Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131)
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

Pathway: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route).UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional purine biosynthesis protein PurH (purH)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route), the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Pathway: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional purine biosynthesis protein PurH (purH)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

GO - Molecular functioni

GO - Biological processi

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 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:FN0982
OrganismiFusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131)
Taxonomic identifieri190304 [NCBI]
Taxonomic lineageiBacteriaFusobacteriaFusobacterialesFusobacteriaceaeFusobacterium
ProteomesiUP000002521 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 504504Bifunctional purine biosynthesis protein PurHPRO_0000192094Add
BLAST

Proteomic databases

PRIDEiQ8REV6.

Interactioni

Protein-protein interaction databases

STRINGi190304.FN0982.

Structurei

3D structure databases

ProteinModelPortaliQ8REV6.
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.
HOGENOMiHOG000230372.
InParanoidiQ8REV6.
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.

Q8REV6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKRALISVY DKTGILDFAK FLVSKGIEII STGGTYKYLK ENNIEVIEVS
60 70 80 90 100
KITNFEEMLD GRVKTLHPNI HGGILALRDN EEHMRTLKER NIDTIDYVIV
110 120 130 140 150
NLYPFFEKVK EDLSFEEKIE FIDIGGPTML RSAAKSFKNV VVISDVKDYE
160 170 180 190 200
SIKEEINKSD DVSYEARKKL AGKVFNLTSA YDAAISQFLL DEDFSEYLNI
210 220 230 240 250
SYKKFMEMRY GENSHQKAAY YTDNMTDGAM KDFKQLNGKE LSYNNIRDMD
260 270 280 290 300
LAWKVVSEFD EICCCAVKHS TPCGVALGDN VEGAYKKAYE TDPVSIFGGI
310 320 330 340 350
VAFNREVDEA TAKLLNEIFL EIIIAPSFSK AALEILTKKK NIRLIECKNK
360 370 380 390 400
PSDKKELIKV DGGILIQDTN NKLYEDLEVV TKAKPTSQEE KDLIFALKVV
410 420 430 440 450
KFVKSNAIVV AKNLQTLGIG GGEVSRIWAA EKALERAKER FNATDVVLSS
460 470 480 490 500
DAFFPFKDVI ELAAKNGVKA IIQPSGSVND KDSIEECDRN NISMIFSKLR

HFKH
Length:504
Mass (Da):56,927
Last modified:June 1, 2002 - v1
Checksum:iADCA67143AE64433
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009951 Genomic DNA. Translation: AAL95178.1.
RefSeqiNP_603879.1. NC_003454.1.
WP_011016803.1. NC_003454.1.

Genome annotation databases

EnsemblBacteriaiAAL95178; AAL95178; FN0982.
GeneIDi991332.
KEGGifnu:FN0982.
PATRICi21951729. VBIFusNuc122357_1547.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009951 Genomic DNA. Translation: AAL95178.1.
RefSeqiNP_603879.1. NC_003454.1.
WP_011016803.1. NC_003454.1.

3D structure databases

ProteinModelPortaliQ8REV6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi190304.FN0982.

Proteomic databases

PRIDEiQ8REV6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL95178; AAL95178; FN0982.
GeneIDi991332.
KEGGifnu:FN0982.
PATRICi21951729. VBIFusNuc122357_1547.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230372.
InParanoidiQ8REV6.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131.

Entry informationi

Entry nameiPUR9_FUSNN
AccessioniPrimary (citable) accession number: Q8REV6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 1, 2002
Last modified: April 29, 2015
This is version 82 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

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.