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A9BDN8 (PUR9_PROM4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 47. 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:P9211_02931
OrganismProchlorococcus marinus (strain MIT 9211) [Complete proteome] [HAMAP]
Taxonomic identifier93059 [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_1000096082

Sequences

Sequence LengthMass (Da)Tools
A9BDN8 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: B8AFE8AE84470FF9

FASTA51856,123
        10         20         30         40         50         60 
MARIALISVS NKDGLIPFAK TLTTLHGFEI ISSGGTARAL KEANIPVKTV SDYTGAPEIL 

        70         80         90        100        110        120 
GGRVKTLHPR IHGGILAKQG NSSHQFDLEK ENIKNIDLVV VNLYPFQETI SDPDVTWDNA 

       130        140        150        160        170        180 
IENIDIGGPA MIRAAAKNHE SVSILTNPNQ YDAFLEKLEA GEISTTIKAK LALEAFEHTA 

       190        200        210        220        230        240 
SYDIAISQWL SKQIESKYSP YLTSQPIKQT LRYGENPHQN ANWYSAVNQG WGQAEQLQGK 

       250        260        270        280        290        300 
ELSTNNLLDL EAAVATIREF GYDLGNKGNS CEKAAVIIKH TNPCGVAVSN NLSNAFNLAL 

       310        320        330        340        350        360 
ECDSISAFGG IVALNCNLDA ATAKELSSLF LECVVAPDYD ANALEILSTK KNLRIIKLSH 

       370        380        390        400        410        420 
SSIKSSERKY IRSILGGILV QEVDDKLIEP NEWKVPTKLQ MSIEDKADLA FAWRVVRHVR 

       430        440        450        460        470        480 
SNAIVVASAG QTLGIGAGQM NRIGAAKIAL EAAGEKAQGA VLASDGFFPF DDTVHLASRY 

       490        500        510 
GIKSIIQPGG SIRDQSSIDA CNQLGLSMIF 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: MIT 9211.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000878 Genomic DNA. Translation: ABX08224.1.
RefSeqYP_001550178.1. NC_009976.1.

3D structure databases

ProteinModelPortalA9BDN8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93059.P9211_02931.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX08224; ABX08224; P9211_02931.
GeneID5731796.
KEGGpmj:P9211_02931.
PATRIC22986032. VBIProMar136502_0311.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMACNLKGIS.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycPMAR93059:GHJV-298-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_PROM4
AccessionPrimary (citable) accession number: A9BDN8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 15, 2008
Last modified: May 14, 2014
This is version 47 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