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Q7TUG1 (PUR9_PROMP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 66. 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:PMM0266
OrganismProchlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4) [Complete proteome] [HAMAP]
Taxonomic identifier59919 [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_1000018932

Sequences

Sequence LengthMass (Da)Tools
Q7TUG1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 3F261B657AC56968

FASTA51757,418
        10         20         30         40         50         60 
MSPLALVSVS DKKNIIPFCT ELVEKFNYKI LSSGGTAKHL MEAKIPVIKV ADFTNSPEIL 

        70         80         90        100        110        120 
GGRVKTLHPK IHGGILAKRT DEEHKKDIEA YDLELIELVV VNLYPFKKTV EKGSKWEDAI 

       130        140        150        160        170        180 
ENIDIGGPSM IRSAAKNHKD VSVLVDPSQY QEFIEESKKG ELKETYKAKL ALEAFQHTAD 

       190        200        210        220        230        240 
YDTAISNWIR KERGLQSSKY IESYPLIKTL RYGENPHQKA FWYGLNNIGW NSAEQLQGKE 

       250        260        270        280        290        300 
LSYNNLLDLE SALSTVLEFG YEEKDELTTE TFASVILKHN NPCGASIGNS ASQAFLNALK 

       310        320        330        340        350        360 
CDSVSAFGGI VAFNSNVDSE TAINLKDIFL ECVVAPSFDP EALEILKIKK NLRILKFSKD 

       370        380        390        400        410        420 
QIPNKNQTST KSIMGGLLVQ DTDNIEEKTE SWITVTKKFP STQDYLDLSF AWKICKHIKS 

       430        440        450        460        470        480 
NAIVIAKDQQ TLGIGAGQMN RVGASKIALQ AAKENGYGGV LASDGFFPFA DTVELANEYG 

       490        500        510 
INSIIQPGGS IRDEESIEMC NLKGISMVFT NKRHFLH 

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCMP1986 / MED4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548174 Genomic DNA. Translation: CAE18725.1.
RefSeqNP_892385.1. NC_005072.1.

3D structure databases

ProteinModelPortalQ7TUG1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59919.PMM0266.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE18725; CAE18725; PMM0266.
GeneID1727240.
KEGGpmm:PMM0266.
PATRIC23031184. VBIProMar68066_0274.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMACNLKGIS.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycPMAR59919:GJMQ-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_PROMP
AccessionPrimary (citable) accession number: Q7TUG1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 66 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