CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005900
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Long-chain-fatty-acid--CoA ligase 1 
Protein Synonyms/Alias
 Fatty acid activator 1; Long-chain acyl-CoA synthetase 1 
Gene Name
 FAA1 
Gene Synonyms/Alias
 YOR317W; O6136 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
81VMKKVDGKETSVEKKubiquitination[1]
189SLLPSLIKPVQAAQDacetylation[2]
189SLLPSLIKPVQAAQDubiquitination[1, 3]
236KEVRPDIKTFSFDDIacetylation[2]
245FSFDDILKLGKESCNubiquitination[3]
261IDVHPPGKDDLCCIMubiquitination[1]
619KLGIMEQKDSSINIEubiquitination[1]
636LEDAKLIKAVYSDLLacetylation[2]
644AVYSDLLKTGKDQGLacetylation[2]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [3] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047] 
Functional Description
 Esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. It may supplement intracellular myristoyl-CoA pools from exogenous myristate. Preferentially acts on C12:0-C16:0 fatty acids with myristic and pentadecanic acid (C15:0) having the highest activities. 
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Direct protein sequencing; Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 700 AA 
Protein Sequence
MVAQYTVPVG KAANEHETAP RRNYQCREKP LVRPPNTKCS TVYEFVLECF QKNKNSNAMG 60
WRDVKEIHEE SKSVMKKVDG KETSVEKKWM YYELSHYHYN SFDQLTDIMH EIGRGLVKIG 120
LKPNDDDKLH LYAATSHKWM KMFLGAQSQG IPVVTAYDTL GEKGLIHSLV QTGSKAIFTD 180
NSLLPSLIKP VQAAQDVKYI IHFDSISSED RRQSGKIYQS AHDAINRIKE VRPDIKTFSF 240
DDILKLGKES CNEIDVHPPG KDDLCCIMYT SGSTGEPKGV VLKHSNVVAG VGGASLNVLK 300
FVGNTDRVIC FLPLAHIFEL VFELLSFYWG ACIGYATVKT LTSSSVRNCQ GDLQEFKPTI 360
MVGVAAVWET VRKGILNQID NLPFLTKKIF WTAYNTKLNM QRLHIPGGGA LGNLVFKKIR 420
TATGGQLRYL LNGGSPISRD AQEFITNLIC PMLIGYGLTE TCASTTILDP ANFELGVAGD 480
LTGCVTVKLV DVEELGYFAK NNQGEVWITG ANVTPEYYKN EEETSQALTS DGWFKTGDIG 540
EWEANGHLKI IDRKKNLVKT MNGEYIALEK LESVYRSNEY VANICVYADQ SKTKPVGIIV 600
PNHAPLTKLA KKLGIMEQKD SSINIENYLE DAKLIKAVYS DLLKTGKDQG LVGIELLAGI 660
VFFDGEWTPQ NGFVTSAQKL KRKDILNAVK DKVDAVYSSS 700 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IDA:SGD.
 GO:0005811; C:lipid particle; IDA:SGD.
 GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
 GO:0005886; C:plasma membrane; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:SGD.
 GO:0015909; P:long-chain fatty acid transport; IMP:SGD.
 GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IMP:SGD. 
Interpro
 IPR020845; AMP-binding_CS.
 IPR000873; AMP-dep_Synth/Lig. 
Pfam
 PF00501; AMP-binding 
SMART
  
PROSITE
 PS00455; AMP_BINDING 
PRINTS