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Q7TUG1

- PUR9_PROMP

UniProt

Q7TUG1 - PUR9_PROMP

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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4)
Status
Reviewed - 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-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciPMAR59919:GJMQ-274-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:PMM0266
OrganismiProchlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4)
Taxonomic identifieri59919 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000001026: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 517517Bifunctional purine biosynthesis protein PurHPRO_1000018932Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi59919.PMM0266.

Structurei

3D structure databases

ProteinModelPortaliQ7TUG1.
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.
OMAiCNLKGIS.
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.

Q7TUG1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSPLALVSVS DKKNIIPFCT ELVEKFNYKI LSSGGTAKHL MEAKIPVIKV
60 70 80 90 100
ADFTNSPEIL GGRVKTLHPK IHGGILAKRT DEEHKKDIEA YDLELIELVV
110 120 130 140 150
VNLYPFKKTV EKGSKWEDAI ENIDIGGPSM IRSAAKNHKD VSVLVDPSQY
160 170 180 190 200
QEFIEESKKG ELKETYKAKL ALEAFQHTAD YDTAISNWIR KERGLQSSKY
210 220 230 240 250
IESYPLIKTL RYGENPHQKA FWYGLNNIGW NSAEQLQGKE LSYNNLLDLE
260 270 280 290 300
SALSTVLEFG YEEKDELTTE TFASVILKHN NPCGASIGNS ASQAFLNALK
310 320 330 340 350
CDSVSAFGGI VAFNSNVDSE TAINLKDIFL ECVVAPSFDP EALEILKIKK
360 370 380 390 400
NLRILKFSKD QIPNKNQTST KSIMGGLLVQ DTDNIEEKTE SWITVTKKFP
410 420 430 440 450
STQDYLDLSF AWKICKHIKS NAIVIAKDQQ TLGIGAGQMN RVGASKIALQ
460 470 480 490 500
AAKENGYGGV LASDGFFPFA DTVELANEYG INSIIQPGGS IRDEESIEMC
510
NLKGISMVFT NKRHFLH
Length:517
Mass (Da):57,418
Last modified:October 1, 2003 - v1
Checksum:i3F261B657AC56968
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX548174 Genomic DNA. Translation: CAE18725.1.
RefSeqiNP_892385.1. NC_005072.1.
WP_011131903.1. NC_005072.1.

Genome annotation databases

EnsemblBacteriaiCAE18725; CAE18725; PMM0266.
GeneIDi1727240.
KEGGipmm:PMM0266.
PATRICi23031184. VBIProMar68066_0274.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX548174 Genomic DNA. Translation: CAE18725.1 .
RefSeqi NP_892385.1. NC_005072.1.
WP_011131903.1. NC_005072.1.

3D structure databases

ProteinModelPortali Q7TUG1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 59919.PMM0266.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE18725 ; CAE18725 ; PMM0266 .
GeneIDi 1727240.
KEGGi pmm:PMM0266.
PATRICi 23031184. VBIProMar68066_0274.

Phylogenomic databases

eggNOGi COG0138.
HOGENOMi HOG000230373.
KOi K00602.
OMAi CNLKGIS.
OrthoDBi EOG6QCDFF.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .
BioCyci PMAR59919:GJMQ-274-MONOMER.

Family and domain databases

Gene3Di 3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPi MF_00139. PurH.
InterProi IPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view ]
PANTHERi PTHR11692. PTHR11692. 1 hit.
Pfami PF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view ]
PIRSFi PIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTi SM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view ]
SUPFAMi SSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsi TIGR00355. purH. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CCMP1986 / MED4.

Entry informationi

Entry nameiPUR9_PROMP
AccessioniPrimary (citable) accession number: Q7TUG1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 1, 2003
Last modified: October 29, 2014
This is version 68 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