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Q62HA6

- PUR9_BURMA

UniProt

Q62HA6 - PUR9_BURMA

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Protein
Bifunctional purine biosynthesis protein PurH
Gene
purH, BMA2356
Organism
Burkholderia mallei (strain ATCC 23344)
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

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:BMA2356
OrganismiBurkholderia mallei (strain ATCC 23344)
Taxonomic identifieri243160 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
ProteomesiUP000006693: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 521521Bifunctional purine biosynthesis protein PurHUniRule annotation
PRO_1000018856Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243160.BMA2356.

Structurei

3D structure databases

ProteinModelPortaliQ62HA6.

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.
HOGENOMiHOG000230372.
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.

Q62HA6-1 [UniParc]FASTAAdd to Basket

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MIKQALISVS DKTGIVDFAK ALSALGVKLL STGGTAKLLA DAGLPVTEVA    50
DYTGFPEMLD GRVKTLHPKV HGGILARRDL PEHMQALEAH GIPTIDLLVV 100
NLYPFVQTIA KDDCTLADAI ENIDIGGPTM LRSAAKNHRD VTVVVDPADY 150
AVVLDEMKAN GNTLGYKTNF RLATKVFAHT AQYDGAITNY LTSLGDDLQH 200
GSRSAYPATL NLAFDKVQDL RYGENPHQSA AFYRDVATPA GALANYRQLQ 250
GKELSYNNIA DSDAAWECVK TFDAPACVII KHANPCGVAV GADAGEAYAK 300
AFQTDPTSAF GGIIAFNREV DEAAAQAVAK QFVEVLIAPS FSDAAKQVFA 350
AKQNVRLLEI ALGEGHNAFD LKRVGGGLLV QSLDSKNVQP RELRVVTKRH 400
PTPKEMDDLL FAWRVAKYVK SNAIVFCGNG MTLGVGAGQM SRVDSARIAS 450
IKAQNAGLTL AGSAVASDAF FPFRDGLDVV VAAGATCVIQ PGGSVRDDEV 500
IAAADEHNIA MVVTGVRHFR H 521
Length:521
Mass (Da):55,458
Last modified:October 25, 2004 - v1
Checksum:iCDDA7B76B25BB0E6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000010 Genomic DNA. Translation: AAU50213.1.
RefSeqiYP_103914.1. NC_006348.1.

Genome annotation databases

EnsemblBacteriaiAAU50213; AAU50213; BMA2356.
GeneIDi3090465.
KEGGibma:BMA2356.
PATRICi19119845. VBIBurMal55007_2427.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000010 Genomic DNA. Translation: AAU50213.1 .
RefSeqi YP_103914.1. NC_006348.1.

3D structure databases

ProteinModelPortali Q62HA6.
ModBasei Search...

Protein-protein interaction databases

STRINGi 243160.BMA2356.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAU50213 ; AAU50213 ; BMA2356 .
GeneIDi 3090465.
KEGGi bma:BMA2356.
PATRICi 19119845. VBIBurMal55007_2427.

Phylogenomic databases

eggNOGi COG0138.
HOGENOMi HOG000230372.
KOi K00602.
OMAi RAFKTDP.
OrthoDBi EOG6QCDFF.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .

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 23344.

Entry informationi

Entry nameiPUR9_BURMA
AccessioniPrimary (citable) accession number: Q62HA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 25, 2004
Last modified: May 14, 2014
This is version 61 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

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