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
Nitrosococcus oceani (strain ATCC 19707 / NCIMB 11848)
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:iIMP 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:iIMP 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

BioCyciNOCE323261:GCI3-1063-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:Noc_1048
OrganismiNitrosococcus oceani (strain ATCC 19707 / NCIMB 11848)
Taxonomic identifieri323261 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeNitrosococcus
ProteomesiUP000006838 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 522522Bifunctional purine biosynthesis protein PurHPRO_1000057900Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi323261.Noc_1048.

Structurei

3D structure databases

ProteinModelPortaliQ3JC90.
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.

Q3JC90-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPIARALIS VSDKTGIVPF AHRLQARGVK ILSTGGSAQL LQKNNIGATE
60 70 80 90 100
ISTYTGFPEM MGGRIKTLHP KIHGGILGRR ETDATTMAEY NIAPIDLVAV
110 120 130 140 150
NLYPFEQTVA KPDCDLATAI ENIDIGGPTL LRAAAKNHAA VTVIVDPDDY
160 170 180 190 200
ERVLREMEAN GGALSSSTRF ELAVKSFEHT ARYDATIANY LGALTPNGEK
210 220 230 240 250
SAFPRSYNIQ FAKKQEMRYG ENPHQRAAFY VEQPPPAGTI ATAQQLQGKT
260 270 280 290 300
LSFNNIADTD AALACVKAFR EAPTCVIVKH ANPCGVATGI NLQEAYERAY
310 320 330 340 350
AADPVSAFGG IIAFNEPLDP TTAKTIIKRQ FAEVIIAPAV TTTAQEILTS
360 370 380 390 400
KPNIRVLACG EWSSQTAAGW DYKRIVGGLL LQDQDTDTVP LEALQTVTER
410 420 430 440 450
SPTPQELKDL LFAWQVVKFV KSNAIVYAKN GRTIGVGAGQ TSRVMSSQIA
460 470 480 490 500
ELKAKEAGFS TQNAVLASDA FFPFRDGLEA AAKAGICAVI QPGGSRRDKE
510 520
VIAAANEWDM AMLFTGMRHF RH
Length:522
Mass (Da):56,313
Last modified:November 8, 2005 - v1
Checksum:i5254E72DFC445927
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000127 Genomic DNA. Translation: ABA57556.1.
RefSeqiWP_002811435.1. NC_007484.1.

Genome annotation databases

EnsemblBacteriaiABA57556; ABA57556; Noc_1048.
KEGGinoc:Noc_1048.
PATRICi22706020. VBINitOce57959_1243.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000127 Genomic DNA. Translation: ABA57556.1.
RefSeqiWP_002811435.1. NC_007484.1.

3D structure databases

ProteinModelPortaliQ3JC90.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi323261.Noc_1048.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABA57556; ABA57556; Noc_1048.
KEGGinoc:Noc_1048.
PATRICi22706020. VBINitOce57959_1243.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230373.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
BioCyciNOCE323261:GCI3-1063-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. "Complete genome sequence of the marine, chemolithoautotrophic, ammonia-oxidizing bacterium Nitrosococcus oceani ATCC 19707."
    Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J., Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T., Vergez L.M., Ward B.B.
    Appl. Environ. Microbiol. 72:6299-6315(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 19707 / NCIMB 11848.

Entry informationi

Entry nameiPUR9_NITOC
AccessioniPrimary (citable) accession number: Q3JC90
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 8, 2005
Last modified: July 22, 2015
This is version 69 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.