Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9X0X6 (PUR9_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:TM_1249
OrganismThermotoga maritima
Taxonomic identifier2336 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 MF_00139

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

Sequence similarities

Belongs to the PurH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 452452Bifunctional purine biosynthesis protein PurH HAMAP MF_00139
PRO_0000192142

Secondary structure

.................................................................................. 452
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9X0X6 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: E4537EF51A5C4469

FASTA45249,867
        10         20         30         40         50         60 
MKRILVSLYE KEKYLDILRE LHEKGWEIWA SSGTAKFLKS NGIEANDVST ITGFENLLGG 

        70         80         90        100        110        120 
LVKTLHPEIF AGILGPEPRW DVVFVDLYPP PDIDIGGVAL LRAAAKNWKK VKPAFDMETL 

       130        140        150        160        170        180 
KLAIEIDDEE TRKYLAGMTF AFTSVYDSIR ANQFVEGISL AFKREDLQLR YGENPHEKAF 

       190        200        210        220        230        240 
VYGKPAFEIL HEGKTISFNN ILDAENAWFM AKNLPRMGAV VVKHQSPCGA AIGEDKVEIV 

       250        260        270        280        290        300 
KKAIEADDES SFGGILAVNF EMDEEVAKSL KKYLEVIVAP SFTQEAIEVL SKKKVRLLKP 

       310        320        330        340        350        360 
GDYASWAGKM AFGSLVLSER KYPEGNFELV VGEPLSEKEL EDLEFAYRVV EGAKSNAVLI 

       370        380        390        400        410        420 
AKDGVTVGIG SGQPSRKRAA WIATVMAGEK AKGAVAASDA FFPFPDSLEI LAQAGVKAVV 

       430        440        450 
APLGSIRDEE VIEKARELGI TFYKAPSRVF RH 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000512 Genomic DNA. Translation: AAD36324.1.
PIRC72277.
RefSeqNP_229054.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZCZX-ray1.88A/B1-452[»]
ProteinModelPortalQ9X0X6.
SMRQ9X0X6. Positions 1-452.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID898234.
GenomeReviewsGene locus TM_1249 in contig AE000512_GR.
KEGGtma:TM1249.
NMPDRfig|243274.1.peg.1238.
PATRIC23937438. VBITheMar51294_1265.
TIGRTM_1249.

Phylogenomic databases

HOGENOMHBG498048.
OMAFTGTRHF.
PhylomeDBQ9X0X6.
ProtClustDBCLSK795778.

Enzyme and pathway databases

BioCycTMAR243274:TM_1249-MONOMER.

Family and domain databases

HAMAPMF_00139. PurH. Divergent sequence.
[Tree]
InterProIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
Gene3DG3DSA:3.40.140.20. G3DSA:3.40.140.20. 2 hits.
G3DSA:3.40.50.1380. MGS-like_dom. 1 hit.
KOK00602.
PANTHERPTHR11692. AICARFT_IMPCHas. 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]
SUPFAMSSF53927. Cytidine_deaminase-like. 1 hit.
SSF52335. MGS-like_dom. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR9_THEMA
AccessionPrimary (citable) accession number: Q9X0X6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: January 25, 2012
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families