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Q0AW31 (PUR9_SYNWW) 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:Swol_1775
OrganismSyntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen) [Complete proteome] [HAMAP]
Taxonomic identifier335541 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesSyntrophomonadaceaeSyntrophomonas

Protein attributes

Sequence length506 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 – 506506Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018983

Sequences

Sequence LengthMass (Da)Tools
Q0AW31 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 9BA05C7BBBBD9459

FASTA50655,047
        10         20         30         40         50         60 
MKRALISVSN KEGLLDFARG LEKLGYEIIS TGGTYNTIKE AGIKVKKVAD ITGFPEILDG 

        70         80         90        100        110        120 
RVKTLHPKIH GGILARRIPE HLQQLQENDI GPIDIVAVNL YPFRETISRP GVSLEEAIEN 

       130        140        150        160        170        180 
IDIGGPAMVR AAAKNYQDVA VVVKPEFYQA LLEALEKPGG ISPEFRLKLA LEAFSHTAAY 

       190        200        210        220        230        240 
DAMISSYLSR VSNSDLNQNL ILAGEKVYDL RYGENPHQKA SFYRFMTPGL GLPDARQLNG 

       250        260        270        280        290        300 
KELSYNNIID TQAAWELVRE FDEPACVIIK HTNPCGTAVA ATLEEAFDRA FAADPLSAFG 

       310        320        330        340        350        360 
GIIALNRPVD GATAQKAAEP FMEVIIAPAY TPEALESLQA KKNLRVLELP LEVAGGLQIR 

       370        380        390        400        410        420 
TVAGGFVVQE SDRDKLDMDK VQVVTQKEPT VEQLKELAFA RKVVKHIKSN AIVVARDGMT 

       430        440        450        460        470        480 
LGVGAGQMNR VGSARIALES AGEKARGAVM ASDAFFPFKD TVELAAQYGI TAIIQPGGSV 

       490        500 
RDQESIDECD KHGIAMVFTG IRHFKH 

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References

[1]"The genome of Syntrophomonas wolfei: new insights into syntrophic metabolism and biohydrogen production."
Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L., McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.
Environ. Microbiol. 12:2289-2301(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2245B / Goettingen.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000448 Genomic DNA. Translation: ABI69073.1.
RefSeqYP_754444.1. NC_008346.1.

3D structure databases

ProteinModelPortalQ0AW31.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335541.Swol_1775.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI69073; ABI69073; Swol_1775.
GeneID4282737.
KEGGswo:Swol_1775.
PATRIC23858545. VBISynWol51738_1911.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBCLSK2780689.

Enzyme and pathway databases

BioCycSWOL335541:GHL1-1828-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_SYNWW
AccessionPrimary (citable) accession number: Q0AW31
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 17, 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