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Q9RHX6

- PUR9_CORAM

UniProt

Q9RHX6 - PUR9_CORAM

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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Corynebacterium ammoniagenes (Brevibacterium ammoniagenes)
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

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
OrganismiCorynebacterium ammoniagenes (Brevibacterium ammoniagenes)
Taxonomic identifieri1697 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 516516Bifunctional purine biosynthesis protein PurHPRO_0000192087Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ9RHX6.
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

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.

Q9RHX6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSDDRKQIKR ALISVYDKTG LEELARTLDS AGVEIVSTGS TAAKIADLGI
60 70 80 90 100
NVTPVESLTG FPECLEGRVK TLHPRVHAGI LADTRKPDHL NQLEELEIEP
110 120 130 140 150
FQLVVVNLYP FKETVASGAD FDGCVEQIDI GGPSMVRAAA KNHPSVAVVV
160 170 180 190 200
DPARYGDIAE AVAQGGFDLA QRRQLAATAF KHTADYDVAV SGWFAQQLAD
210 220 230 240 250
DSVASAELEG DALRYGENPH QQASIVREGT TGVANAKQLH GKEMSYNNYQ
260 270 280 290 300
DADAAWRAAW DHERPCVAII KHANPCGIAV SDESIAAAHA AAHACDPMSA
310 320 330 340 350
FGGVIAVNRE VTKEMATQVA DIFTEVIIAP SYEDGAVEIL QGKKNIRILV
360 370 380 390 400
AEHEVPAVEV KEISGGRLLQ EADVYQAEGD KASSWTLAAG EAASEEKLAE
410 420 430 440 450
LEFAWRAVRS VKSNAILLAH EGATVGVGMG QVNRVDSAKL AVDRANTLAD
460 470 480 490 500
SAERARGSVA ASDAFFPFAD GLQVLIDAGV SAVVQPGGSI RDEEVIAAAE
510
AAGITMYFTG TRHFAH
Length:516
Mass (Da):54,757
Last modified:May 1, 2000 - v1
Checksum:i14EF915D6DB72B93
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB003159 Genomic DNA. Translation: BAA89444.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB003159 Genomic DNA. Translation: BAA89444.1 .

3D structure databases

ProteinModelPortali Q9RHX6.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. "Corynebacterium ammoniagenes purNH region."
    Yonetani Y., Teshiba S.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 6872 / DSM 20305 / KCTC 1019 / NCTC 2399.

Entry informationi

Entry nameiPUR9_CORAM
AccessioniPrimary (citable) accession number: Q9RHX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: May 1, 2000
Last modified: October 1, 2014
This is version 61 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

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