CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009897
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Long-chain-fatty-acid--CoA ligase 
Protein Synonyms/Alias
 Long-chain acyl-CoA synthetase; Acyl-CoA synthetase 
Gene Name
 fadD 
Gene Synonyms/Alias
 oldD; b1805; JW1794 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
528LTGYKVPKLVEFRDEacetylation[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 esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. 
Sequence Annotation
 NP_BIND 213 224 ATP (Probable).  
Keyword
 ATP-binding; Complete proteome; Direct protein sequencing; Fatty acid metabolism; Ligase; Lipid metabolism; Membrane; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 561 AA 
Protein Sequence
MKKVWLNRYP ADVPTEINPD RYQSLVDMFE QSVARYADQP AFVNMGEVMT FRKLEERSRA 60
FAAYLQQGLG LKKGDRVALM MPNLLQYPVA LFGILRAGMI VVNVNPLYTP RELEHQLNDS 120
GASAIVIVSN FAHTLEKVVD KTAVQHVILT RMGDQLSTAK GTVVNFVVKY IKRLVPKYHL 180
PDAISFRSAL HNGYRMQYVK PELVPEDLAF LQYTGGTTGV AKGAMLTHRN MLANLEQVNA 240
TYGPLLHPGK ELVVTALPLY HIFALTINCL LFIELGGQNL LITNPRDIPG LVKELAKYPF 300
TAITGVNTLF NALLNNKEFQ QLDFSSLHLS AGGGMPVQQV VAERWVKLTG QYLLEGYGLT 360
ECAPLVSVNP YDIDYHSGSI GLPVPSTEAK LVDDDDNEVP PGQPGELCVK GPQVMLGYWQ 420
RPDATDEIIK NGWLHTGDIA VMDEEGFLRI VDRKKDMILV SGFNVYPNEI EDVVMQHPGV 480
QEVAAVGVPS GSSGEAVKIF VVKKDPSLTE ESLVTFCRRQ LTGYKVPKLV EFRDELPKSN 540
VGKILRRELR DEARGKVDNK A 561 
Gene Ontology
 GO:0005829; C:cytosol; TAS:EcoCyc.
 GO:0009898; C:internal side of plasma membrane; TAS:EcoCyc.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:EcoCyc.
 GO:0070538; F:oleic acid binding; IMP:EcoliWiki.
 GO:0006637; P:acyl-CoA metabolic process; IDA:EcoCyc.
 GO:0006635; P:fatty acid beta-oxidation; IDA:EcoCyc.
 GO:0008654; P:phospholipid biosynthetic process; IMP:EcoliWiki. 
Interpro
 IPR020845; AMP-binding_CS.
 IPR000873; AMP-dep_Synth/Lig.
 IPR025110; DUF4009. 
Pfam
 PF00501; AMP-binding
 PF13193; DUF4009 
SMART
  
PROSITE
 PS00455; AMP_BINDING 
PRINTS