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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Clostridium botulinum (strain Kyoto / Type A2)
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

BioCyciCBOT536232:GCO3-3174-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:CLM_3270
OrganismiClostridium botulinum (strain Kyoto / Type A2)
Taxonomic identifieri536232 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000001374 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499Bifunctional purine biosynthesis protein PurHPRO_1000122952Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi536232.CLM_3270.

Structurei

3D structure databases

ProteinModelPortaliC1FV76.
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.

C1FV76-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIKRALISVF DKTGILDLAK FLESRDVEII STGGTYKHLK ENGVKVIDIE
60 70 80 90 100
EVTGFPEMLD GRVKTLNPLI HGGILAIRDN EEHMKVIEEK GINPIDMVVV
110 120 130 140 150
NLYPFFNKVE ENLSFDEKVE FIDIGGPTMI RAAAKNFKDV VVLTDTKDYE
160 170 180 190 200
NVINEIKENN QVNTQTRKKL AGKVFNLMSA YDAAISNFLL EEEYPEYLTL
210 220 230 240 250
SYKKNMDLRY GENPHQTAAY YTSTVGKYPM KNFEKLNGKE LSYNNIKDMD
260 270 280 290 300
IAWKTVCEFE EVACCALKHN TPCGVAIGDT VQEAYTKAYE CDPISIFGGI
310 320 330 340 350
VAFNRKVDKE TAENLAKIFL EIVVAPDFDE DALEVLKNKK NLRVIKCEEK
360 370 380 390 400
STEGKDMAKV DGGILVQKSD NKLLENTKVV TEKSPTEQEM KDLIFGMKVV
410 420 430 440 450
KYVKSNAIVV VKDGMAKGIG GGQVNRIWAA KEALDRAGDG VVLASDAFFP
460 470 480 490
FGDVAEEAAK WGIKAIIQPG GSIRDEESIK VCNEKGISMV FTGIRHFKH
Length:499
Mass (Da):55,734
Last modified:May 25, 2009 - v1
Checksum:iF1B9691379E98906
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001581 Genomic DNA. Translation: ACO87280.1.
RefSeqiYP_002805397.1. NC_012563.1.

Genome annotation databases

EnsemblBacteriaiACO87280; ACO87280; CLM_3270.
KEGGicby:CLM_3270.
PATRICi19382963. VBICloBot91161_3107.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001581 Genomic DNA. Translation: ACO87280.1.
RefSeqiYP_002805397.1. NC_012563.1.

3D structure databases

ProteinModelPortaliC1FV76.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi536232.CLM_3270.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACO87280; ACO87280; CLM_3270.
KEGGicby:CLM_3270.
PATRICi19382963. VBICloBot91161_3107.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230373.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
BioCyciCBOT536232:GCO3-3174-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. "Genome sequence of Clostridium botulinum A2 Kyoto."
    Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C., Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
    Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Kyoto / Type A2.

Entry informationi

Entry nameiPUR9_CLOBJ
AccessioniPrimary (citable) accession number: C1FV76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 27, 2009
Last sequence update: May 25, 2009
Last modified: March 31, 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.