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A0AJL9 (PUR9_LISW6) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:lwe1783
OrganismListeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / SLCC5334) [Complete proteome] [HAMAP]
Taxonomic identifier386043 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length509 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 – 509509Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018907

Sequences

Sequence LengthMass (Da)Tools
A0AJL9 [UniParc].

Last modified November 28, 2006. Version 1.
Checksum: 78829DB4085563B6

FASTA50954,908
        10         20         30         40         50         60 
MKRALISVSD KNGIVPFAEK LVELGVEIIS TGGTKATFEQ AGIPVTGIED VTKFPEMLDG 

        70         80         90        100        110        120 
RVKTLHPAIH GGLLARRDTA EHMEAIAAHD IEPIDLVVVN LYPFQETIQK PGVTLEEAIE 

       130        140        150        160        170        180 
NIDIGGPSML RSAAKNYAAV TVVVDAADYD TVLTELKEHG ATTFETRQRL AAKVFRHTAA 

       190        200        210        220        230        240 
YDAVIAEYLT KITGETFPEK VTFTYNRKQA LRYGENPHQD AAFYTEPVAL LNSISAAKQL 

       250        260        270        280        290        300 
HGKELSYNNI RDADAALKIA NEFTEPVAVA VKHMNPCGVG VGENIEEAYL KAYEADETSI 

       310        320        330        340        350        360 
FGGIVALNKE VDAKTAEHMS KIFLEIIIAP SFSEEAFTIL AKKKNIRLLT VPFAGSVESL 

       370        380        390        400        410        420 
EKTSVNGGLL IQASDSFVED SAGYEVVTEK QPTEAEMKAL LAQWKIVKHV KSNAIVVGSD 

       430        440        450        460        470        480 
KQTLGIGAGQ MNRIGSALIA LEQAGEKAKG AVLASDAFFP MDDTVEAAAK AGITAIIQPG 

       490        500 
GSIKDKESIA MADKYGISMV LTHVRHFKH 

« Hide

References

[1]"Whole-genome sequence of Listeria welshimeri reveals common steps in genome reduction with Listeria innocua as compared to Listeria monocytogenes."
Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S., Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O., Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T. expand/collapse author list , Lampidis R., Kreft J., Goebel W., Chakraborty T.
J. Bacteriol. 188:7405-7415(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35897 / DSM 20650 / SLCC5334.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM263198 Genomic DNA. Translation: CAK21201.1.
RefSeqYP_849980.1. NC_008555.1.

3D structure databases

ProteinModelPortalA0AJL9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING386043.lwe1783.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAK21201; CAK21201; lwe1783.
GeneID4465468.
KEGGlwe:lwe1783.
PATRIC20330765. VBILisWel39304_1792.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycLWEL386043:GI5X-1830-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_LISW6
AccessionPrimary (citable) accession number: A0AJL9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 28, 2006
Last modified: February 19, 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