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Q8YSJ2 (PUR9_NOSS1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 69. 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:all3093
OrganismNostoc sp. (strain PCC 7120 / UTEX 2576) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length506 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 – 506506Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_0000192067

Sequences

Sequence LengthMass (Da)Tools
Q8YSJ2 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: B6F3187B7F026D33

FASTA50654,035
        10         20         30         40         50         60 
MARLALLSVS NKTGLIDLAR RLVEEFEFDL ISSGGTAQAL KDAGLPVTKV ADYTGSPEIL 

        70         80         90        100        110        120 
GGRVKTLHPR IHGGILARRD VASDLTDLEN NQIRPIDLVV VNLYPFESTI AKPGVTLAEA 

       130        140        150        160        170        180 
VEQIDIGGPA MLRASSKNFA HLTVLCDPAQ YDEYLQELRQ NNGVASLEFR QKAALKGFLH 

       190        200        210        220        230        240 
TASYDSAIAS YLSGTQQHTL SGTELQSLRY GENPHQPAAW YQTGTTPTGW TAAEKLQGKE 

       250        260        270        280        290        300 
LSYNNLVDLE AARRIIAEFT DTPAATIIKH TNPCGTALAD TIVEAYQKAF NADATSAFGG 

       310        320        330        340        350        360 
IVALNRPIDA ATASELTKTF LECVIAPDCD AEAQKILSKK SNVRVLTLAD LSTGPKTLVK 

       370        380        390        400        410        420 
QIAGGFLVQA ADDIAADTSQ WQVVTERQPT PDELAELLFA WKVCKHVKSN AIVVTSDRTT 

       430        440        450        460        470        480 
LGVGAGQMNR IGSTKIALEQ AGDKAKGAIL ASDGFFPFDD TVRTAAAAGI SAIVQPGGSL 

       490        500 
RDQDSVKAAN ELGLLMVLTG VRHFLH 

« Hide

References

[1]"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takazawa M., Yamada M., Yasuda M., Tabata S.
DNA Res. 8:205-213(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7120 / UTEX 2576.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000019 Genomic DNA. Translation: BAB74792.1.
PIRAF2192.
RefSeqNP_487133.1. NC_003272.1.

3D structure databases

ProteinModelPortalQ8YSJ2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING103690.all3093.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB74792; BAB74792; BAB74792.
GeneID1106691.
KEGGana:all3093.
PATRIC22776530. VBINosSp37423_3725.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

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_NOSS1
AccessionPrimary (citable) accession number: Q8YSJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: March 1, 2002
Last modified: February 19, 2014
This is version 69 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