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C0RF67 (PUR9_BRUMB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 38. 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:BMEA_A1866
OrganismBrucella melitensis biotype 2 (strain ATCC 23457) [Complete proteome] [HAMAP]
Taxonomic identifier546272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length538 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 – 538538Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000122949

Sequences

Sequence LengthMass (Da)Tools
C0RF67 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: 099349D5160AC19F

FASTA53856,481
        10         20         30         40         50         60 
MAVSSKHIPA PDLHRVRRAL LSVSDKTGLI DFAKALHANG VEILSTGGTA KSIAAAGIPV 

        70         80         90        100        110        120 
KDVSEITGFP EIMDGRVKTL HPAVHGGLLA VRNDPEHVAA MEEHGIGGID LAVINLYPFE 

       130        140        150        160        170        180 
EVRFKGGDYD TTVENIDIGG PAMIRASAKN HAYVATVVDP ADYADVVAEL EKHSGSLPLA 

       190        200        210        220        230        240 
FRKKLAAKAF SRTAAYDAAI SNWFAEAIDE ETPTYRAVAG KLHSVMRYGE NPHQTAGFYL 

       250        260        270        280        290        300 
TGEKRPGVAT ATQLQGKQLS YNNINDTDAA FELVAEFDPA RTAAVAIIKH ANPCGVAEAS 

       310        320        330        340        350        360 
TIKEAYLKAL ACDPVSAFGG IVALNRTLDE EAAEEIVKTF TEVIIAPDAT EGAQAIVAAK 

       370        380        390        400        410        420 
KNLRLLVTGG LPDPRAKGIA AKTVAGGLLV QSRDNGVVDD LDLKVVTKRA PTEAELNDLK 

       430        440        450        460        470        480 
FAFRVGKHVK SNAIVYVKDG ATVGIGAGQM SRVDSARIAA RKAEDAAEAA GLAAPLTKGC 

       490        500        510        520        530 
VVASDAFFPF ADGLLSAVEA GATAVIQPGG SMRDDEVIAA ADEHGIAMVM TGMRHFRH 

« Hide

References

[1]"Brucella melitensis ATCC 23457 whole genome shotgun sequencing project."
Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J., Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C. expand/collapse author list , Tapia R., Han C., Detter J.C., Bruce D., Brettin T.S.
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 23457.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001488 Genomic DNA. Translation: ACO01539.1.
RefSeqYP_002733493.1. NC_012441.1.

3D structure databases

ProteinModelPortalC0RF67.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING546272.BMEA_A1866.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO01539; ACO01539; BMEA_A1866.
GeneID7677352.
KEGGbmi:BMEA_A1866.
PATRIC17839524. VBIBruMel14466_1887.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBMEL546272:GJOX-1815-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...

Other

PROC0RF67.

Entry information

Entry namePUR9_BRUMB
AccessionPrimary (citable) accession number: C0RF67
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 5, 2009
Last modified: February 19, 2014
This is version 38 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