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Q3B083 (PUR9_SYNS9) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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:Syncc9902_0272
OrganismSynechococcus sp. (strain CC9902) [Complete proteome] [HAMAP]
Taxonomic identifier316279 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length520 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 – 520520Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018981

Sequences

Sequence LengthMass (Da)Tools
Q3B083 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 39883258022C7E60

FASTA52055,018
        10         20         30         40         50         60 
MAPVALLSVS DKSGLLPLAE ALHRIHGYQL LSSGGTAKVL EQAGLPVTRV SEYTGAPEIL 

        70         80         90        100        110        120 
GGRVKTLHPR VHGGILAKRG DAAHQNDLEQ QNINFIDVVV VNLYPFRETV AKADVTWDQA 

       130        140        150        160        170        180 
IENIDIGGPT MVRSAAKNHA DVAVLTSPDQ YDRLLEAMAQ AGGEVPAALR RQLALEAFQH 

       190        200        210        220        230        240 
TAAYDTAISR WMDQAVAADG SPWLEAVPLR QTLRYGENPH QKARWYSHAQ QGWGGAVQLQ 

       250        260        270        280        290        300 
GKELSTNNLL DLEAALAMVR EFGYGSDGAE PAVQPAAVVV KHTNPCGVAI GSDVSTALTR 

       310        320        330        340        350        360 
ALDADRVSAF GGIVAINGVV SAAAAGELKS LFLECVVAPS FSPEAREILA AKANLRLLEL 

       370        380        390        400        410        420 
QPAAIDAAGP DHVRSILGGL LVQDLDDQAI TPSEWTVASQ RPPSSQEQQD LEFAWRLVRH 

       430        440        450        460        470        480 
VRSNAIVVAS KGQSLGIGAG QMNRVGSARL ALDAAGDQAT GAVLASDGFF PFDDTVRLAA 

       490        500        510        520 
SHGITAVIHP GGSLRDADSI KACDELGLAM LLTGRRHFLH 

« Hide

References

[1]"Complete sequence of Synechococcus sp. CC9902."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CC9902.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000097 Genomic DNA. Translation: ABB25245.1.
RefSeqYP_376288.1. NC_007513.1.

3D structure databases

ProteinModelPortalQ3B083.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316279.Syncc9902_0272.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB25245; ABB25245; Syncc9902_0272.
GeneID3742317.
KEGGsye:Syncc9902_0272.
PATRIC23797609. VBISynSp76179_0279.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSSP316279:GJCI-274-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_SYNS9
AccessionPrimary (citable) accession number: Q3B083
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 22, 2005
Last modified: February 19, 2014
This is version 59 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