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Q46HA8 (PUR9_PROMT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 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
Ordered Locus Names:PMN2A_1632
OrganismProchlorococcus marinus (strain NATL2A) [Complete proteome] [HAMAP]
Taxonomic identifier59920 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length518 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 – 518518Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018934

Sequences

Sequence LengthMass (Da)Tools
Q46HA8 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: A2B43068CABC44AE

FASTA51856,649
        10         20         30         40         50         60 
MSPIALLSVS DKTGLIPLAK ALVNDLGFKI ISSGGTAKLI ESENLPVTRV ADYTGFPEIL 

        70         80         90        100        110        120 
GGRVKTLNPK IHGGILARRD KQSHLDDLDK QNINPIDLVV VNLYPFVKTI SKENVSWEEA 

       130        140        150        160        170        180 
IENIDIGGPT MIRAAAKNHQ DVLVVTDPSQ YSNLIDAYKS KKITTELRKK YSQQAFEHTA 

       190        200        210        220        230        240 
TYDLTISNWI ANQSSSKKVS WLQSLPLKQE LRYGENPHQK ASWYGEPEKG WSGANQLQGK 

       250        260        270        280        290        300 
ELSTNNLLDL EAALSTLREF GYKNNISNPS YQKAAVVIKH TNPCGVAIGD SPSSALKRAL 

       310        320        330        340        350        360 
DGDRVSAFGG IIAINCPVDE AAAKEIENIF IECVVAPYFD ETAKEILSKK KNLRLLELKA 

       370        380        390        400        410        420 
ESVQKADKNH IRSILGGLLI QDLDEPSIDQ KKWKSVTELI PTDEEMNDLS FAWKIVKHIR 

       430        440        450        460        470        480 
SNAIAVASNQ QSLGIGAGQM NRVGSAKLAL EAAGTKSKGA VLASDGFFPF DDTVKMASDY 

       490        500        510 
GISSIIQPGG SIRDEDSIKA CNELGIKMIL TGKRHFLH 

« 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: NATL2A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000095 Genomic DNA. Translation: AAZ59120.1.
RefSeqYP_292823.1. NC_007335.2.

3D structure databases

ProteinModelPortalQ46HA8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59920.PMN2A_1632.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ59120; AAZ59120; PMN2A_1632.
GeneID3607032.
KEGGpmn:PMN2A_1632.
PATRIC23022749. VBIProMar14922_0331.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.
PhylomeDBQ46HA8.

Enzyme and pathway databases

BioCycPMAR59920:GI1O-331-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_PROMT
AccessionPrimary (citable) accession number: Q46HA8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 13, 2005
Last modified: July 9, 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