}; OS Trabulsiella guamensis ATCC 49490. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Trabulsiella. OX NCBI_TaxID=1005994 {ECO:0000313|EMBL:KFC06923.1, ECO:0000313|Proteomes:UP000028630}; RN [1] {ECO:0000313|EMBL:KFC06923.1, ECO:0000313|Proteomes:UP000028630} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49490 {ECO:0000313|EMBL:KFC06923.1, RC ECO:0000313|Proteomes:UP000028630}; RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.; RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of RT the evolutionary history of the Enterobacteriaceae."; RL Submitted (MAY-2014) 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: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:ARBA00001367, 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|ARBA:ARBA00008750, CC 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:KFC06923.1}. 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; JMTB01000075; KFC06923.1; -; Genomic_DNA. DR RefSeq; WP_038156749.1; NZ_JMTB01000075.1. DR STRING; 1005994.GTGU_02248; -. DR EnsemblBacteria; KFC06923; KFC06923; GTGU_02248. DR eggNOG; COG1024; Bacteria. DR eggNOG; COG1250; Bacteria. DR UniPathway; UPA00659; -. DR Proteomes; UP000028630; 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:0051287; 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; 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; 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; SSF48179; 2. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF52096; SSF52096; 1. DR TIGRFAMs; TIGR02440; FadJ; 1. DR PROSITE; PS00067; 3HCDH; 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|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01617, KW ECO:0000313|EMBL:KFC06923.1}; 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 ECO:0000313|EMBL:KFC06923.1}; 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, ECO:0000313|EMBL:KFC06923.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000028630}. FT DOMAIN 311..489 FT /note="3HCDH_N" FT /evidence="ECO:0000259|Pfam:PF02737" FT DOMAIN 492..586 FT /note="3HCDH" FT /evidence="ECO:0000259|Pfam:PF00725" FT DOMAIN 620..704 FT /note="3HCDH" FT /evidence="ECO:0000259|Pfam:PF00725" FT REGION 1..190 FT /note="Enoyl-CoA hydratase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01617" FT REGION 306..716 FT /note="3-hydroxyacyl-CoA dehydrogenase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01617" FT SITE 118 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01617" FT SITE 140 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01617" SQ SEQUENCE 716 AA; 77197 MW; C093D94133C75ECB CRC64; MTTTSAFTLE IRPDNVAVIA IDVPGEKMNT LKAEFGGQVR EILRQLRENK DLLGVVFISA KEDNFIAGAD INMIGNCKTA KEAEGLSTQG QQVMAEIHAL PFPVVAAIHG ACLGGGLELA LACHSRICTD DSKTVLGLPE VQLGLLPGSG GTQRLPRLIG VSTALEMILT GKQLRPRQAL KAGLVDDVVP HSILLDAAVE QVKKGKPDHR RLPVRERVLA GPLGRAVLFR IVGKKTEQKT QGNYPATERI LQVIETGLAQ GSRSGYEAEA RAFGELAMTP QSRALRSIFF ASTELKKDPG TSAEAGPLRT AGVLGGGLMG GGIAFVTACK GKLPVRIKDI NAKGINHALK YSWDLLDKKV RRRHIKASER DSQLALISGT TDYRGFSQRD VVIEAVFEDL ALKQQMVAEV EEQCAPHTVF ASNTSSLPIG DIAAGAQRPE QVIGLHFFSP VEKMPLVEVI PHAGTSARTI ATTVQLAKKQ GKTPIVVADK AGFYVNRILA PYINEAMRLL MEGQRIEFID HALVKYGFPV GPIQLLDEVG IDTGTKIIPV LEAAYGERFS PPANIISAIL NDDRKGRKNS RGFYLYAAKG RKSKKQPDPA IYSLVGITAA QSAISPQQAA ERCVMMMLNE AARCFDEGVV RSARDGDIGA VFGIGFPPFL GGPFRYMDSL GAGEVVAILQ RLAAQYGPRF TPCEPLLRMA EQGQTFWPVK ETDALS //