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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875)
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.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-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciMFLA265072:GHWJ-366-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:Mfla_0349
OrganismiMethylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875)
Taxonomic identifieri265072 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaMethylophilalesMethylophilaceaeMethylobacillus
ProteomesiUP000002440 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 528528Bifunctional purine biosynthesis protein PurHPRO_1000076484Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi265072.Mfla_0349.

Structurei

3D structure databases

ProteinModelPortaliQ1H4G7.
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.
HOGENOMiHOG000230372.
KOiK00602.
OMAiPCGVAEG.
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.

Q1H4G7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVIKRALIS VSDKTGILEF AKALAEFGVE ILSTGGTAKL FRDNGIPVTE
60 70 80 90 100
VSDYTGFPEM LDGRVKTLHP KIHGGLLGRR DLPEHVTAMQ AAGIPDIDMI
110 120 130 140 150
VVNLYPFEAT VARPDATLED AIENIDIGGP AMVRSAAKNW QDVAVLTDAS
160 170 180 190 200
QYEEVLAEMR STGGATSKAT RFALSVAAFN RISNYDGAIS DYLSSFNADG
210 220 230 240 250
TRNEFPGQIN GRLVKVQDLR YGENPHQQAA FYRDLYPAPG SLVTAQQLQG
260 270 280 290 300
KELSYNNIAD ADAAWECVKS FDSTACVIVK HANPCGVALG ATPLEAYQKA
310 320 330 340 350
FQTDPTSAFG GIIAFNHTLD GAAAEAVSKQ FVEVLIAPDY TEEALAVFKA
360 370 380 390 400
KANVRVLKIA LPVGGDSPWS RGRNSHDTKR VGSGVLIQTA DNHEISAADI
410 420 430 440 450
KVVTKKQPTP EQLEDLLFAW RVAKYVKSNA IVFCGNGMTL GVGAGQMSRV
460 470 480 490 500
DSTRIAAIKA QNAGLSLQGS AVASDAFFPF RDGVDVLAEA GASCVIQPGG
510 520
SIRDDEVIAA ADEHGLVMIF TNIRHFRH
Length:528
Mass (Da):56,430
Last modified:June 27, 2006 - v1
Checksum:i5ED93D58E0752A67
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000284 Genomic DNA. Translation: ABE48620.1.
RefSeqiYP_544461.1. NC_007947.1.

Genome annotation databases

EnsemblBacteriaiABE48620; ABE48620; Mfla_0349.
GeneIDi3999316.
KEGGimfa:Mfla_0349.
PATRICi32266223. VBIMetFla97085_0354.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000284 Genomic DNA. Translation: ABE48620.1.
RefSeqiYP_544461.1. NC_007947.1.

3D structure databases

ProteinModelPortaliQ1H4G7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi265072.Mfla_0349.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE48620; ABE48620; Mfla_0349.
GeneIDi3999316.
KEGGimfa:Mfla_0349.
PATRICi32266223. VBIMetFla97085_0354.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230372.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
BioCyciMFLA265072:GHWJ-366-MONOMER.

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.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: KT / ATCC 51484 / DSM 6875.

Entry informationi

Entry nameiPUR9_METFK
AccessioniPrimary (citable) accession number: Q1H4G7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 27, 2006
Last modified: April 29, 2015
This is version 64 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.