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Reviewed, UniProtKB/Swiss-Prot Q8A155 (PUR9_BACTN)

Last modified June 16, 2009. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Bifunctional purine biosynthesis protein purH
Including the following 2 domains:
    1- Recommended name:
            Phosphoribosylaminoimidazolecarboxamide formyltransferase
              EC=2.1.2.3
        Alternative name(s):
            AICAR transformylase
    2- Recommended name:
            IMP cyclohydrolase
              EC=3.5.4.10
        Alternative name(s):
            Inosinicase
            IMP synthetase
            ATIC
Gene names
Name: purH
Ordered Locus Names: BT_3812
OrganismBacteroides thetaiotaomicron [Complete proteome] [HAMAP]
Taxonomic identifier818 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length507 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 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.

Sequence similarities

Belongs to the purH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 507507Bifunctional purine biosynthesis protein purH HAMAP MF_00139
PRO_0000192071

Sequences

Sequence LengthMass (Da)Tools
Q8A155-1 [UniParc].

Last modified June 20, 2003. Version 1.
Checksum: 0C09966527E570E4

FASTA50755,880
        10         20         30         40         50         60 
MSESKRIKTA LVSVYHKEGL DEIITKLYEE GVEFLSTGGT RQFIESLGYP CKAVEDLTTY 

        70         80         90        100        110        120 
PSILGGRVKT LHPKIFGGIL CRRDLEQDIQ QIEKYEIPEI DLVIVDLYPF EATVASGASE 

       130        140        150        160        170        180 
ADIIEKIDIG GISLIRAAAK NYNDVIIVAS QAQYKPLLDM LMEHGATSSL EERRWMAKEA 

       190        200        210        220        230        240 
FAVSSHYDSA IFNYFDAGEG SAFRCSVNNQ KQLRYGENPH QKGYFYGNLD AMFDQIHGKE 

       250        260        270        280        290        300 
ISYNNLLDIN AAVDLIDEYE DLTFAILKHN NACGLASRPT VLEAWTDALA GDPVSAFGGV 

       310        320        330        340        350        360 
LITNGVIDKA AAEEINKIFF EVIIAPDYDV DALEILGQKK NRIILVRKEA KLPKKQFRAL 

       370        380        390        400        410        420 
LNGVLVQDKD MNIETVADLR TVTDKAPTPE EVEDLLFANK IVKNSKSNAI VLAKGKQLLA 

       430        440        450        460        470        480 
SGVGQTSRVD ALKQAIEKAK SFGFDLNGAV MASDAFFPFP DCVEIADKEG ITAVIQPGGS 

       490        500 
VKDDLTFAYC NEHGMAMVTT GIRHFKH 

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References

[1]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed: 12663928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

AE015928 Genomic DNA. Translation: AAO78917.1.
RefSeqNP_812723.1.

3D structure databases

HSSPHSSP built from PDB template 1G8M based on UniProtKB P31335.
ModBaseSearch...

Genome annotation databases

GeneID1072684.
GenomeReviewsGene locus BT_3812 in contig AE015928_GR.
KEGGbth:BT_3812.
NMPDRfig|226186.1.peg.3810.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8A155.
OMAQ8A155. VILAHEY.

Enzyme and pathway databases

BioCycBTHE226186:BT_3812-MON.
BRENDA2.1.2.3. 21018.
3.5.4.10. 21018.

Family and domain databases

HAMAPMF_00139.
[Tree]
InterProIPR002695. AICARFT_IMPCHas.
IPR013982. AICARFT_IMPCHas_formly.
IPR011607. MGS.
[Graphical view]
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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePUR9_BACTN
AccessionPrimary (citable) accession number: Q8A155
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 20, 2003
Last modified: June 16, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents