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Q9RW01

- PUR9_DEIRA

UniProt

Q9RW01 - PUR9_DEIRA

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Protein
Bifunctional purine biosynthesis protein PurH
Gene
purH, DR_0868
Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
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

BioCyciDRAD243230:GH46-891-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:DR_0868
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
ProteomesiUP000002524: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 510510Bifunctional purine biosynthesis protein PurHUniRule annotation
PRO_0000192090Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243230.DR_0868.

Structurei

3D structure databases

ProteinModelPortaliQ9RW01.

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.
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.

Q9RW01-1 [UniParc]FASTAAdd to Basket

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MTKRALISVS DKTGVVEFAA QLQQRGWELL STGGTFATLS GAGIPVRQVS    50
DVTGFPEMLD GRVKTLHPAI HGGILARREA GHLGQLAAQD IGTIDLVCVN 100
LYPFRETVAR GAPDPEVIEN IDIGGPAMIR SAAKNHDAVL VLVDPADYAL 150
ALQDEVSPAE RRRLAAKAYR HTSEYDAAIT AYLSGESDEL PTQLPEHLSL 200
DLTRTAQVRY GENPHQPGAI YRWGNARGPV IDAQVVAGKP MSFNNYADAD 250
AAWSLCQELA AQEQGAVCVA VKHANPCGVA VAADVKTAWE RARDADTLSV 300
FGGVVAVSQP VDFGAAQSMK GTFLEVLIAP DVTPDAVEWF AAKKPDLRVL 350
IAGQPQGVSV LDVRPLTGGF AVQERDARPW DDLCPEVVTE RQPSEQEWAD 400
LRFAWAVVKG ARSNAVALCK GGVTVGLGAG AVSRIWAAER AIANAGEAAQ 450
GAVLASEAFF PFDDVVRLAA SAGVTAVLQP GGAKRDPEVI AACNELGISM 500
VFTGSRHFRH 510
Length:510
Mass (Da):54,046
Last modified:June 20, 2003 - v2
Checksum:i668734C53416269C
GO

Sequence cautioni

The sequence AAF10444.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000513 Genomic DNA. Translation: AAF10444.1. Different initiation.
PIRiB75467.
RefSeqiNP_294592.1. NC_001263.1.

Genome annotation databases

EnsemblBacteriaiAAF10444; AAF10444; DR_0868.
GeneIDi1797790.
KEGGidra:DR_0868.
PATRICi21629294. VBIDeiRad64572_1052.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000513 Genomic DNA. Translation: AAF10444.1 . Different initiation.
PIRi B75467.
RefSeqi NP_294592.1. NC_001263.1.

3D structure databases

ProteinModelPortali Q9RW01.
ModBasei Search...

Protein-protein interaction databases

STRINGi 243230.DR_0868.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF10444 ; AAF10444 ; DR_0868 .
GeneIDi 1797790.
KEGGi dra:DR_0868.
PATRICi 21629294. VBIDeiRad64572_1052.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .
BioCyci DRAD243230:GH46-891-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: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.

Entry informationi

Entry nameiPUR9_DEIRA
AccessioniPrimary (citable) accession number: Q9RW01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 20, 2003
Last modified: May 14, 2014
This is version 85 of the entry and version 2 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

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