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A9R8E1

- PUR9_YERPG

UniProt

A9R8E1 - PUR9_YERPG

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Protein
Bifunctional purine biosynthesis protein PurH
Gene
purH, YpAngola_A0465
Organism
Yersinia pestis bv. Antiqua (strain Angola)
Status
Reviewed - Annotation score: 3 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
Complete GO annotation...

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

BioCyciYPES349746:GHPB-465-MONOMER.
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
Ordered Locus Names:YpAngola_A0465
OrganismiYersinia pestis bv. Antiqua (strain Angola)
Taxonomic identifieri349746 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000001204: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 529529Bifunctional purine biosynthesis protein PurHUniRule annotation
PRO_1000096112Add
BLAST

Proteomic databases

PRIDEiA9R8E1.

Interactioni

Protein-protein interaction databases

STRINGi349746.YpAngola_A0465.

Structurei

3D structure databases

ProteinModelPortaliA9R8E1.

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230372.
KOiK00602.
OMAiRAFKTDP.
OrthoDBiEOG6QCDFF.

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.

A9R8E1-1 [UniParc]FASTAAdd to Basket

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MQQRRPIRRA LLSVSDKAGI IEFAQALSQR GIELLSTGGT ARLLADAGLP    50
VTEVSDYTGF PEMMDGRVKT LHPKVHGGIL GRRGQDDGIM AQHGIQPIDI 100
VVVNLYPFAQ TVARPDCSLE DAVENIDIGG PTMVRSAAKN HKDVAIVVKS 150
SDYPAIITEL DNNDGSLTYP TRFNLAIKAF EHTAAYDSMI ANYFGTLVPP 200
YHGDTEQPSG HFPRTLNLNY IKKQDMRYGE NSHQQAAFYI EEDVKEASVA 250
TAQQLQGKAL SYNNIADTDA ALECVKEFSE PACVIVKHAN PCGVAIGDSI 300
LAAYERAYQT DPTSAFGGII AFNRELDAAT ASAIISRQFV EVIIAPTVSS 350
DALALLAAKQ NVRVLTCGQW QARSAGLDFK RVNGGLLVQE RDLGMVTAAD 400
LRVVSKRQPT EQELRDALFC WKVAKFVKSN AIVYARDNMT IGIGAGQMSR 450
VYSAKIAGIK AADEGLEVAG SAMASDAFFP FRDGIDAAAA VGITCVIQPG 500
GSIRDDEVIA AADEHSIAMI FTDMRHFRH 529
Length:529
Mass (Da):57,154
Last modified:February 5, 2008 - v1
Checksum:i5A76A59B82F39BFE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000901 Genomic DNA. Translation: ABX85892.1.
RefSeqiYP_001605070.1. NC_010159.1.

Genome annotation databases

EnsemblBacteriaiABX85892; ABX85892; YpAngola_A0465.
GeneIDi5798929.
KEGGiypg:YpAngola_A0465.
PATRICi18569892. VBIYerPes97331_0767.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000901 Genomic DNA. Translation: ABX85892.1 .
RefSeqi YP_001605070.1. NC_010159.1.

3D structure databases

ProteinModelPortali A9R8E1.
ModBasei Search...

Protein-protein interaction databases

STRINGi 349746.YpAngola_A0465.

Proteomic databases

PRIDEi A9R8E1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABX85892 ; ABX85892 ; YpAngola_A0465 .
GeneIDi 5798929.
KEGGi ypg:YpAngola_A0465.
PATRICi 18569892. VBIYerPes97331_0767.

Phylogenomic databases

eggNOGi COG0138.
HOGENOMi HOG000230372.
KOi K00602.
OMAi RAFKTDP.
OrthoDBi EOG6QCDFF.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .
BioCyci YPES349746:GHPB-465-MONOMER.

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. "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals new insights into the evolution and pangenome of the plague bacterium."
    Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S., Achtman M., Lindler L.E., Ravel J.
    J. Bacteriol. 192:1685-1699(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Angola.

Entry informationi

Entry nameiPUR9_YERPG
AccessioniPrimary (citable) accession number: A9R8E1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: May 14, 2014
This is version 49 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

Complete proteome, 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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