CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006282
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphoribosylglycinamide formyltransferase 2 
Protein Synonyms/Alias
 GART 2; 5'-phosphoribosylglycinamide transformylase 2; Formate-dependent GAR transformylase; GAR transformylase 2 
Gene Name
 purT 
Gene Synonyms/Alias
 b1849; JW1838 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
109VPCARATKLTMNREGacetylation[1]
179EQLAQAWKYAQQGGRacetylation[1, 2]
355LQIRLFGKPEIDGSRacetylation[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] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842
Functional Description
 Catalyzes two reactions: the first one is the production of beta-formyl glycinamide ribonucleotide (GAR) from formate, ATP and beta GAR; the second, a side reaction, is the production of acetyl phosphate and ADP from acetate and ATP. 
Sequence Annotation
 DOMAIN 119 308 ATP-grasp.
 NP_BIND 160 165 ATP.
 NP_BIND 195 198 ATP.
 REGION 22 23 5'-phosphoribosylglycinamide binding.
 REGION 362 363 5'-phosphoribosylglycinamide binding.
 METAL 267 267 Magnesium (By similarity).
 METAL 279 279 Magnesium (By similarity).
 BINDING 82 82 5'-phosphoribosylglycinamide.
 BINDING 114 114 ATP.
 BINDING 155 155 ATP.
 BINDING 203 203 ATP.
 BINDING 267 267 ATP.
 BINDING 279 279 ATP.
 BINDING 286 286 5'-phosphoribosylglycinamide.
 BINDING 355 355 5'-phosphoribosylglycinamide.
 MOD_RES 179 179 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Complete proteome; Direct protein sequencing; Magnesium; Metal-binding; Nucleotide-binding; Purine biosynthesis; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 392 AA 
Protein Sequence
MTLLGTALRP AATRVMLLGS GELGKEVAIE CQRLGVEVIA VDRYADAPAM HVAHRSHVIN 60
MLDGDALRRV VELEKPHYIV PEIEAIATDM LIQLEEEGLN VVPCARATKL TMNREGIRRL 120
AAEELQLPTS TYRFADSESL FREAVADIGY PCIVKPVMSS SGKGQTFIRS AEQLAQAWKY 180
AQQGGRAGAG RVIVEGVVKF DFEITLLTVS AVDGVHFCAP VGHRQEDGDY RESWQPQQMS 240
PLALERAQEI ARKVVLALGG YGLFGVELFV CGDEVIFSEV SPRPHDTGMV TLISQDLSEF 300
ALHVRAFLGL PVGGIRQYGP AASAVILPQL TSQNVTFDNV QNAVGADLQI RLFGKPEIDG 360
SRRLGVALAT AESVVDAIER AKHAAGQVKV QG 392 
Gene Ontology
 GO:0008776; F:acetate kinase activity; IDA:EcoCyc.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0043815; F:phosphoribosylglycinamide formyltransferase 2 activity; IEA:HAMAP.
 GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:InterPro.
 GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway. 
Interpro
 IPR011761; ATP-grasp.
 IPR003135; ATP-grasp_carboxylate-amine.
 IPR013815; ATP_grasp_subdomain_1.
 IPR013816; ATP_grasp_subdomain_2.
 IPR016185; PreATP-grasp_dom.
 IPR005862; PurT.
 IPR011054; Rudment_hybrid_motif. 
Pfam
 PF02222; ATP-grasp 
SMART
  
PROSITE
 PS50975; ATP_GRASP 
PRINTS