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C4LA41

- PUR9_TOLAT

UniProt

C4LA41 - PUR9_TOLAT

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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Tolumonas auensis (strain DSM 9187 / TA4)
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

BioCyciTAUE595494:GHEF-564-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:Tola_0541
OrganismiTolumonas auensis (strain DSM 9187 / TA4)
Taxonomic identifieri595494 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeTolumonas
ProteomesiUP000009073: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 530530Bifunctional purine biosynthesis protein PurHPRO_1000203255Add
BLAST

Proteomic databases

PRIDEiC4LA41.

Interactioni

Protein-protein interaction databases

STRINGi595494.Tola_0541.

Structurei

3D structure databases

ProteinModelPortaliC4LA41.
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.
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.

C4LA41-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MENARPIRRA LLSVSDKTGI VEFARALQQR GVELLSTGGT ARLLADAGLA
60 70 80 90 100
VTEVSDYTGF PEMMDGRVKT LHPKVHGGIL GRRNTDDAIM TQHGIKPIDL
110 120 130 140 150
VAVNLYPFAA TVANPDCALE DAIENIDIGG PTMVRSAAKN HKDVTIVVNA
160 170 180 190 200
KDYTRVLAEM DANANSLTYT TRFDLAIAAF EHTAAYDGMI ANYFGTKVPT
210 220 230 240 250
YGVQDEASAD SKFPRTINFQ FIKKQDMRYG ENSHQAAAFY VEADVKEASV
260 270 280 290 300
STATQLQGKA LSYNNIADTD AALECVKEFA EPACVIVKHA NPCGVALGND
310 320 330 340 350
ILEAYNRAYQ TDPTSAFGGI IAFNRELDAA TAEAIVSRQF VEVIIAPVVS
360 370 380 390 400
EEAKAVVAKK ANVRLLECGQ WQGKANGFDV KRVNGGLLVQ DRDQGMVTLT
410 420 430 440 450
DLKVVTKRQP TEQELKDLLF CWKVGKFVKS NAIVYAKDSM TIGVGAGQMS
460 470 480 490 500
RVYSAKIAGI KAADEGLEVK GSVMASDAFF PFRDGIDAAA EAGITCVIQP
510 520 530
GGSMRDQEVI DAADEHGMAM VFTNMRHFRH
Length:530
Mass (Da):57,280
Last modified:July 7, 2009 - v1
Checksum:i666614F6C764A14B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001616 Genomic DNA. Translation: ACQ92170.1.
RefSeqiYP_002891756.1. NC_012691.1.

Genome annotation databases

EnsemblBacteriaiACQ92170; ACQ92170; Tola_0541.
GeneIDi7883356.
KEGGitau:Tola_0541.
PATRICi23977685. VBITolAue42623_0545.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001616 Genomic DNA. Translation: ACQ92170.1 .
RefSeqi YP_002891756.1. NC_012691.1.

3D structure databases

ProteinModelPortali C4LA41.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 595494.Tola_0541.

Proteomic databases

PRIDEi C4LA41.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACQ92170 ; ACQ92170 ; Tola_0541 .
GeneIDi 7883356.
KEGGi tau:Tola_0541.
PATRICi 23977685. VBITolAue42623_0545.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .
BioCyci TAUE595494:GHEF-564-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: DSM 9187 / TA4.

Entry informationi

Entry nameiPUR9_TOLAT
AccessioniPrimary (citable) accession number: C4LA41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 7, 2009
Last modified: October 1, 2014
This is version 41 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