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Q8NS21 (PUR9_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 75. 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:Cgl0861, cg0984
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 520520Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_0000192089

Sequences

Sequence LengthMass (Da)Tools
Q8NS21 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 8A3A80B3AF18AAB7

FASTA52055,760
        10         20         30         40         50         60 
MSDDRKAIKR ALISVYDKTG LEDLAQALHR ENVEIVSTGS TAAKIAELGI PVTPVEELTG 

        70         80         90        100        110        120 
FPECLEGRVK TLHPKVHAGI LADTRKEDHL RQLKELEVAP FQLVVVNLYP FAETVASGAD 

       130        140        150        160        170        180 
FDACVEQIDI GGPSMVRAAA KNHPSVAVVV SPNRYEDVQE ALKTGGFSRA ERTKLAAEAF 

       190        200        210        220        230        240 
RHTATYDVTV ATWMSEQLAA EDSETEFPGW IGTTNTLSRS LRYGENPHQS AALYVGNTRG 

       250        260        270        280        290        300 
LAQAKQFHGK EMSYNNYTDS DAAWRAAWDH ERPCVAIIKH ANPCGIAVSD ESIAAAHREA 

       310        320        330        340        350        360 
HACDSVSAFG GVIASNREVS VEMANQVAEI FTEVIIAPSY EEGAVEILSQ KKNIRILQAE 

       370        380        390        400        410        420 
APVRKGFESR EISGGLLVQE RDLIHAEGDN SANWTLAAGS AVSPEVLKDL EFAWTAVRSV 

       430        440        450        460        470        480 
KSNAILLAKN GATVGVGMGQ VNRVDSARLA VDRAGAERAT GSVAASDAFF PFADGFEVLA 

       490        500        510        520 
EAGITAVVQP GGSIRDNEVI EAANKAGVTM YLTGARHFAH 

« Hide

References

[1]"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
Ikeda M., Nakagawa S.
Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000036 Genomic DNA. Translation: BAB98254.1.
BX927150 Genomic DNA. Translation: CAF19567.1.
RefSeqNP_600090.1. NC_003450.3.
YP_225153.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ8NS21.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196627.cg0984.

2D gel databases

World-2DPAGE0001:Q8NS21.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB98254; BAB98254; BAB98254.
CAF19567; CAF19567; cg0984.
GeneID1018856.
KEGGcgb:cg0984.
cgl:NCgl0827.
PATRIC21493774. VBICorGlu203724_0846.

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMAHRRAHAC.
OrthoDBEOG6QCDFF.

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_CORGL
AccessionPrimary (citable) accession number: Q8NS21
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: October 1, 2002
Last modified: July 9, 2014
This is version 75 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