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Q3B5R1 (PUR9_PELLD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:Plut_0432
OrganismPelodictyon luteolum (strain DSM 273) (Chlorobium luteolum (strain DSM 273)) [Complete proteome] [HAMAP]
Taxonomic identifier319225 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupPelodictyon

Protein attributes

Sequence length524 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 – 524524Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018923

Sequences

Sequence LengthMass (Da)Tools
Q3B5R1 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: B4B6EBFC53C4587B

FASTA52456,876
        10         20         30         40         50         60 
MSDPLIKRAL VSVSDKTGIV DFCRELSSLG VEIFSTGGTL KALQDSGVKA ASISLITGFP 

        70         80         90        100        110        120 
EIMDGRVKTL HPKIHGGLLA VRDNADHVAQ AVENGIGFID MVVVNLYPFE ATVARPGVSF 

       130        140        150        160        170        180 
EDAIENIDIG GPSMLRSAAK NNESVTVLTD SADYPCVLAE MRSSGGRTTR ATRLRLARQV 

       190        200        210        220        230        240 
FQLTSRYDGA IARYLTGAEG AAPAAAETMT VKLERELDMR YGENPHQSAG FYTLTDGEGT 

       250        260        270        280        290        300 
RSFGDYFEKL HGKELSYNNM LDIAAASGLV EEFRGEEPSV VIIKHTNPCG VAQAPTLVEA 

       310        320        330        340        350        360 
WHNAFATDTQ APFGGIIAFN RPLDMVTAEA VNGIFTEILI APSYEEGVLD LLMKKKDRRL 

       370        380        390        400        410        420 
LVQKQALPKG GWEFKSTPFG MLVQERDSKI VAREDLNVVT KRQPTEEELG DLMFAWKICK 

       430        440        450        460        470        480 
HIKSNTILYV KNRRTFGVGA GQMSRVDSSK IARWKASEVN LDLHGSVVAS DAFFPFADGL 

       490        500        510        520 
LAAAEAGVTA VIQPGGSIRD NEVIEAADAN NLAMVFTGMR HFKH 

« Hide

References

[1]"Complete sequence of Pelodictyon luteolum DSM 273."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 273.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000096 Genomic DNA. Translation: ABB23320.1.
RefSeqYP_374363.1. NC_007512.1.

3D structure databases

ProteinModelPortalQ3B5R1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING319225.Plut_0432.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB23320; ABB23320; Plut_0432.
GeneID3745358.
KEGGplt:Plut_0432.
PATRIC21378334. VBIChlLut1287_0452.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycPLUT319225:GHDM-444-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_PELLD
AccessionPrimary (citable) accession number: Q3B5R1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 22, 2005
Last modified: May 14, 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