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Q11CT4 (PUR9_MESSB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:Meso_3420
OrganismMesorhizobium sp. (strain BNC1) [Complete proteome] [HAMAP]
Taxonomic identifier266779 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeChelativorans

Protein attributes

Sequence length537 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 – 537537Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018908

Sequences

Sequence LengthMass (Da)Tools
Q11CT4 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 6A3FC694E5002FE8

FASTA53756,842
        10         20         30         40         50         60 
MTVSAKNIPA PDLVPVRRAL ISVSDKTGIV DFARSLAARE VALASTGGTA ALLARSGIGV 

        70         80         90        100        110        120 
MDVSQLTGFP EIMDGRVKTL HPAVHGGLLA IRDDPDHRSA METHAIKPID LVVINLYPFE 

       130        140        150        160        170        180 
DVRFGGGDYA ATVENIDIGG PAMLRAAAKN HAYVAVVTDP ADYARVLEAL EKNDGALPYR 

       190        200        210        220        230        240 
LRQELAAKAY ARTAAYDAAI SQWFAESLAI AEPEWRSFGG RLAQVMRYGE NPHQQAGFYA 

       250        260        270        280        290        300 
TGEKRPGVAT ARQVQGKQLS YNNINDTDAA FELVCEFDPK KVAAVAIIKH ANPCGVAEGT 

       310        320        330        340        350        360 
SLAEAYRKAL ACDPVSAFGG IVALNRILDA EAAEEIAKIF TEVIIAPDAT EEAQAIIATK 

       370        380        390        400        410        420 
KNLRLLLTEG VADPRAPGLS AKTVAGGLLV QTRDNGVIDD LDLRVVTRRA PSEKEMANLK 

       430        440        450        460        470        480 
FAFRVAKHVK SNAIVYARDL ATVGIGAGQM SRVDSARIAA RKAEDAAAAA GGQPLTKGSV 

       490        500        510        520        530 
VASDAFFPFA DGLLSAVEAG ATAVIQPGGS MRDDEVIKAA DEHGIAMVFT GMRHFRH 

« Hide

References

[1]"Complete sequence of chromosome of Mesorhizobium sp. BNC1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BNC1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000390 Genomic DNA. Translation: ABG64791.1.
RefSeqYP_675956.1. NC_008254.1.

3D structure databases

ProteinModelPortalQ11CT4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266779.Meso_3420.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG64791; ABG64791; Meso_3420.
GeneID4183118.
KEGGmes:Meso_3420.
PATRIC21347164. VBICheSp72577_4184.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycCSP266779:GI09-3480-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_MESSB
AccessionPrimary (citable) accession number: Q11CT4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: February 19, 2014
This is version 57 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