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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Rhizobium leguminosarum bv. trifolii (strain WSM2304)
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

BioCyciRLEG395492:GJB3-3971-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:Rleg2_3915
OrganismiRhizobium leguminosarum bv. trifolii (strain WSM2304)
Taxonomic identifieri395492 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium
ProteomesiUP000008330: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 538538Bifunctional purine biosynthesis protein PurHPRO_1000096087Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi395492.Rleg2_3915.

Structurei

3D structure databases

ProteinModelPortaliB5ZV31.
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.
HOGENOMiHOG000230373.
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.

B5ZV31-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVISKKIPA PDKVEIKTAL LSVFDKTGIV ELAQALSEQG VRLLSTGGTY
60 70 80 90 100
KAIAAAGLAV TDVSEITGFP EIMDGRVKTL HPTVHGGLLA IRDDSEHQEA
110 120 130 140 150
MKTHGIEAID LAVINLYPFE DVRAAGGDYP TTVENIDIGG PAMIRASAKN
160 170 180 190 200
HAYVTILTDP NDYAEFTEQL SADGGKTAYA FRQRMAAKAY ARTAAYDAVI
210 220 230 240 250
SNWFAEALSI DTPRHRVIGG ALKEEMRYGE NPHQKAAFYV TGEKRPGVST
260 270 280 290 300
AALLQGKQLS YNNINDTDAA YELVAEFLPE KEPACAIIKH ANPCGVATGS
310 320 330 340 350
SLVEAYRRAL ACDSVSAFGG IIALNRTLDA ETAEEIVKLF TEVIIAPDVT
360 370 380 390 400
EEAKAIIARK PNLRLLSAGG LPDPRAAGLT AKTVSGGLLV QSRDNGMVED
410 420 430 440 450
LELKVVTKRA PTAQELDDMK FAFKIGKHVK SNAVVYAKDG QTAGIGAGQM
460 470 480 490 500
SRVDSARIAA LKAEEAAKAL GLAVPMTHGS AVASEAFLPF ADGLLSMIAA
510 520 530
GATAVIQPGG SMRDQEVIDA ADEHGIAMVF TGMRHFRH
Length:538
Mass (Da):57,027
Last modified:November 25, 2008 - v1
Checksum:i00D02314897764F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001191 Genomic DNA. Translation: ACI57177.1.
RefSeqiWP_012559376.1. NC_011369.1.
YP_002283403.1. NC_011369.1.

Genome annotation databases

EnsemblBacteriaiACI57177; ACI57177; Rleg2_3915.
GeneIDi6982679.
KEGGirlt:Rleg2_3915.
PATRICi23132116. VBIRhiLeg95088_5857.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001191 Genomic DNA. Translation: ACI57177.1.
RefSeqiWP_012559376.1. NC_011369.1.
YP_002283403.1. NC_011369.1.

3D structure databases

ProteinModelPortaliB5ZV31.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi395492.Rleg2_3915.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACI57177; ACI57177; Rleg2_3915.
GeneIDi6982679.
KEGGirlt:Rleg2_3915.
PATRICi23132116. VBIRhiLeg95088_5857.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230373.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
BioCyciRLEG395492:GJB3-3971-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. "Complete sequence of chromosome of Rhizobium leguminosarum bv. trifolii WSM2304."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Yates R.
    , Ardley J., Tiwari R.P., O'Hara G., Howieson J., Brau L., Reeve W.
    Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: WSM2304.

Entry informationi

Entry nameiPUR9_RHILW
AccessioniPrimary (citable) accession number: B5ZV31
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 25, 2008
Last modified: February 4, 2015
This is version 45 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.