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Q71YQ3 (PUR9_LISMF) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. 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:LMOf2365_1790
OrganismListeria monocytogenes serotype 4b (strain F2365) [Complete proteome] [HAMAP]
Taxonomic identifier265669 [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_0000192102

Sequences

Sequence LengthMass (Da)Tools
Q71YQ3 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: EE5D704F1A683D8F

FASTA50954,911
        10         20         30         40         50         60 
MKRALISVSD KNGIVPFAEK LVELGVEIIS TGGTKAAFEQ AGVPVTGIEE VTEFPEMLDG 

        70         80         90        100        110        120 
RVKTLHPAIH GGLLARRDTA EHMEAIAAHD IKPIDLVVVN LYPFQETIQK SGVTLEEAIE 

       130        140        150        160        170        180 
NIDIGGPSML RSAAKNYAAV TVVVDTADYD TVLTELEEHG ATTFETRQRL AAKVFRHTAA 

       190        200        210        220        230        240 
YDALIAEYLT NITGETFPEK VTLTYNRKQV LRYGENPHQD AAFYTEPGTV ENSISSAKQL 

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

       310        320        330        340        350        360 
FGGIVALNKE VDAKTAEHMS KIFLEIIIAP SFSEEAFAIL AKKKNIRLLT VPFAGSVKGF 

       370        380        390        400        410        420 
EKTSVNGGLL IQASDSVIED TASYEVVTEK QPTEAEMKAL IAQWKIVKHV KSNAIVVGSD 

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

       490        500 
GSIKDKESIE MANKYGISMV LTHVRHFKH 

« Hide

References

[1]"Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne pathogen Listeria monocytogenes reveal new insights into the core genome components of this species."
Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M., Daugherty S.C., Dodson R.J. expand/collapse author list , Durkin A.S., Madupu R., Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O., Luchansky J.B., Fraser C.M.
Nucleic Acids Res. 32:2386-2395(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: F2365.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017262 Genomic DNA. Translation: AAT04561.1.
RefSeqYP_014384.1. NC_002973.6.

3D structure databases

ProteinModelPortalQ71YQ3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING265669.LMOf2365_1790.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT04561; AAT04561; LMOf2365_1790.
GeneID2798131.
KEGGlmf:LMOf2365_1790.
PATRIC20324869. VBILisMon105049_1797.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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_LISMF
AccessionPrimary (citable) accession number: Q71YQ3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 68 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