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B7VM57 (PUR9_VIBSL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. 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:VS_2951
OrganismVibrio splendidus (strain LGP32) (Vibrio splendidus (strain Mel32)) [Complete proteome] [HAMAP]
Taxonomic identifier575788 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length530 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 – 530530Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000122980

Sequences

Sequence LengthMass (Da)Tools
B7VM57 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 0FBA08B4FCCE3945

FASTA53057,425
        10         20         30         40         50         60 
MNNARPIRRA LISVSDKTGI VEFAQALANR GVDILSTGGT ARLLAEKGIS VTEVSDYTGF 

        70         80         90        100        110        120 
PEMMDGRVKT LHPKVHGGVL GRRGQDDDVM ETHGINPIDM VVVNLYPFAE TVAKEGCTLA 

       130        140        150        160        170        180 
DAVENIDIGG PTMVRSAAKN HKDVTIVVNA HDYERVVAEM DANEKSLTLE TRFDLAIAAF 

       190        200        210        220        230        240 
EHTASYDGMI ANYFGTMVPS YGENKEGDEE SKFPRTFNQQ FEKKQDMRYG ENSHQAAAFY 

       250        260        270        280        290        300 
VEANPEEASV STARQIQGKA LSYNNIADTD AALECVKEFD EPACVIVKHA NPCGVALGED 

       310        320        330        340        350        360 
ILEAYDRAFK TDPTSAFGGI IAFNRELDAA TATAITERQF VEVIIAPSVS AEAVAIVAAK 

       370        380        390        400        410        420 
KNLRLLECGE WTTKTTGFDV KRVNGGLLVQ DRDQGMVSED DLKVVSKRQP TAEELKDALF 

       430        440        450        460        470        480 
CWKVAKYVKS NAIVYSKGDM TIGVGAGQMS RVYSAKIAGI KAADEGLQVE GCVMASDAFF 

       490        500        510        520        530 
PFRDGIDAAA EAGIKCVIQP GGSMRDDEVI AAADEHGMAM IFTGMRHFRH 

« Hide

References

[1]"Vibrio splendidus str. LGP32 complete genome."
Mazel D., Le Roux F.
Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LGP32.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM954972 Genomic DNA. Translation: CAV20247.1.
RefSeqYP_002418488.1. NC_011753.2.

3D structure databases

ProteinModelPortalB7VM57.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING575788.VS_2951.

Proteomic databases

PRIDEB7VM57.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAV20247; CAV20247; VS_2951.
GeneID7162434.
KEGGvsp:VS_2951.
PATRIC20156436. VBIVibSpl48387_4160.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycVSPL575788:GH64-2897-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_VIBSL
AccessionPrimary (citable) accession number: B7VM57
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: February 19, 2014
This is version 41 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