CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004015
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Molybdopterin molybdenumtransferase 
Protein Synonyms/Alias
 MPT Mo-transferase 
Gene Name
 moeA 
Gene Synonyms/Alias
 bisB; chlE; narE; b0827; JW0811 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
79QPLPVAGKSFAGQPYacetylation[1]
279AFWKLAIKPGKPFAFacetylation[1, 2]
282KLAIKPGKPFAFGKLacetylation[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]
 [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111
Functional Description
 Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. 
Sequence Annotation
  
Keyword
 3D-structure; Complete proteome; Magnesium; Metal-binding; Molybdenum; Molybdenum cofactor biosynthesis; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 411 AA 
Protein Sequence
MEFTTGLMSL DTALNEMLSR VTPLTAQETL PLVQCFGRIL ASDVVSPLDV PGFDNSAMDG 60
YAVRLADIAS GQPLPVAGKS FAGQPYHGEW PAGTCIRIMT GAPVPEGCEA VVMQEQTEQM 120
DNGVRFTAEV RSGQNIRRRG EDISAGAVVF PAGTRLTTAE LPVIASLGIA EVPVIRKVRV 180
ALFSTGDELQ LPGQPLGDGQ IYDTNRLAVH LMLEQLGCEV INLGIIRDDP HALRAAFIEA 240
DSQADVVISS GGVSVGEADY TKTILEELGE IAFWKLAIKP GKPFAFGKLS NSWFCGLPGN 300
PVSATLTFYQ LVQPLLAKLS GNTASGLPAR QRVRTASRLK KTPGRLDFQR GVLQRNADGE 360
LEVTTTGHQG SHIFSSFSLG NCFIVLERDR GNVEVGEWVE VEPFNALFGG L 411 
Gene Ontology
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
 GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IMP:EcoCyc. 
Interpro
 IPR020817; Mo_cofactor_synthesis.
 IPR008284; MoCF_biosynth_CS.
 IPR005111; MoeA_C_domain_IV.
 IPR005110; MoeA_linker/N.
 IPR001453; Mopterin-bd_dom. 
Pfam
 PF00994; MoCF_biosynth
 PF03454; MoeA_C
 PF03453; MoeA_N 
SMART
 SM00852; MoCF_biosynth 
PROSITE
 PS01079; MOCF_BIOSYNTHESIS_2 
PRINTS