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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Vibrio tasmaniensis (strain LGP32) (Vibrio splendidus (strain Mel32))
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

BioCyciVSPL575788:GH64-2897-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:VS_2951
OrganismiVibrio tasmaniensis (strain LGP32) (Vibrio splendidus (strain Mel32))
Taxonomic identifieri575788 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000009100 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 530530Bifunctional purine biosynthesis protein PurHPRO_1000122980Add
BLAST

Proteomic databases

PRIDEiB7VM57.

Interactioni

Protein-protein interaction databases

STRINGi575788.VS_2951.

Structurei

3D structure databases

ProteinModelPortaliB7VM57.
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.

B7VM57-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNARPIRRA LISVSDKTGI VEFAQALANR GVDILSTGGT ARLLAEKGIS
60 70 80 90 100
VTEVSDYTGF PEMMDGRVKT LHPKVHGGVL GRRGQDDDVM ETHGINPIDM
110 120 130 140 150
VVVNLYPFAE TVAKEGCTLA DAVENIDIGG PTMVRSAAKN HKDVTIVVNA
160 170 180 190 200
HDYERVVAEM DANEKSLTLE TRFDLAIAAF EHTASYDGMI ANYFGTMVPS
210 220 230 240 250
YGENKEGDEE SKFPRTFNQQ FEKKQDMRYG ENSHQAAAFY VEANPEEASV
260 270 280 290 300
STARQIQGKA LSYNNIADTD AALECVKEFD EPACVIVKHA NPCGVALGED
310 320 330 340 350
ILEAYDRAFK TDPTSAFGGI IAFNRELDAA TATAITERQF VEVIIAPSVS
360 370 380 390 400
AEAVAIVAAK KNLRLLECGE WTTKTTGFDV KRVNGGLLVQ DRDQGMVSED
410 420 430 440 450
DLKVVSKRQP TAEELKDALF CWKVAKYVKS NAIVYSKGDM TIGVGAGQMS
460 470 480 490 500
RVYSAKIAGI KAADEGLQVE GCVMASDAFF PFRDGIDAAA EAGIKCVIQP
510 520 530
GGSMRDDEVI AAADEHGMAM IFTGMRHFRH
Length:530
Mass (Da):57,425
Last modified:February 10, 2009 - v1
Checksum:i0FBA08B4FCCE3945
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FM954972 Genomic DNA. Translation: CAV20247.1.
RefSeqiWP_012604990.1. NC_011753.2.
YP_002418488.1. NC_011753.2.

Genome annotation databases

EnsemblBacteriaiCAV20247; CAV20247; VS_2951.
GeneIDi7162434.
KEGGivsp:VS_2951.
PATRICi20156436. VBIVibSpl48387_4160.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FM954972 Genomic DNA. Translation: CAV20247.1.
RefSeqiWP_012604990.1. NC_011753.2.
YP_002418488.1. NC_011753.2.

3D structure databases

ProteinModelPortaliB7VM57.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi575788.VS_2951.

Proteomic databases

PRIDEiB7VM57.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAV20247; CAV20247; VS_2951.
GeneIDi7162434.
KEGGivsp:VS_2951.
PATRICi20156436. VBIVibSpl48387_4160.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230373.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
BioCyciVSPL575788:GH64-2897-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. "Vibrio splendidus str. LGP32 complete genome."
    Mazel D., Le Roux F.
    Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LGP32.

Entry informationi

Entry nameiPUR9_VIBTL
AccessioniPrimary (citable) accession number: B7VM57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: May 27, 2015
This is version 48 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.