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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87)
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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciTYEL289376:GH9L-1236-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:THEYE_A1243
OrganismiThermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87)
Taxonomic identifieri289376 [NCBI]
Taxonomic lineageiBacteriaNitrospiraeNitrospiralesNitrospiraceaeThermodesulfovibrio
ProteomesiUP000000718 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 522522Bifunctional purine biosynthesis protein PurHPRO_1000096105Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi289376.THEYE_A1243.

Structurei

3D structure databases

ProteinModelPortaliB5YLE5.
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.
HOGENOMiHOG000230372.
InParanoidiB5YLE5.
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.

B5YLE5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKRALISVS DKRGLVDFAK ELDKLGVEIL STGGTAKTLR DSGIKVIDVS
60 70 80 90 100
QYTGFPEIMD GRVKTLHPLI HGGILARRDN KEDIEAMERL GIKPIDMVVV
110 120 130 140 150
NLYPFESVAK KHLSQILQPS DLNLQAFLEE AIENIDIGGP TLLRASAKNY
160 170 180 190 200
KDVIVIVDPD DYSSIIEDIK KGSVSIEKKF ELAKKVFSHT ARYDALIADY
210 220 230 240 250
FEKISPSGFK KDWTLPLKMT RTLRYGENPH QKAALYALNE SPSLIDADVL
260 270 280 290 300
QGKEMSFNNY LDTHSAVLLA TEFSEPVCVI VKHNNPCGVA IGENIHTAYK
310 320 330 340 350
KAFECDPVSA FGGIIAFNRV VDKETASEII NTFYEVIVAP DFDKDALEVF
360 370 380 390 400
ETKKNLRLLR FPSLSDKIQP SGFDLKRILG GFIVQEWDKV DNEFSQAKVV
410 420 430 440 450
TKRQPTDEEW KALKFAWKVC KHIKSNAVVY AKEDRTVGLG IGQTSRVFSA
460 470 480 490 500
KIGAMHALSS LKGTVVASDG FFPFRDNIDV LAQNGVTSII QPGGSVRDQE
510 520
VIDAANQYNI AMVFTGIRHF RH
Length:522
Mass (Da):58,100
Last modified:November 25, 2008 - v1
Checksum:i83323A65C8570910
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001147 Genomic DNA. Translation: ACI21021.1.
RefSeqiWP_012545749.1. NC_011296.1.
YP_002249060.1. NC_011296.1.

Genome annotation databases

EnsemblBacteriaiACI21021; ACI21021; THEYE_A1243.
GeneIDi6943286.
KEGGitye:THEYE_A1243.
PATRICi23909503. VBITheYel104483_1215.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001147 Genomic DNA. Translation: ACI21021.1.
RefSeqiWP_012545749.1. NC_011296.1.
YP_002249060.1. NC_011296.1.

3D structure databases

ProteinModelPortaliB5YLE5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi289376.THEYE_A1243.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACI21021; ACI21021; THEYE_A1243.
GeneIDi6943286.
KEGGitye:THEYE_A1243.
PATRICi23909503. VBITheYel104483_1215.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230372.
InParanoidiB5YLE5.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
BioCyciTYEL289376:GH9L-1236-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. "The complete genome sequence of Thermodesulfovibrio yellowstonii strain ATCC 51303 / DSM 11347 / YP87."
    Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.
    Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51303 / DSM 11347 / YP87.

Entry informationi

Entry nameiPUR9_THEYD
AccessioniPrimary (citable) accession number: B5YLE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 25, 2008
Last modified: April 29, 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, Reference proteome

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.