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Q9RHX6 (PUR9_CORAM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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
OrganismCorynebacterium ammoniagenes (Brevibacterium ammoniagenes)
Taxonomic identifier1697 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length516 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

Keywords
   Biological processPurine biosynthesis
   Molecular functionHydrolase
Transferase
   Technical termMultifunctional enzyme
Gene Ontology (GO)
   Biological_process'de novo' IMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionIMP cyclohydrolase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

phosphoribosylaminoimidazolecarboxamide formyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 516516Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_0000192087

Sequences

Sequence LengthMass (Da)Tools
Q9RHX6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 14EF915D6DB72B93

FASTA51654,757
        10         20         30         40         50         60 
MSDDRKQIKR ALISVYDKTG LEELARTLDS AGVEIVSTGS TAAKIADLGI NVTPVESLTG 

        70         80         90        100        110        120 
FPECLEGRVK TLHPRVHAGI LADTRKPDHL NQLEELEIEP FQLVVVNLYP FKETVASGAD 

       130        140        150        160        170        180 
FDGCVEQIDI GGPSMVRAAA KNHPSVAVVV DPARYGDIAE AVAQGGFDLA QRRQLAATAF 

       190        200        210        220        230        240 
KHTADYDVAV SGWFAQQLAD DSVASAELEG DALRYGENPH QQASIVREGT TGVANAKQLH 

       250        260        270        280        290        300 
GKEMSYNNYQ DADAAWRAAW DHERPCVAII KHANPCGIAV SDESIAAAHA AAHACDPMSA 

       310        320        330        340        350        360 
FGGVIAVNRE VTKEMATQVA DIFTEVIIAP SYEDGAVEIL QGKKNIRILV AEHEVPAVEV 

       370        380        390        400        410        420 
KEISGGRLLQ EADVYQAEGD KASSWTLAAG EAASEEKLAE LEFAWRAVRS VKSNAILLAH 

       430        440        450        460        470        480 
EGATVGVGMG QVNRVDSAKL AVDRANTLAD SAERARGSVA ASDAFFPFAD GLQVLIDAGV 

       490        500        510 
SAVVQPGGSI RDEEVIAAAE AAGITMYFTG TRHFAH 

« Hide

References

[1]"Corynebacterium ammoniagenes purNH region."
Yonetani Y., Teshiba S.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 6872 / DSM 20305 / KCTC 1019 / NCTC 2399.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB003159 Genomic DNA. Translation: BAA89444.1.

3D structure databases

ProteinModelPortalQ9RHX6.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_CORAM
AccessionPrimary (citable) accession number: Q9RHX6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: May 1, 2000
Last modified: February 19, 2014
This is version 60 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