CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010318
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Fatty acid oxidation complex subunit alpha 
Protein Synonyms/Alias
 Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase; 3-hydroxyacyl-CoA dehydrogenase 
Gene Name
 fadJ 
Gene Synonyms/Alias
 yfcX; b2341; JW2338 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
27TIDVPGEKMNTLKAEacetylation[1]
296FFASTDVKKDPGSDAacetylation[1]
350QGINHALKYSWDQLEacetylation[1]
359SWDQLEGKVRRRHLKacetylation[1]
475QTIATTVKLAKKQGKacetylation[1]
595QKGRKSKKQVDPAIYacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618] 
Functional Description
 Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities. Strongly involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate and weakly involved in the aerobic degradation of long-chain fatty acids. 
Sequence Annotation
 REGION 1 190 Enoyl-CoA hydratase.
 REGION 306 714 3-hydroxyacyl-CoA dehydrogenase.  
Keyword
 Complete proteome; Cytoplasm; Fatty acid metabolism; Isomerase; Lipid degradation; Lipid metabolism; Lyase; Multifunctional enzyme; NAD; Oxidoreductase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 714 AA 
Protein Sequence
MEMTSAFTLN VRLDNIAVIT IDVPGEKMNT LKAEFASQVR AIIKQLRENK ELRGVVFVSA 60
KPDNFIAGAD INMIGNCKTA QEAEALARQG QQLMAEIHAL PIQVIAAIHG ACLGGGLELA 120
LACHGRVCTD DPKTVLGLPE VQLGLLPGSG GTQRLPRLIG VSTALEMILT GKQLRAKQAL 180
KLGLVDDVVP HSILLEAAVE LAKKERPSSR PLPVRERILA GPLGRALLFK MVGKKTEHKT 240
QGNYPATERI LEVVETGLAQ GTSSGYDAEA RAFGELAMTP QSQALRSIFF ASTDVKKDPG 300
SDAPPAPLNS VGILGGGLMG GGIAYVTACK AGIPVRIKDI NPQGINHALK YSWDQLEGKV 360
RRRHLKASER DKQLALISGT TDYRGFAHRD LIIEAVFENL ELKQQMVAEV EQNCAAHTIF 420
ASNTSSLPIG DIAAHATRPE QVIGLHFFSP VEKMPLVEII PHAGTSAQTI ATTVKLAKKQ 480
GKTPIVVRDK AGFYVNRILA PYINEAIRML TQGERVEHID AALVKFGFPV GPIQLLDEVG 540
IDTGTKIIPV LEAAYGERFS APANVVSSIL NDDRKGRKNG RGFYLYGQKG RKSKKQVDPA 600
IYPLIGTQGQ GRISAPQVAE RCVMLMLNEA VRCVDEQVIR SVRDGDIGAV FGIGFPPFLG 660
GPFRYIDSLG AGEVVAIMQR LATQYGSRFT PCERLVEMGA RGESFWKTTA TDLQ 714 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:HAMAP.
 GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:HAMAP.
 GO:0004300; F:enoyl-CoA hydratase activity; IEA:HAMAP.
 GO:0051287; F:NAD binding; IEA:InterPro.
 GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway. 
Interpro
 IPR006180; 3-OHacyl-CoA_DH_CS.
 IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
 IPR006108; 3HC_DH_C.
 IPR008927; 6-PGluconate_DH_C-like.
 IPR001753; Crotonase_core_superfam.
 IPR013328; DH_multihelical.
 IPR012802; FadJ.
 IPR016040; NAD(P)-bd_dom. 
Pfam
 PF00725; 3HCDH
 PF02737; 3HCDH_N
 PF00378; ECH 
SMART
  
PROSITE
 PS00067; 3HCDH
 PS00166; ENOYL_COA_HYDRATASE 
PRINTS