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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Bartonella tribocorum (strain CIP 105476 / IBS 506)
Status
Reviewed-Annotation score: 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-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciBTRI382640:GJEK-2029-MONOMER.
UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein PurHUniRule annotation
Including the following 2 domains:
Phosphoribosylaminoimidazolecarboxamide formyltransferaseUniRule annotation (EC:2.1.2.3UniRule annotation)
Alternative name(s):
AICAR transformylaseUniRule annotation
IMP cyclohydrolaseUniRule annotation (EC:3.5.4.10UniRule annotation)
Alternative name(s):
ATICUniRule annotation
IMP synthaseUniRule annotation
InosinicaseUniRule annotation
Gene namesi
Name:purHUniRule annotation
Ordered Locus Names:BT_2562
OrganismiBartonella tribocorum (strain CIP 105476 / IBS 506)
Taxonomic identifieri382640 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella
ProteomesiUP000001592 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 539539Bifunctional purine biosynthesis protein PurHPRO_1000076474Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi382640.Btr_2562.

Structurei

3D structure databases

ProteinModelPortaliA9IZD0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000094758.
KOiK00602.
OMAiPCGVAEG.
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.

A9IZD0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVVAKNFPI PDLHRVRRIL LSVSDKTGVV AFAQALHATY SVELISTGGT
60 70 80 90 100
AKTLIAAGLP VKDVSEVTGF PEIMDGRVKT LHPLIHGALL GIREDPSHRE
110 120 130 140 150
AMEKNSIHGI DLLVVNLYPF EETIQSGADG KTILENIDIG GPAMIRAAAK
160 170 180 190 200
NYAYTGVVTA INDYDSILAE LKQHNGCLSL SMRHQLAMRA YAHTAAYDTA
210 220 230 240 250
IAAWFARDLK IETPSWQSFS GHLESVMRYG ENPHQQAAFY RNNEKRFGVA
260 270 280 290 300
TAKLLQGKAL SYNNLNDTDA AFELVAEFDP QKTAAVALIK HANPCGVAEG
310 320 330 340 350
ENLKDAYLKA LMCDNVSAFG GIVALNQTLD EECAEEIVKI FTEVIIAPDA
360 370 380 390 400
TMAAREIIAK KKNLRLLITG GIPNPRCGGL LAKTLAGGIL VQSRDNVVID
410 420 430 440 450
DLKLQVVTKR TPTQDEMRDL QFAFRVAKHV KSNAIVYAKN SATVGIGAGQ
460 470 480 490 500
MSRIDSAKIA ASKAAESARR AGLTETLTKG SVVASDAFFP FADGLLAAAA
510 520 530
AGATAVIQPG GSMRDEEVIT AADEQGLAMV FTGIRHFRH
Length:539
Mass (Da):57,832
Last modified:February 4, 2008 - v1
Checksum:i081EFFB0133DDDA5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM260525 Genomic DNA. Translation: CAK02522.1.
RefSeqiYP_001610517.1. NC_010161.1.

Genome annotation databases

KEGGibtr:Btr_2562.
PATRICi20552974. VBIBarTri113218_2604.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM260525 Genomic DNA. Translation: CAK02522.1.
RefSeqiYP_001610517.1. NC_010161.1.

3D structure databases

ProteinModelPortaliA9IZD0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi382640.Btr_2562.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGibtr:Btr_2562.
PATRICi20552974. VBIBarTri113218_2604.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000094758.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
BioCyciBTRI382640:GJEK-2029-MONOMER.

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.
ProtoNetiSearch...

Publicationsi

  1. "Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors."
    Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.
    Nat. Genet. 39:1469-1476(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CIP 105476 / IBS 506.

Entry informationi

Entry nameiPUR9_BART1
AccessioniPrimary (citable) accession number: A9IZD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 19, 2008
Last sequence update: February 4, 2008
Last modified: March 31, 2015
This is version 51 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.