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C8UBU9 (C8UBU9_ECO1A) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoribosylglycinamide formyltransferase 2 HAMAP-Rule MF_01643
Short name=GART 2 HAMAP-Rule MF_01643
EC=2.1.2.- HAMAP-Rule MF_01643
Alternative name(s):
5'-phosphoribosylglycinamide transformylase 2 HAMAP-Rule MF_01643
Formate-dependent GAR transformylase HAMAP-Rule MF_01643
GAR transformylase 2 HAMAP-Rule MF_01643
Gene names
Name:purT HAMAP-Rule MF_01643 EMBL BAI36221.1
Ordered Locus Names:ECO111_2357 EMBL BAI36221.1
OrganismEscherichia coli O111:H- (strain 11128 / EHEC) [Complete proteome] [HAMAP] EMBL BAI36221.1
Taxonomic identifier585396 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length392 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_01643 SAAS SAAS011054

Catalytic activity

Formate + ATP + 5'-phospho-ribosylglycinamide = 5'-phosphoribosyl-N-formylglycinamide + ADP + diphosphate. HAMAP-Rule MF_01643 SAAS SAAS011054

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (formate route): step 1/1. HAMAP-Rule MF_01643 SAAS SAAS011054

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01643

Sequence similarities

Belongs to the PurK/PurT family. HAMAP-Rule MF_01643

Contains 1 ATP-grasp domain. HAMAP-Rule MF_01643 SAAS SAAS003135

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain119 – 308190ATP-grasp By similarity HAMAP-Rule MF_01643
Nucleotide binding160 – 1656ATP By similarity HAMAP-Rule MF_01643
Nucleotide binding195 – 1984ATP By similarity HAMAP-Rule MF_01643
Region22 – 2325'-phosphoribosylglycinamide binding By similarity HAMAP-Rule MF_01643
Region362 – 36325'-phosphoribosylglycinamide binding By similarity HAMAP-Rule MF_01643

Sites

Metal binding2671Magnesium By similarity HAMAP-Rule MF_01643
Metal binding2791Magnesium By similarity HAMAP-Rule MF_01643
Binding site8215'-phosphoribosylglycinamide By similarity HAMAP-Rule MF_01643
Binding site1141ATP By similarity HAMAP-Rule MF_01643
Binding site1551ATP By similarity HAMAP-Rule MF_01643
Binding site2031ATP By similarity HAMAP-Rule MF_01643
Binding site2671ATP By similarity HAMAP-Rule MF_01643
Binding site2791ATP By similarity HAMAP-Rule MF_01643
Binding site28615'-phosphoribosylglycinamide By similarity HAMAP-Rule MF_01643
Binding site35515'-phosphoribosylglycinamide By similarity HAMAP-Rule MF_01643

Sequences

Sequence LengthMass (Da)Tools
C8UBU9 [UniParc].

Last modified November 3, 2009. Version 1.
Checksum: 98AC34C16FC44041

FASTA39242,272
        10         20         30         40         50         60 
MTLLGTALRP AATRVMLLGS GELGKEVAIE CQRLGVEVIA VDRYADAPAM HVAHRSHVIN 

        70         80         90        100        110        120 
MLDGDALRRV VELEKPHYIV PEIEAIATDM LIQLEEEGLN VVPCARATKL TMNREGIRRL 

       130        140        150        160        170        180 
AAEQLQLPTS TYRFADSESL FREAVAAIGY PCIVKPVMSS SGKGQTFIRS AEQLAQAWEY 

       190        200        210        220        230        240 
AQQGGRAGAG RVIVEGVVKF DFEITLLTVS AVDGVHFCAP VGHRQEDGDY RESWQPQQMS 

       250        260        270        280        290        300 
PLALERAQEI ARKVVLALGG YGLFGVELFV CGDEVIFSEV SPRPHDTGMV TLISQDLSEF 

       310        320        330        340        350        360 
ALHVRAFLGL PVGGIRQYGP AASAVILPQL TSQNVTFDNV QNAVGAGLQI RLFGKPAING 

       370        380        390 
SRRLGVALAT AESVVDAIKR AKHAAGQVKV QG

« Hide

References

[1]"Comparative genomics reveal the mechanism of the parallel evolution of O157 and non-O157 enterohemorrhagic Escherichia coli."
Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., Hayashi T.
Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 11128 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP010960 Genomic DNA. Translation: BAI36221.1.
RefSeqYP_003234772.1. NC_013364.1.

3D structure databases

ProteinModelPortalC8UBU9.
ModBaseSearch...

Protein-protein interaction databases

STRING585396.ECO111_2357.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAI36221; BAI36221; ECO111_2357.
GeneID8488910.
KEGGeoi:ECO111_2357.
PATRIC32107986. VBIEscCol143187_2447.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0027.
HOGENOMHOG000072820.
KOK08289.
OMAHRQEKGD.
ProtClustDBPRK09288.

Enzyme and pathway databases

BioCycECOL585396:GJCW-2424-MONOMER.
UniPathwayUPA00074; UER00127.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
HAMAPMF_01643. PurT.
InterProIPR011761. 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.
[Graphical view]
PANTHERPTHR23047:SF2. PTHR23047:SF2. 1 hit.
PfamPF02222. ATP-grasp. 1 hit.
[Graphical view]
SUPFAMSSF52440. PreATP-grasp-like. 1 hit.
SSF51246. Rudmnt_hyb_motif. 1 hit.
TIGRFAMsTIGR01142. purT. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC8UBU9_ECO1A
AccessionPrimary (citable) accession number: C8UBU9
Entry history
Integrated into UniProtKB/TrEMBL: November 3, 2009
Last sequence update: November 3, 2009
Last modified: May 1, 2013
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info