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Q1B3W0 (PUR9_MYCSS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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:Mmcs_4319
OrganismMycobacterium sp. (strain MCS) [Complete proteome] [HAMAP]
Taxonomic identifier164756 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length527 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 – 527527Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018913

Sequences

Sequence LengthMass (Da)Tools
Q1B3W0 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: 47F4078911419553

FASTA52755,533
        10         20         30         40         50         60 
MSGDQGQAGA KRPIRRALIS VYDKTGLIDL ARGLHEAGVD IVSTGSTAKT IADKGIPVTP 

        70         80         90        100        110        120 
VEFVTGFPEV LDGRVKTLHP HIHAGLLADT RKPEHVEALA KLGIAPFDLV VVNLYPFSET 

       130        140        150        160        170        180 
VESGASVDEC VEQIDIGGPS MVRAAAKNHP SVAVVVEPNG YDGVLAAVRT GGFTLAERKI 

       190        200        210        220        230        240 
LASLAFRHTA EYDVAVASWM GSTLAPEEPA QKLPAWVGGT WRRAAVLRYG ENPHQQAALY 

       250        260        270        280        290        300 
RDATAWPGLA QAEQLHGKEM SYNNYTDADA AWRAAFDHEE ICVAIIKHAN PCGIAISSVS 

       310        320        330        340        350        360 
VADAHRKAHE CDPLSAFGGV IATNSSVSVE MAETVADIFT EVIVAPAYEP GAVEILSRKK 

       370        380        390        400        410        420 
NIRILVAAQP PTTGTELRPI SGGLLLQQRD ALDADGDDPV NWTLATGEPA DPATLANLKF 

       430        440        450        460        470        480 
AWRSCRAVKS NAIVVVADGA TVGVGMGQVN RVDAARLAVQ RAGDRVRGAV AASDAFFPFP 

       490        500        510        520 
DGLETLTEAG VKAIVHPGGS MRDDVVTEAA AKAGISLYLT GARHFAH 

« Hide

References

[1]"Complete sequence of chromosome of Mycobacterium sp. MCS."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. expand/collapse author list , Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MCS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000384 Genomic DNA. Translation: ABG10424.1.
RefSeqYP_641480.1. NC_008146.1.

3D structure databases

ProteinModelPortalQ1B3W0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING164756.Mmcs_4319.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG10424; ABG10424; Mmcs_4319.
GeneID4113149.
KEGGmmc:Mmcs_4319.
PATRIC18118987. VBIMycSp106721_4420.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycMSP164756:GHQ8-4364-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_MYCSS
AccessionPrimary (citable) accession number: Q1B3W0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 11, 2006
Last modified: May 14, 2014
This is version 59 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