ID A0A085A9M8_9ENTR Unreviewed; 716 AA. AC A0A085A9M8; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 27-MAY-2015, entry version 7. DE RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000256|HAMAP-Rule:MF_01617, ECO:0000256|SAAS:SAAS00051619}; 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; Enterobacteriales; OC Enterobacteriaceae; Trabulsiella. OX NCBI_TaxID=1005994 {ECO:0000313|EMBL:KFC06923.1}; RN [1] {ECO:0000313|EMBL:KFC06923.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=ATCC 49490 {ECO:0000313|EMBL:KFC06923.1}; RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.; RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction RT of 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 CC of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase CC and 3-hydroxyacyl-CoA dehydrogenase activities. CC {ECO:0000256|HAMAP-Rule:MF_01617}. CC -!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl- CC CoA + H(2)O. {ECO:0000256|HAMAP-Rule:MF_01617, CC ECO:0000256|SAAS:SAAS00079495}. CC -!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA CC + NADH. {ECO:0000256|HAMAP-Rule:MF_01617, CC ECO:0000256|SAAS:SAAS00080685}. CC -!- CATALYTIC ACTIVITY: (S)-3-hydroxybutanoyl-CoA = (R)-3- CC hydroxybutanoyl-CoA. {ECO:0000256|HAMAP-Rule:MF_01617, CC ECO:0000256|SAAS:SAAS00051638}. CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC {ECO:0000256|HAMAP-Rule:MF_01617, ECO:0000256|SAAS:SAAS00079424}. CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadJ) and two beta CC chains (FadI). {ECO:0000256|HAMAP-Rule:MF_01617, CC ECO:0000256|SAAS:SAAS00051625}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01617, CC ECO:0000256|SAAS:SAAS00051632}. 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- CC CoA dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_01617}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 EnsemblBacteria; KFC06923; KFC06923; GTGU_02248. DR UniPathway; UPA00659; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.1040.10; -; 2. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.226.10; -; 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_C-like. DR InterPro; IPR013328; 6PGD_dom_2. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR001753; Crotonase_core_superfam. DR InterPro; IPR012802; FadJ. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00725; 3HCDH; 2. DR Pfam; PF02737; 3HCDH_N; 1. DR Pfam; PF00378; ECH; 1. DR SUPFAM; SSF48179; SSF48179; 2. DR SUPFAM; SSF52096; SSF52096; 1. DR TIGRFAMs; TIGR02440; FadJ; 1. DR PROSITE; PS00067; 3HCDH; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01617, KW ECO:0000256|SAAS:SAAS00051630}; KW Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01617, KW ECO:0000256|SAAS:SAAS00080774}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01617, KW ECO:0000256|SAAS:SAAS00079503}; KW Lipid degradation {ECO:0000256|HAMAP-Rule:MF_01617, KW ECO:0000256|SAAS:SAAS00051618}; KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01617, KW ECO:0000256|SAAS:SAAS00080724}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01617, KW ECO:0000256|SAAS:SAAS00079415}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01617, KW ECO:0000256|SAAS:SAAS00079419}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01617, ECO:0000256|SAAS:SAAS00080806}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01617, KW ECO:0000256|SAAS:SAAS00079460}. FT REGION 1 190 Enoyl-CoA hydratase. {ECO:0000256|HAMAP- FT Rule:MF_01617}. FT REGION 306 716 3-hydroxyacyl-CoA dehydrogenase. FT {ECO:0000256|HAMAP-Rule:MF_01617}. FT SITE 118 118 Important for catalytic activity. FT {ECO:0000256|HAMAP-Rule:MF_01617}. FT SITE 140 140 Important for catalytic activity. FT {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 //