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Q1H4G7 (PUR9_METFK) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional purine biosynthesis protein PurH

Including the following 2 domains:

  1. Phosphoribosylaminoimidazolecarboxamide formyltransferase
    EC=2.1.2.3
    Alternative name(s):
    AICAR transformylase
  2. IMP cyclohydrolase
    EC=3.5.4.10
    Alternative name(s):
    ATIC
    IMP synthase
    Inosinicase
Gene names
Name:purH
Ordered Locus Names:Mfla_0349
OrganismMethylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875) [Complete proteome] [HAMAP]
Taxonomic identifier265072 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaMethylophilalesMethylophilaceaeMethylobacillus

Protein attributes

Sequence length528 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 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): step 1/1. HAMAP-Rule MF_00139

Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.

Domain

The IMP cyclohydrolase activity resides in the N-terminal region By similarity. HAMAP-Rule MF_00139

Sequence similarities

Belongs to the PurH family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 528528Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000076484

Sequences

Sequence LengthMass (Da)Tools
Q1H4G7 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: 5ED93D58E0752A67

FASTA52856,430
        10         20         30         40         50         60 
MAVIKRALIS VSDKTGILEF AKALAEFGVE ILSTGGTAKL FRDNGIPVTE VSDYTGFPEM 

        70         80         90        100        110        120 
LDGRVKTLHP KIHGGLLGRR DLPEHVTAMQ AAGIPDIDMI VVNLYPFEAT VARPDATLED 

       130        140        150        160        170        180 
AIENIDIGGP AMVRSAAKNW QDVAVLTDAS QYEEVLAEMR STGGATSKAT RFALSVAAFN 

       190        200        210        220        230        240 
RISNYDGAIS DYLSSFNADG TRNEFPGQIN GRLVKVQDLR YGENPHQQAA FYRDLYPAPG 

       250        260        270        280        290        300 
SLVTAQQLQG KELSYNNIAD ADAAWECVKS FDSTACVIVK HANPCGVALG ATPLEAYQKA 

       310        320        330        340        350        360 
FQTDPTSAFG GIIAFNHTLD GAAAEAVSKQ FVEVLIAPDY TEEALAVFKA KANVRVLKIA 

       370        380        390        400        410        420 
LPVGGDSPWS RGRNSHDTKR VGSGVLIQTA DNHEISAADI KVVTKKQPTP EQLEDLLFAW 

       430        440        450        460        470        480 
RVAKYVKSNA IVFCGNGMTL GVGAGQMSRV DSTRIAAIKA QNAGLSLQGS AVASDAFFPF 

       490        500        510        520 
RDGVDVLAEA GASCVIQPGG SIRDDEVIAA ADEHGLVMIF TNIRHFRH 

« Hide

References

[1]"Complete sequence of Methylobacillus flagellatus KT."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KT / ATCC 51484 / DSM 6875.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000284 Genomic DNA. Translation: ABE48620.1.
RefSeqYP_544461.1. NC_007947.1.

3D structure databases

ProteinModelPortalQ1H4G7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING265072.Mfla_0349.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE48620; ABE48620; Mfla_0349.
GeneID3999316.
KEGGmfa:Mfla_0349.
PATRIC32266223. VBIMetFla97085_0354.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycMFLA265072:GHWJ-366-MONOMER.
UniPathwayUPA00074; UER00133.
UPA00074; UER00135.

Family and domain databases

Gene3D3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPMF_00139. PurH.
InterProIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERPTHR11692. PTHR11692. 1 hit.
PfamPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR9_METFK
AccessionPrimary (citable) accession number: Q1H4G7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 27, 2006
Last modified: February 19, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways