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Q5FIV5 (PUR9_LACAC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:LBA1552
OrganismLactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) [Complete proteome] [HAMAP]
Taxonomic identifier272621 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length513 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 – 513513Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018896

Sequences

Sequence LengthMass (Da)Tools
Q5FIV5 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 9BED709279B278C3

FASTA51357,008
        10         20         30         40         50         60 
MKRALISVSD KTNLVDFAKG LVQNGYEIIS TGGTKKTLDE AGVKTISVEE VTNFPEILDG 

        70         80         90        100        110        120 
RVKTLNPYIH GGLLAKRDDL EHMATLEKLN IKPIDLVCVN LYPFKQTIEK PDVTTEEAIE 

       130        140        150        160        170        180 
NIDIGGPSLL RAASKNYQDV TVVTDKNDYD LVLKEIAEKG NTTLETRAKL AAKVFRATAA 

       190        200        210        220        230        240 
YDAVIANYLT KQVGLEDPEK LTLTYDLKEK MRYGENSHQK AWLYEDAIPK SFSILQAHQL 

       250        260        270        280        290        300 
HGKKLSYNNI KDADEALRCI REFQDEPTVV AMKHMNPCGI GRGDTLEEAW DRAYEADSVS 

       310        320        330        340        350        360 
IFGGVIALNR KVDLATAKKM HKIFLEIIIA PGFDDDALEV LEKKKNIRLL KLDFSKENEP 

       370        380        390        400        410        420 
TRPEIVSVMG GILQQEQDTL VENTDDWKVV TNAQPTEAQL KTMMFALKAV KHTKSNAIVV 

       430        440        450        460        470        480 
ANDERTLGVG AGQPNRIDSA KIAIKHAGDA IDDRAVLSSD AFFPFNDCVE YAAKHGIKAI 

       490        500        510 
VQPGGSIRDK DSIEIADKYG VAMVFTGYRH FRH 

« Hide

References

[1]"Complete genome sequence of the probiotic lactic acid bacterium Lactobacillus acidophilus NCFM."
Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L., McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S., Hamrick A., Cano R., Klaenhammer T.R.
Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700396 / NCK56 / N2 / NCFM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000033 Genomic DNA. Translation: AAV43369.1.
RefSeqYP_194400.1. NC_006814.3.

3D structure databases

ProteinModelPortalQ5FIV5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272621.LBA1552.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV43369; AAV43369; LBA1552.
GeneID3251379.
KEGGlac:LBA1552.
PATRIC22198122. VBILacAci7974_1474.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycLACI272621:GJO8-2509-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_LACAC
AccessionPrimary (citable) accession number: Q5FIV5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 1, 2005
Last modified: February 19, 2014
This is version 60 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