Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q81ZG8 (PUR9_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. 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:BA_0298, GBAA_0298, BAS0285
OrganismBacillus anthracis
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length511 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 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. HAMAP MF_00139

Sequence similarities

Belongs to the PurH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 511511Bifunctional purine biosynthesis protein PurH HAMAP MF_00139
PRO_1000018838

Sequences

Sequence LengthMass (Da)Tools
Q81ZG8 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 19080315B512F890

FASTA51155,516
        10         20         30         40         50         60 
MKKRALVSVS DKTGVVEFVK GLLEQGIEVI STGGTKKLLE ENGLQVIGIS EVTGFPEIMD 

        70         80         90        100        110        120 
GRVKTLHPNI HGGLLAVRDN ETHVAQMNEL GMEPIDFVVV NLYPFKETIA KPDVTFADAI 

       130        140        150        160        170        180 
ENIDIGGPTM IRSAAKNHKF VSVIVDPVDY DVVLAELKEN GEVAEETKRK LAAKVFRHTA 

       190        200        210        220        230        240 
AYDALISNYL TEQMGEESPE TLTVTFEKKQ DLRYGENPHQ KATFYKAPFA ATSSVAYAEQ 

       250        260        270        280        290        300 
LHGKELSYNN INDADAALSI VKEFTEPAVV AVKHMNPCGV GVGTDIHEAY TRAYEADPVS 

       310        320        330        340        350        360 
IFGGIIAANR EIDKATAEKL HEIFLEIIIA PSFSKEALEV LQSKKNLRLL TVNIEKATSA 

       370        380        390        400        410        420 
SKKLTSVQGG LLVQEEDTLS LDESTISIPT KREPSEQEWK DLKLAWKVVK HVKSNAIVLA 

       430        440        450        460        470        480 
KDDMTIGVGA GQMNRVGSAK IAITQAGEKA QGSALASDAF FPMPDTVEEA AKAGITAIIQ 

       490        500        510 
PGGSIRDEDS IKVADTYGIA MVFTGVRHFK H 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.
[3]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016879 Genomic DNA. Translation: AAP24334.1.
AE017334 Genomic DNA. Translation: AAT29385.1.
AE017225 Genomic DNA. Translation: AAT52616.1.
RefSeqNP_842848.1. NC_003997.3.
YP_016910.1. NC_007530.2.
YP_026565.1. NC_005945.1.

3D structure databases

HSSPHSSP built from PDB template 1P4R based on UniProtKB P31939.
ProteinModelPortalQ81ZG8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000010856; EBBACP00000010612; EBBACG00000010848.
EBBACT00000016675; EBBACP00000016296; EBBACG00000016666.
EBBACT00000024033; EBBACP00000023518; EBBACG00000024024.
GeneID1085697.
2818909.
2848503.
GenomeReviewsGene locus BA_0298 in contig AE016879_GR.
Gene locus BAS0285 in contig AE017225_GR.
Gene locus GBAA_0298 in contig AE017334_GR.
KEGGban:BA_0298.
bar:GBAA_0298.
bat:BAS0285.
TIGRBA_0298.
GBAA_0298.

Phylogenomic databases

GeneTreeEBGT00050000002320.
HOGENOMHBG498048.
OMAFTGTRHF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycBANT260799:BAS0285-MONOMER.
BANT261594:GBAA0298-MONOMER.

Family and domain databases

HAMAPMF_00139. PurH.
[Tree]
InterProIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
Gene3DG3DSA:3.40.140.20. G3DSA:3.40.140.20. 2 hits.
G3DSA:3.40.50.1380. MGS-like_dom. 1 hit.
KOK00602.
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.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF53927. Cytidine_deaminase-like. 1 hit.
SSF52335. MGS-like_dom. 1 hit.
TIGRFAMsTIGR00355. PurH. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR9_BACAN
AccessionPrimary (citable) accession number: Q81ZG8
Secondary accession number(s): Q6I4B5, Q6KY17
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 2003
Last modified: November 16, 2011
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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families