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Q322G6 (PURT_SHIBS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoribosylglycinamide formyltransferase 2
Short name=GART 2
EC=2.1.2.-
Alternative name(s):
5'-phosphoribosylglycinamide transformylase 2
Formate-dependent GAR transformylase
GAR transformylase 2
Gene names
Name:purT
Ordered Locus Names:SBO_1157
OrganismShigella boydii serotype 4 (strain Sb227) [Complete proteome] [HAMAP]
Taxonomic identifier300268 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella ›

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

Catalytic activity

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

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

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the PurK/PurT family.

Contains 1 ATP-grasp domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 392392Phosphoribosylglycinamide formyltransferase 2 HAMAP-Rule MF_01643
PRO_0000319238

Regions

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

Sites

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

Amino acid modifications

Modified residue1791N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q322G6 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 8EAF3233E74B9DAF

FASTA39242,563
        10         20         30         40         50         60 
MTLLGTALRP AATRVMLLGS GELGKEVAIE CQRLGVEVIA VDRYADAPAM HVAHRSHVIN 

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

       130        140        150        160        170        180 
AAEELQLPTS TYRFADSESL FREAVADIGY PCIVKPVMSS SGKGQTFIRS AEQLAQAWKY 

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

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

       310        320        330        340        350        360 
ALHVRAFLGL PVGGIRQYGP AASAVILPQL TSQNVTFDNV QNAVGADLQI RLFGKPEIDG 

       370        380        390 
SRRLGVALAT AESVVDAIER AKHAAGQVKV QG

« Hide

References

[1]"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery."
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. expand/collapse author list , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.
Nucleic Acids Res. 33:6445-6458(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sb227.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000036 Genomic DNA. Translation: ABB65792.1.
RefSeqYP_407620.1. NC_007613.1.

3D structure databases

ProteinModelPortalQ322G6.
SMRQ322G6. Positions 2-392.
ModBaseSearch...

Protein-protein interaction databases

STRING300268.SBO_1157.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB65792; ABB65792; SBO_1157.
GeneID3780290.
KEGGsbo:SBO_1157.
PATRIC18681181. VBIShiBoy33460_1529.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0027.
HOGENOMHOG000072820.
KOK08289.
OMAHRQEKGD.
ProtClustDBPRK09288.

Enzyme and pathway databases

BioCycSBOY300268:GJFL-1154-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 namePURT_SHIBS
AccessionPrimary (citable) accession number: Q322G6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: December 6, 2005
Last modified: May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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