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B0KBQ1 (PUR9_THEP3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:Teth39_1709
OrganismThermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium thermohydrosulfuricum) [Complete proteome] [HAMAP]
Taxonomic identifier340099 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeThermoanaerobacter

Protein attributes

Sequence length508 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 – 508508Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000096103

Sequences

Sequence LengthMass (Da)Tools
B0KBQ1 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: 068AEAD615646E5B

FASTA50856,589
        10         20         30         40         50         60 
MAKKALISVS KKEGIVEFAK KLNELGYEII STGGTYNLLK ENRVNVVKVS DITGFPEIMD 

        70         80         90        100        110        120 
GRVKTLHPKI HGGLLAIRDN EEHIKALKEH GIEPIDIVVI NLYPFKETIL KENVTLEEAI 

       130        140        150        160        170        180 
ENIDIGGPSM IRAAAKNYKY VTILVDPKDY DTVIEEIKQY GNTKEETRFY LAAKAFGHTA 

       190        200        210        220        230        240 
LYDSLIYNYL IQKNNIEFPE VMAFAYEKAQ DMRYGENPHQ KAAFYKNPIK AYGIAECEQL 

       250        260        270        280        290        300 
HGKELSFNNI NDANAAIELL REFKEPAAVA VKHTNPCGVA IADNIYNAYL KAYESDPVSI 

       310        320        330        340        350        360 
FGGIVALNRT VDVKTAEELI KIFLEIVIAP DFEEEAFEIL KKKKNLRILR LKEGYEKEYD 

       370        380        390        400        410        420 
LKKVEGGLLV QEKDEIDLDE NNLKVVTKKA PTQKEMEDLR FAWKVVKHVK SNAIVLAKDG 

       430        440        450        460        470        480 
ATVGIGVGQV NRIWPTEQAI KQAGSKAKGS VLASDAFFPF PDVVEVASKA GITAIIQPGG 

       490        500 
SQNDALSIEA ADKGGVSMIF TGIRHFKH 

« Hide

References

[1]"Complete sequence of Thermoanaerobacter pseudethanolicus 39E."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33223 / 39E.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000924 Genomic DNA. Translation: ABY95346.1.
RefSeqYP_001665682.1. NC_010321.1.

3D structure databases

ProteinModelPortalB0KBQ1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING340099.Teth39_1709.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY95346; ABY95346; Teth39_1709.
GeneID5874597.
KEGGtpd:Teth39_1709.
PATRIC23888195. VBIThePse6203_1790.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycTPSE340099:GH4W-1759-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_THEP3
AccessionPrimary (citable) accession number: B0KBQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 18, 2008
Last modified: February 19, 2014
This is version 45 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