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Q7TUM7

- PUR9_PROMM

UniProt

Q7TUM7 - PUR9_PROMM

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Protein
Bifunctional purine biosynthesis protein PurH
Gene
purH, PMT_1857
Organism
Prochlorococcus marinus (strain MIT 9313)
Status
Reviewed - Annotation score: 3 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

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein PurH
Including the following 2 domains:
Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC:2.1.2.3)
Alternative name(s):
AICAR transformylase
IMP cyclohydrolase (EC:3.5.4.10)
Alternative name(s):
ATIC
IMP synthase
Inosinicase
Gene namesi
Name:purH
Ordered Locus Names:PMT_1857
OrganismiProchlorococcus marinus (strain MIT 9313)
Taxonomic identifieri74547 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000001423: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 517517Bifunctional purine biosynthesis protein PurHUniRule annotation
PRO_1000018931Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi74547.PMT1857.

Structurei

3D structure databases

ProteinModelPortaliQ7TUM7.

Family & Domainsi

Domaini

The IMP cyclohydrolase activity resides in the N-terminal region By similarity.UniRule annotation

Sequence similaritiesi

Belongs to the PurH family.

Phylogenomic databases

eggNOGiCOG0138.
KOiK00602.
OMAiRAFKTDP.
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.

Q7TUM7-1 [UniParc]FASTAAdd to Basket

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MAPIALLSVS NKHGIVPLAE SLHRMHGFQL LSSGGTAKVL EDAGLPVTRV    50
AEHTGAAEIL GGRVKTLHPR VHGGILAMRG DPDHEVDLEQ HQIPPIDVVV 100
VNLYPFRETV ANPQVSWETA IENIDIGGPA MVRAAAKNHA HVAVLTRPDQ 150
YDRFLVALSD GVDDQLRREL ALEAFEHTAA YDVAISHWMG ERLTEQASQW 200
LEAIPLRQRL RYGENPHQHA AWYSAPQQGW GGAIQLQGKE LSTNNLLDLE 250
AALATVREFG YGTEGAQQAV QDAAVVVKHT NPCGVAIGTG VASALSRALD 300
ADRVSAFGGI VALNGLVDAT TARELTSLFL ECVVAPGFEP EAREILATKA 350
NLRLLELAPG AIDAAGRDHI RTILGGVLVQ DQDDQSIDPT SWTVASKRSP 400
NAEENADLTF AWRLVRHVRS NAIVVARAGQ SLGVGAGQMN RVGSARLALE 450
AAGDQARGAV LASDGFFPFD DTVRLAANHG ICAVIQPGGS KRDADSIAVC 500
DDFGLAMVLT GKRHFLH 517
Length:517
Mass (Da):55,196
Last modified:October 1, 2003 - v1
Checksum:i2CC55FB1AA76B3B7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX548175 Genomic DNA. Translation: CAE22032.1.
RefSeqiNP_895684.1. NC_005071.1.
WP_011131224.1. NC_005071.1.

Genome annotation databases

EnsemblBacteriaiCAE22032; CAE22032; PMT_1857.
GeneIDi1728817.
KEGGipmt:PMT1857.
PATRICi23012509. VBIProMar135351_2381.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX548175 Genomic DNA. Translation: CAE22032.1 .
RefSeqi NP_895684.1. NC_005071.1.
WP_011131224.1. NC_005071.1.

3D structure databases

ProteinModelPortali Q7TUM7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 74547.PMT1857.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE22032 ; CAE22032 ; PMT_1857 .
GeneIDi 1728817.
KEGGi pmt:PMT1857.
PATRICi 23012509. VBIProMar135351_2381.

Phylogenomic databases

eggNOGi COG0138.
KOi K00602.
OMAi RAFKTDP.
OrthoDBi EOG6QCDFF.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .

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: MIT 9313.

Entry informationi

Entry nameiPUR9_PROMM
AccessioniPrimary (citable) accession number: Q7TUM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 1, 2003
Last modified: September 3, 2014
This is version 67 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

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