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B3QS62 (PUR9_CHLT3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional purine biosynthesis protein PurH

Including the following 2 domains:

  1. Phosphoribosylaminoimidazolecarboxamide formyltransferase
    EC=2.1.2.3
    Alternative name(s):
    AICAR transformylase
  2. IMP cyclohydrolase
    EC=3.5.4.10
    Alternative name(s):
    ATIC
    IMP synthase
    Inosinicase
Gene names
Name:purH
Ordered Locus Names:Ctha_1548
OrganismChloroherpeton thalassium (strain ATCC 35110 / GB-78) [Complete proteome] [HAMAP]
Taxonomic identifier517418 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChloroherpeton

Protein attributes

Sequence length525 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1. HAMAP-Rule MF_00139

Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.

Domain

The IMP cyclohydrolase activity resides in the N-terminal region By similarity. HAMAP-Rule MF_00139

Sequence similarities

Belongs to the PurH family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 525525Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000096052

Sequences

Sequence LengthMass (Da)Tools
B3QS62 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: CC8EDE53887E6724

FASTA52557,327
        10         20         30         40         50         60 
MAERKIKRAL ISVSDKTGII DFAKSLAEFG VEIFSTGGTL KKLIEAGIAA KSISEITKFP 

        70         80         90        100        110        120 
EIMDGRVKTL HPAIHGGLLA VRGNSDHEKQ AAENNINFID LVAVNLYPFE ATVAKPDVTF 

       130        140        150        160        170        180 
ADAIENIDIG GPSMLRSAAK NHKSVTVITD AADYQCVLEE MRANDGATTE ATRLYLAKKV 

       190        200        210        220        230        240 
FALTARYDGA ISNYLEKISQ TDESVLPNHL SVSLTKEIDM RYGENPHQKA GFYAMKVGEQ 

       250        260        270        280        290        300 
NLSFDEFFEK LHGKSLSYNN LLDISAAAGL IEEFRGAEPT VAIFKHTNPC GVAQADSLET 

       310        320        330        340        350        360 
AYRKAFSTDT QAPFGGIIAV NRPLDMATAK AINEIFTEIV IAPEFEEGVL EYLMKKKDRR 

       370        380        390        400        410        420 
LIRQLKALPS SALEFRSTVC GLLVQDKDAK TATKEELKVV TKRQPTEAEL EDLLFAWKIC 

       430        440        450        460        470        480 
KHVKSNTIVY AKDMQTVGVG AGQMSRVDSS RIARWKAGEV NLELKNSVVA SDAFFPFADG 

       490        500        510        520 
LIAAAEAGAS AVIQPGGSIR DEEVIAAADE RNIAMVFTGT RHFRH 

« Hide

References

[1]"Complete sequence of Chloroherpeton thalassium ATCC 35110."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35110 / GB-78.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001100 Genomic DNA. Translation: ACF14007.1.
RefSeqYP_001996454.1. NC_011026.1.

3D structure databases

ProteinModelPortalB3QS62.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING517418.Ctha_1548.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF14007; ACF14007; Ctha_1548.
GeneID6422621.
KEGGcts:Ctha_1548.
PATRIC21432031. VBIChlTha99257_1816.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycCTHA517418:GHTO-1581-MONOMER.
UniPathwayUPA00074; UER00133.
UPA00074; UER00135.

Family and domain databases

Gene3D3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPMF_00139. PurH.
InterProIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERPTHR11692. PTHR11692. 1 hit.
PfamPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR9_CHLT3
AccessionPrimary (citable) accession number: B3QS62
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 2, 2008
Last modified: February 19, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways