Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q04EU6 (PUR9_OENOB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. 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:OEOE_1129
OrganismOenococcus oeni (strain ATCC BAA-331 / PSU-1) [Complete proteome] [HAMAP]
Taxonomic identifier203123 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesOenococcus

Protein attributes

Sequence length509 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 – 509509Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018921

Sequences

Sequence LengthMass (Da)Tools
Q04EU6 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 2DB56A46B16940E1

FASTA50956,130
        10         20         30         40         50         60 
MKRALLSVSD KRGLIDFAKG LIKNNYEIIS TGGTLKFLTE AGVKAKAVEE ITGFPEILNG 

        70         80         90        100        110        120 
RVKTLHPKIH AALLAKRENS EHMKTLEEHQ ITPIDLLAVN LYPFKETIEK KDVSYDQAIE 

       130        140        150        160        170        180 
NIDIGGPSML RSAAKNARDV IVVVDPDDYD SILKAIANDD LSHDFRRHLQ AKTFRHTAAY 

       190        200        210        220        230        240 
DALIADYLSK EEYPEKLTVT YDKDFDLRYG ENPNQTAAVY ADAIPKAYSI LQAKILHGKK 

       250        260        270        280        290        300 
LSYNNIKDAD AALRTIADFQ DQPTVVTLKH MNPAGIGQAI TIEKAWDKAF YADDISIFGG 

       310        320        330        340        350        360 
IVVLNREVDL ATAQKMHTIF LEIIIAPGFS EEAYQILAKK KNLRLLTVAM TNTLPKELEL 

       370        380        390        400        410        420 
TSVLGGAVVQ EMDRLVENAA DFEVVSSAKP TDEQLEALVF AQKAVKHVKS NAILIAAQGQ 

       430        440        450        460        470        480 
TLGIGAGQPN RIDSVKIAFK HAEAKKNFDQ AVLASDAFFP MDDSVEFAAE HGIKAIVEPG 

       490        500 
GSIKDKDSIA MADKLGVVLV FSHNRHFRH 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000411 Genomic DNA. Translation: ABJ57026.1.
RefSeqYP_810691.1. NC_008528.1.

3D structure databases

ProteinModelPortalQ04EU6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203123.OEOE_1129.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ57026; ABJ57026; OEOE_1129.
GeneID4415337.
KEGGooe:OEOE_1129.
PATRIC22800454. VBIOenOen113004_1153.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycOOEN203123:GHNL-1129-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_OENOB
AccessionPrimary (citable) accession number: Q04EU6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: February 19, 2014
This is version 55 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