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A5F3U8 (PUR9_VIBC3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 51. 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:VC0395_A2653, VC395_0305
OrganismVibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395) [Complete proteome] [HAMAP]
Taxonomic identifier345073 [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_1000071453

Sequences

Sequence LengthMass (Da)Tools
A5F3U8 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: BE70E3C0956AB252

FASTA53057,297
        10         20         30         40         50         60 
MNNARPIHRA LLSVSDKTGI VEFAKALAER GVELLSTGGT ARLLAEQGLT VTEVSDYTGF 

        70         80         90        100        110        120 
PEMMDGRVKT LHPKVHGGIL GRRGQDDAVM NTHGIQPIDM VVVNLYPFAQ TVANPNCTLA 

       130        140        150        160        170        180 
DAVENIDIGG PTMVRSAAKN HKDVAIVVNA HDYDRVIREM DANHNSLTLA TRFDLAIAAF 

       190        200        210        220        230        240 
EHTAAYDGMI ANYFGTLVPS YGDNKEGDEE SKFPRTFNAQ FIKKQDMRYG ENSHQAAAFY 

       250        260        270        280        290        300 
VEANPQEASV ATARQIQGKA LSYNNIADTD AALECVKEFS EPACVIVKHA NPCGVALGDD 

       310        320        330        340        350        360 
LLQAYNRAYQ TDPTSAFGGI IAFNRELDGE TARAIIERQF VEVIIAPKVS QAAIDIVAAK 

       370        380        390        400        410        420 
QNVRLLECGE WQGQTTGFDL KRVNGGLLVQ DRDQGMVAQD DLQVVSTRQP SDAELKDALF 

       430        440        450        460        470        480 
CWKVAKYVKS NAIVYAKGDM AIGIGAGQMS RVYSAKIAGI KAADEGLEVA GSVMASDAFF 

       490        500        510        520        530 
PFRDGIDAAA EAGITCVIQP GGSMRDQEVI DAANEHGMAM IFTGMRHFRH 

« Hide

References

[1]Heidelberg J.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39541 / Classical Ogawa 395 / O395.
[2]"A recalibrated molecular clock and independent origins for the cholera pandemic clones."
Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.
PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39541 / Classical Ogawa 395 / O395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000627 Genomic DNA. Translation: ABQ20331.1.
CP001235 Genomic DNA. Translation: ACP08328.1.
RefSeqYP_001218531.1. NC_009457.1.
YP_002818564.1. NC_012582.1.

3D structure databases

ProteinModelPortalA5F3U8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING345073.VC0395_A2653.

Proteomic databases

PRIDEA5F3U8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ20331; ABQ20331; VC0395_A2653.
ACP08328; ACP08328; VC395_0305.
GeneID5137582.
7774377.
KEGGvco:VC0395_A2653.
vcr:VC395_0305.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.

Enzyme and pathway databases

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_VIBC3
AccessionPrimary (citable) accession number: A5F3U8
Secondary accession number(s): C3M3S0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: June 12, 2007
Last modified: May 14, 2014
This is version 51 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