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C3MAR5

- PUR9_RHISN

UniProt

C3MAR5 - PUR9_RHISN

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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Rhizobium sp. (strain NGR234)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

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

BioCyciSFRE394:GBYN-3312-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:NGR_c33280
OrganismiRhizobium sp. (strain NGR234)
Taxonomic identifieri394 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
ProteomesiUP000001054: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 536536Bifunctional purine biosynthesis protein PurHPRO_1000122968Add
BLAST

Proteomic databases

ProMEXiC3MAR5.

Interactioni

Protein-protein interaction databases

STRINGi394.NGR_c33280.

Structurei

3D structure databases

ProteinModelPortaliC3MAR5.
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.
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.

C3MAR5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVASKKIPA PDEVRIQTAL LSVSDKAGIV ELARALHGKG VRLVSTGGTH
60 70 80 90 100
KALAAAGLPV SDVSELTGFP EVMDGRVKTL HPGVHGGLLA IRDDADHKAA
110 120 130 140 150
MDEHGITGID LAVINLYPFE EVRAQGGDYP TTVENIDIGG PAMIRASAKN
160 170 180 190 200
HAYVTIVTDP ADYSALLEEI ADGTTRYAFR QKMAAKAYAR TAAYDAAISN
210 220 230 240 250
WFAEALDLAM PRHRVIGGVL KEEMRYGENP HQKAGFYVTG EQRPGVATAA
260 270 280 290 300
LLQGKQLSYN NINDTDAAFE LVAEFLPEKA PACAIIKHAN PCGVATAPSL
310 320 330 340 350
TEAYRRALAC DSTSAFGGII ALNQELDAET AEEIVKLFTE VIIAPSVSDE
360 370 380 390 400
AKAIIARKPN LRLLAAGGLP DARTPGLTAK TVAGGLLVQT RDNGMVEDLE
410 420 430 440 450
LKVVTKRAPT AQELEDMKFA FKVAKHVKSN AVVYAKDGQT AGIGAGQMSR
460 470 480 490 500
VDSARIAAIK AEEAARAHGL AAPLTRGSAV ASEAFLPFAD GLLSAIAAGA
510 520 530
TAVIQPGGSM RDEEVIAAAN EHNVAMVFTG MRHFRH
Length:536
Mass (Da):56,436
Last modified:June 16, 2009 - v1
Checksum:i396CEC3E68E713E0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001389 Genomic DNA. Translation: ACP27058.1.
RefSeqiYP_002827811.1. NC_012587.1.

Genome annotation databases

EnsemblBacteriaiACP27058; ACP27058; NGR_c33280.
GeneIDi7792595.
KEGGirhi:NGR_c33280.
PATRICi32313181. VBIRhiSp122450_6170.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001389 Genomic DNA. Translation: ACP27058.1 .
RefSeqi YP_002827811.1. NC_012587.1.

3D structure databases

ProteinModelPortali C3MAR5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 394.NGR_c33280.

Proteomic databases

ProMEXi C3MAR5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACP27058 ; ACP27058 ; NGR_c33280 .
GeneIDi 7792595.
KEGGi rhi:NGR_c33280.
PATRICi 32313181. VBIRhiSp122450_6170.

Phylogenomic databases

eggNOGi COG0138.
HOGENOMi HOG000230373.
KOi K00602.
OMAi RAFKTDP.
OrthoDBi EOG6QCDFF.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .
BioCyci SFRE394:GBYN-3312-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NGR234.

Entry informationi

Entry nameiPUR9_RHISN
AccessioniPrimary (citable) accession number: C3MAR5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 16, 2009
Last modified: October 1, 2014
This is version 40 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