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B9DSR6 (PUR9_STRU0) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. 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:SUB0030
OrganismStreptococcus uberis (strain ATCC BAA-854 / 0140J) [Complete proteome] [HAMAP]
Taxonomic identifier218495 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length515 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 – 515515Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000122975

Sequences

Sequence LengthMass (Da)Tools
B9DSR6 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 5D4680607974EBC9

FASTA51556,571
        10         20         30         40         50         60 
MTKRALISVS DKAGIVDFAQ ELKKLGWDII STGGTKTALD TAGIKTIAID DITGFPEMMD 

        70         80         90        100        110        120 
GRVKTLHPNI HGGLLARRDL DTHLKAAQEN GIELIDLVVV NLYPFKETIL RPDVTYAQAV 

       130        140        150        160        170        180 
ENIDIGGPSM LRSAAKNHAS VTVVVDPSDY ERVLAELTEI GETTYETRQA LAAKVFRHTA 

       190        200        210        220        230        240 
AYDALIAEYF TAQVGETKPE KLTLTYDLKQ EMRYGENPQQ AADFYQKALP TDYSIASAKQ 

       250        260        270        280        290        300 
LNGKELSFNN IRDADAAIRI IRDFKERPTV VALKHMNPCG IGQADTIEKA WDYAYEADSV 

       310        320        330        340        350        360 
SIFGGIVVLN REVDKATAEK MHPIFLEIII APSYSDEALA ILTNKKKNLR ILQLPFEGQA 

       370        380        390        400        410        420 
ASEIEAEYTG VVGGMLVQNQ DVIEEKADAW EVVTERQPSD DEKEALEFAW RAIKYVKSNG 

       430        440        450        460        470        480 
ILIANNHMTL GVGPGQTNRV ASVRIAIEQA KDRLEGAALA SDAFFPFADN IEEIAAAGIK 

       490        500        510 
AIIQPGGSVR DQESIDAANK HGIAMIFTGV RHFRH 

« Hide

References

[1]"Evidence for niche adaptation in the genome of the bovine pathogen Streptococcus uberis."
Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A., Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R., Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D., Parkhill J.
BMC Genomics 10:54-54(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-854 / 0140J.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM946015 Genomic DNA. Translation: CAR40373.1.
RefSeqYP_002561406.1. NC_012004.1.

3D structure databases

ProteinModelPortalB9DSR6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING218495.SUB0030.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR40373; CAR40373; SUB0030.
GeneID7392433.
KEGGsub:SUB0030.
PATRIC19805754. VBIStrUbe20775_0029.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycSUBE218495:GJ7D-51-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_STRU0
AccessionPrimary (citable) accession number: B9DSR6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 45 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