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Q9F1T4

- PUR9_STRSU

UniProt

Q9F1T4 - PUR9_STRSU

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Protein
Bifunctional purine biosynthesis protein PurH
Gene
purH
Organism
Streptococcus suis
Status
Reviewed - Annotation score: 2 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotation
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotation

Pathwayi

GO - Molecular functioni

  1. IMP cyclohydrolase activity Source: UniProtKB-HAMAP
  2. phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein PurH
Including the following 2 domains:
Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC:2.1.2.3)
Alternative name(s):
AICAR transformylase
IMP cyclohydrolase (EC:3.5.4.10)
Alternative name(s):
ATIC
IMP synthase
Inosinicase
Gene namesi
Name:purH
OrganismiStreptococcus suis
Taxonomic identifieri1307 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 515515Bifunctional purine biosynthesis protein PurHUniRule annotation
PRO_0000192139Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ9F1T4.

Family & Domainsi

Domaini

The IMP cyclohydrolase activity resides in the N-terminal region By similarity.UniRule annotation

Sequence similaritiesi

Belongs to the PurH family.

Family and domain databases

Gene3Di3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPiMF_00139. PurH.
InterProiIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERiPTHR11692. PTHR11692. 1 hit.
PfamiPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFiPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTiSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR00355. purH. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9F1T4-1 [UniParc]FASTAAdd to Basket

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MTKRALISVS DKNGIVEFAQ ELTKFGWEII STGGTKVALD QAGVTTIAID    50
DVTGFPEMMD GRVKTLHPKI HGGLLARRDL DSHLQAANDH EIGLIDLVVV 100
NLYPFKETIL RPDVTYDLAV ENIDIGGPSM LRSAAKNHAS VTVVVDPADY 150
PTVLGEIAEQ GETSYATRQR LAAKVFRHTA AYDALIADYF TKQVGEDKPE 200
KLTITYDLNQ PMRYGENPQQ NADFYQNALP TAYSIAAAKQ LNGKELSFNN 250
IRDADAAIRI IRDFKDRPTV VALKHMNPCG IGQAETIEQA WDYAYEADPV 300
SIFGGIVVLN REVDAATAEK MHPIFLEIII APGYSAEALA ILTNKKKNLR 350
ILELAFDAQD ASEVEKEFTG VVGGLLVQDQ DVVVESPVDW QVVTERQPSE 400
QEWAAMEFAW KSSKYVKSNG IIITNDKMTL GVGPGQTNRV ASVRIAIEQA 450
KDRLEGAVLA SDAFFPFADN VEEIAAAGIK AIIQPGGSVR DQDSIDMANK 500
YGLTMVFTGV RHFRH 515
Length:515
Mass (Da):56,511
Last modified:March 1, 2001 - v1
Checksum:i92D3B3B63F39288A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB045609 Genomic DNA. Translation: BAB20827.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB045609 Genomic DNA. Translation: BAB20827.1 .

3D structure databases

ProteinModelPortali Q9F1T4.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .

Family and domain databases

Gene3Di 3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPi MF_00139. PurH.
InterProi IPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view ]
PANTHERi PTHR11692. PTHR11692. 1 hit.
Pfami PF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view ]
PIRSFi PIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTi SM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view ]
SUPFAMi SSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsi TIGR00355. purH. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Evidence for horizontal transfer of the SsuDAT1I restriction-modification genes to the Streptococcus suis genome."
    Sekizaki T., Otani Y., Osaki M., Takamatsu D., Shimoji Y.
    J. Bacteriol. 183:500-511(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: DAT1 / Serotype 2.

Entry informationi

Entry nameiPUR9_STRSU
AccessioniPrimary (citable) accession number: Q9F1T4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: March 1, 2001
Last modified: February 19, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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