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A1BE85 (PUR9_CHLPD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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:Cpha266_0657
OrganismChlorobium phaeobacteroides (strain DSM 266) [Complete proteome] [HAMAP]
Taxonomic identifier290317 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupChlorobium

Protein attributes

Sequence length521 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 – 521521Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018872

Sequences

Sequence LengthMass (Da)Tools
A1BE85 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 9CAAAFA3D2B081E9

FASTA52157,053
        10         20         30         40         50         60 
MSDPVIKRAL VSVSDKTGIV DFCRELSLLG VEVFSTGGTL KTLQDAGIAA ASISTITGFP 

        70         80         90        100        110        120 
EIMDGRVKTL HPKIHGGLLA VRENPDHVNQ ANENGISFID LVVVNLYPFE ATVAKPDVTF 

       130        140        150        160        170        180 
EDAIENIDIG GPSMLRSAAK NNESVTVVTD SADYALVLQE MRNNNGATKR ETRLALALKV 

       190        200        210        220        230        240 
FELTSRYDRA IASYLAGAQH EADSSMTVKL ERELDMRYGE NPHQSAGLYR LTDENGTRSF 

       250        260        270        280        290        300 
SDYFEKLHGK ELSYNNMLDI AAAVSLIEEF RGEEPTVVII KHTNPCGVAQ APTLAEAYRR 

       310        320        330        340        350        360 
AFSTDTQAPF GGIIAFNHPL DMEAATAVNE IFTEILIAPA FEDGVLEMLM KKKDRRLVRQ 

       370        380        390        400        410        420 
TSALPKGGWE FKSTPFGMLV QERDSKIVTK EDLTVVTKRQ PTEEEVADMM FAWKICKHIK 

       430        440        450        460        470        480 
SNTILYVKNR QTFGVGAGQM SRVDSSKIAR WKASEVNLDL HGSVVASDAF FPFADGLLAA 

       490        500        510        520 
AEAGVTAVIQ PGGSIRDNEV IEAADANNLA MVFTGMRHFK H 

« Hide

References

[1]"Complete sequence of Chlorobium phaeobacteroides DSM 266."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E., Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J., Bryant D.A., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 266.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000492 Genomic DNA. Translation: ABL64712.1.
RefSeqYP_911136.1. NC_008639.1.

3D structure databases

ProteinModelPortalA1BE85.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290317.Cpha266_0657.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL64712; ABL64712; Cpha266_0657.
GeneID4569811.
KEGGcph:Cpha266_0657.
PATRIC21389133. VBIChlPha122104_0751.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMAIRASSKN.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycCPHA290317:GHX4-669-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_CHLPD
AccessionPrimary (citable) accession number: A1BE85
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 54 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