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
Prochlorococcus marinus (strain MIT 9211)
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

BioCyciPMAR93059:GHJV-298-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:P9211_02931
OrganismiProchlorococcus marinus (strain MIT 9211)
Taxonomic identifieri93059 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000000788 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 518518Bifunctional purine biosynthesis protein PurHPRO_1000096082Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi93059.P9211_02931.

Structurei

3D structure databases

ProteinModelPortaliA9BDN8.
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.

A9BDN8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARIALISVS NKDGLIPFAK TLTTLHGFEI ISSGGTARAL KEANIPVKTV
60 70 80 90 100
SDYTGAPEIL GGRVKTLHPR IHGGILAKQG NSSHQFDLEK ENIKNIDLVV
110 120 130 140 150
VNLYPFQETI SDPDVTWDNA IENIDIGGPA MIRAAAKNHE SVSILTNPNQ
160 170 180 190 200
YDAFLEKLEA GEISTTIKAK LALEAFEHTA SYDIAISQWL SKQIESKYSP
210 220 230 240 250
YLTSQPIKQT LRYGENPHQN ANWYSAVNQG WGQAEQLQGK ELSTNNLLDL
260 270 280 290 300
EAAVATIREF GYDLGNKGNS CEKAAVIIKH TNPCGVAVSN NLSNAFNLAL
310 320 330 340 350
ECDSISAFGG IVALNCNLDA ATAKELSSLF LECVVAPDYD ANALEILSTK
360 370 380 390 400
KNLRIIKLSH SSIKSSERKY IRSILGGILV QEVDDKLIEP NEWKVPTKLQ
410 420 430 440 450
MSIEDKADLA FAWRVVRHVR SNAIVVASAG QTLGIGAGQM NRIGAAKIAL
460 470 480 490 500
EAAGEKAQGA VLASDGFFPF DDTVHLASRY GIKSIIQPGG SIRDQSSIDA
510
CNQLGLSMIF TGKRHFLH
Length:518
Mass (Da):56,123
Last modified:January 15, 2008 - v1
Checksum:iB8AFE8AE84470FF9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000878 Genomic DNA. Translation: ABX08224.1.
RefSeqiYP_001550178.1. NC_009976.1.

Genome annotation databases

EnsemblBacteriaiABX08224; ABX08224; P9211_02931.
KEGGipmj:P9211_02931.
PATRICi22986032. VBIProMar136502_0311.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000878 Genomic DNA. Translation: ABX08224.1.
RefSeqiYP_001550178.1. NC_009976.1.

3D structure databases

ProteinModelPortaliA9BDN8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93059.P9211_02931.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABX08224; ABX08224; P9211_02931.
KEGGipmj:P9211_02931.
PATRICi22986032. VBIProMar136502_0311.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230373.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
BioCyciPMAR93059:GHJV-298-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MIT 9211.

Entry informationi

Entry nameiPUR9_PROM4
AccessioniPrimary (citable) accession number: A9BDN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 15, 2008
Last modified: April 1, 2015
This is version 52 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.