CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009319
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lipoyl synthase 
Protein Synonyms/Alias
 Lip-syn; LS; Lipoate synthase; Lipoic acid synthase; Sulfur insertion protein LipA 
Gene Name
 lipA 
Gene Synonyms/Alias
 RPA2587 
Created Date
 July 27, 2013 
Organism
 Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) 
NCBI Taxa ID
 258594 
Lysine Modification
Position
Peptide
Type
References
97ACAFCNVKTGMPGALacetylation[1]
Reference
 [1] System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases.
 Crosby HA, Pelletier DA, Hurst GB, Escalante-Semerena JC.
 J Biol Chem. 2012 May 4;287(19):15590-601. [PMID: 22416131] 
Functional Description
 Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives (By similarity). 
Sequence Annotation
 METAL 61 61 Iron-sulfur 1 (4Fe-4S) (By similarity).
 METAL 66 66 Iron-sulfur 1 (4Fe-4S) (By similarity).
 METAL 72 72 Iron-sulfur 1 (4Fe-4S) (By similarity).
 METAL 87 87 Iron-sulfur 2 (4Fe-4S-S-AdoMet) (By
 METAL 91 91 Iron-sulfur 2 (4Fe-4S-S-AdoMet) (By
 METAL 94 94 Iron-sulfur 2 (4Fe-4S-S-AdoMet) (By  
Keyword
 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; Metal-binding; S-adenosyl-L-methionine; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 319 AA 
Protein Sequence
MVVLVDTVSA NPVRPRHPEK AARPDALSPK KPDWIRVRAP TTRGYGETRG IVKENGLHTV 60
CEEAGCPNIG ECWDKKHATF MIMGDTCTRA CAFCNVKTGM PGALDANEPA YVAEATRKLG 120
LQHLVITSVD RDDLADGGAA HFAATIRAVR EACPTTTIEI LTPDFLRKDG ALEVVVAAKP 180
DVFNHNLETV PSRYLSVRPG ARYFHSIRLL QRVKELDPSI FTKSGIMVGL GEERHEVLQV 240
MDDLRSAEVD FLTIGQYLQP TRKHHAVMRY VTPDEFAGYQ TTAYAKGFLM VSASPMTRSS 300
HHAGDDFAKL KAARAARAR 319 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:HAMAP.
 GO:0016992; F:lipoate synthase activity; IEA:HAMAP.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0009249; P:protein lipoylation; IEA:HAMAP. 
Interpro
 IPR013785; Aldolase_TIM.
 IPR006638; Elp3/MiaB/NifB.
 IPR003698; Lipoyl_synth.
 IPR007197; rSAM. 
Pfam
 PF04055; Radical_SAM 
SMART
 SM00729; Elp3 
PROSITE
  
PRINTS