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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Prochlorococcus marinus (strain MIT 9515)
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

BioCyciPMAR167542:GI3N-305-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:P9515_02991
OrganismiProchlorococcus marinus (strain MIT 9515)
Taxonomic identifieri167542 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000001589 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 517517Bifunctional purine biosynthesis protein PurHPRO_1000018928Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi167542.P9515_02991.

Structurei

3D structure databases

ProteinModelPortaliA2BUP7.
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.

A2BUP7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPLALVSVS DKTNIIPFCK DLVEKFGYNI LSSGGTAEYL TEAKVPVLKV
60 70 80 90 100
ADFTESPEIL DGRVKTLHPK IHGGILAKRS NEEHQREILE NKLELIDLVV
110 120 130 140 150
VNLYPFKKKV EEQCPWEEAI ENIDIGGPSM IRSAAKNHAD VAVLVDPNQY
160 170 180 190 200
QNYIEEIKKG PLSKDFKTKL AFEAFQHTAS YDSAISNWIS KEKDLRPSNF
210 220 230 240 250
IESYPLIKQL RYGENPHQKA LWYGLNNIGW NSAEQLQGKE LSYNNILDLE
260 270 280 290 300
SALLTVLEFG YETKPNIKTE SIAAVILKHN NPCGASISNS ASSSFKNALK
310 320 330 340 350
CDSVSAFGGI VAFNANVDKE TALILKDIFL ECVVAPSFDK EALEIFKTKK
360 370 380 390 400
NLRVLKLTKE MLPKENQTCS KSIMGGILIQ DSDNQENSED SWISVTKKNP
410 420 430 440 450
TEQEYLDLKF AWKICKHVKS NAIVVAKDQQ TLGIGAGQMN RVGASKIALE
460 470 480 490 500
AAKEIDSGGV LASDGFFPFA DTVRLADKYG ISSIIQPGGS IRDEESIKMC
510
DSRGISMIFT HKRHFLH
Length:517
Mass (Da):57,437
Last modified:February 19, 2007 - v1
Checksum:iAE9C2D43313409ED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000552 Genomic DNA. Translation: ABM71508.1.
RefSeqiYP_001010615.1. NC_008817.1.

Genome annotation databases

EnsemblBacteriaiABM71508; ABM71508; P9515_02991.
KEGGipmc:P9515_02991.
PATRICi23014124. VBIProMar113831_0303.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000552 Genomic DNA. Translation: ABM71508.1.
RefSeqiYP_001010615.1. NC_008817.1.

3D structure databases

ProteinModelPortaliA2BUP7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi167542.P9515_02991.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM71508; ABM71508; P9515_02991.
KEGGipmc:P9515_02991.
PATRICi23014124. VBIProMar113831_0303.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230373.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
BioCyciPMAR167542:GI3N-305-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 9515.

Entry informationi

Entry nameiPUR9_PROM5
AccessioniPrimary (citable) accession number: A2BUP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 14, 2008
Last sequence update: February 19, 2007
Last modified: March 31, 2015
This is version 58 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.