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A7HSQ6 (PUR9_PARL1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 49. 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:Plav_1319
OrganismParvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966) [Complete proteome] [HAMAP]
Taxonomic identifier402881 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhodobiaceaeParvibaculum

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_1000096078

Sequences

Sequence LengthMass (Da)Tools
A7HSQ6 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 0557115B71D42E44

FASTA53756,441
        10         20         30         40         50         60 
MTSSKSHPEA ADIQRVRRAL LSVSDKTGLI DFARALHGAG VELISTGGTA KAIKDAALPV 

        70         80         90        100        110        120 
KDVADLTGFP EMMDGRVKTL HPKVHGGLLA VRDDAEHAAA MKEHGIAGID LLCVNLYPFE 

       130        140        150        160        170        180 
ATVAKGAAYD ECVENIDIGG PAMIRAAAKN HAYVGVIVDG ADYAAVIEEI TGKGGTSLVL 

       190        200        210        220        230        240 
RKRLAQKAYA RTAAYDAAIS NWFANAIGET APDYRAFGGS LKQTLRYGEN PHQVASFYVT 

       250        260        270        280        290        300 
GENRPGVSNA EQLQGKELSY NNINDTDAAF ELVGEFDPKL APAIAIIKHA NPCGVATGAT 

       310        320        330        340        350        360 
LADAYRKALA CDPVSAFGGI IAANRPLDGE TAEEIARIFT EVIIAPEADE DARRIIGAKK 

       370        380        390        400        410        420 
NLRLLITHGL PDPATAGLFY KSVAGGLLVQ SRDNGRVDTL DLKVVTKRAP TAQEMEDLKF 

       430        440        450        460        470        480 
AFRVCKHVKS NAIIYVKNGA TVGIGAGQMS RVDSARIAAR KAQDAAEAAG EKTPATIGSV 

       490        500        510        520        530 
VASDAFFPFA DGLLSAAEAG ATAVIQPGGS VRDDEVIAAA DEKGLAMVMT GMRHFRH 

« Hide

References

[1]"Complete genome sequence and annotation of Parvibaculum lavamentivorans DS-1."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DS-1 / DSM 13023 / NCIMB 13966.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000774 Genomic DNA. Translation: ABS62939.1.
RefSeqYP_001412596.1. NC_009719.1.

3D structure databases

ProteinModelPortalA7HSQ6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING402881.Plav_1319.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS62939; ABS62939; Plav_1319.
GeneID5456027.
KEGGpla:Plav_1319.
PATRIC22864244. VBIParLav90819_1360.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycPLAV402881:GHQA-1334-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_PARL1
AccessionPrimary (citable) accession number: A7HSQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 11, 2007
Last modified: May 14, 2014
This is version 49 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