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A2CCK6 (PUR9_PROM3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 49. 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:P9303_24851
OrganismProchlorococcus marinus (strain MIT 9303) [Complete proteome] [HAMAP]
Taxonomic identifier59922 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length517 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 – 517517Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018927

Sequences

Sequence LengthMass (Da)Tools
A2CCK6 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 8DD264EBBDE007D3

FASTA51755,150
        10         20         30         40         50         60 
MAPIALLSVS NKHGIVSLAE SLHRMHGFQL LSSGGTAKVL EDAGLPVTRV AEHTGAAEIL 

        70         80         90        100        110        120 
GGRVKTLHPR VHGGILAMRG DPDHEVDLEQ HQIPPIDVVV VNLYPFRETV ANPQVSWETA 

       130        140        150        160        170        180 
IENIDIGGPA MVRAAAKNHA HVAVLTRPDQ YDRFLVALSD GVDGQLRREL ALEAFEHTAA 

       190        200        210        220        230        240 
YDVAISHWMG VRLSEQASQW LEAIPLRQRL RYGENPHQQA AWYSAPKQGW GGAIQLQGKE 

       250        260        270        280        290        300 
LSTNNLLDLE AALATVREFG YGTDGAHQAV QDAAVVVKHT NPCGVAIGTG VASALSRALD 

       310        320        330        340        350        360 
ADRVSAFGGI VALNGLVDAT TARELTSLFL ECVVAPGFEP EAREILASKA NLRLLELAPG 

       370        380        390        400        410        420 
AVDAAGRDHI RTILGGVLVQ DQDDQLIDPT SWTVASKRAP TAEENDDLTF AWRLVRHVRS 

       430        440        450        460        470        480 
NAIVVARAGQ SLGVGAGQMN RVGSARLALE AAGDQARGAV LASDGFFPFD DTVRLAANHG 

       490        500        510 
IRAVIQPGGS KRDADSIAVC DEFGLAMVLT GKRHFLH 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9303.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000554 Genomic DNA. Translation: ABM79216.1.
RefSeqYP_001018481.1. NC_008820.1.

3D structure databases

ProteinModelPortalA2CCK6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59922.P9303_24851.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM79216; ABM79216; P9303_24851.
GeneID4776758.
KEGGpmf:P9303_24851.
PATRIC23002519. VBIProMar17757_2546.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPMAR59922:GH54-2590-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_PROM3
AccessionPrimary (citable) accession number: A2CCK6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 20, 2007
Last modified: February 19, 2014
This is version 49 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