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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.
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

Pathwayi: IMP 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).
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.

Pathwayi: IMP 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.
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

Keywordsi

Molecular functionHydrolase, Transferase
Biological processPurine 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:P9211_02931
OrganismiProchlorococcus marinus (strain MIT 9211)
Taxonomic identifieri93059 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesProchloraceaeProchlorococcus
Proteomesi
  • UP000000788 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000960821 – 518Bifunctional purine biosynthesis protein PurHAdd BLAST518

Interactioni

Protein-protein interaction databases

STRINGi93059.P9211_02931.

Structurei

3D structure databases

ProteinModelPortaliA9BDN8.
SMRiA9BDN8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The IMP cyclohydrolase activity resides in the N-terminal region.

Sequence similaritiesi

Belongs to the PurH family.

Phylogenomic databases

eggNOGiENOG4105DC1. Bacteria.
COG0138. LUCA.
HOGENOMiHOG000230373.
KOiK00602.
OMAiDLLFAWK.
OrthoDBiPOG091H00UT.

Family and domain databases

Gene3Di3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPiMF_00139. PurH. 1 hit.
InterProiView protein in InterPro
IPR024051. AICAR_Tfase_dup_dom_sf.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
IPR036914. MGS-like_dom_sf.
PANTHERiPTHR11692. PTHR11692. 1 hit.
PfamiView protein in Pfam
PF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
PIRSFiPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTiView protein in SMART
SM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
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.
RefSeqiWP_012194849.1. NC_009976.1.

Genome annotation databases

EnsemblBacteriaiABX08224; ABX08224; P9211_02931.
KEGGipmj:P9211_02931.

Similar proteinsi

Entry informationi

Entry nameiPUR9_PROM4
AccessioniPrimary (citable) accession number: A9BDN8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 15, 2008
Last modified: November 22, 2017
This is version 62 of the entry and version 1 of the sequence. See 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