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Reviewed, UniProtKB/Swiss-Prot Q1LU51 (PUR9_BAUCH)

Last modified June 16, 2009. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Bifunctional purine biosynthesis protein purH
Including the following 2 domains:
    1- Recommended name:
            Phosphoribosylaminoimidazolecarboxamide formyltransferase
              EC=2.1.2.3
        Alternative name(s):
            AICAR transformylase
    2- Recommended name:
            IMP cyclohydrolase
              EC=3.5.4.10
        Alternative name(s):
            Inosinicase
            IMP synthetase
            ATIC
Gene names
Name: purH
Ordered Locus Names: BCI_0035
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia

Protein attributes

Sequence length526 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Sequence similarities

Belongs to the purH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 526526Bifunctional purine biosynthesis protein purH HAMAP MF_00139
PRO_1000018847

Sequences

Sequence LengthMass (Da)Tools
Q1LU51-1 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 4A77AA22AA874B48

FASTA52658,384
        10         20         30         40         50         60 
MQRPIIIRRA LLSVSDKTNI CELAKSLLKR GVQLISTNGT ARLLVNAGIH VTEVSNYTGF 

        70         80         90        100        110        120 
PEIMDGRVKT LHPKIHGGIL ARRNIDDTIM QQYKIEHIDM VVVNLYPFAE VVASATCNHE 

       130        140        150        160        170        180 
KVVENIDIGG TALLRSAAKN YSNVVVVVSI NDYISIINEI DCNNGAVSLE TRLNLAIKAF 

       190        200        210        220        230        240 
QHTATYDSQI KDYFTSQVYT DSSKCSSIFP PILNINFVKK QDMRYGENQH QLAAFYLDTR 

       250        260        270        280        290        300 
NKEKSIATTK QLQGRALSYN NIADADAALE CVKEFSEPAC VIVKHINPCS VAMGKTILVA 

       310        320        330        340        350        360 
YQRAYETDPT SAFGGVIAFN RSLDLCTAQE IIARQFIEVI IAPTVDQEAL LILAKKKNIR 

       370        380        390        400        410        420 
VLSSGQWNKP IPNLNFRQVN GGLLVQERDL VMINLHDLRI VSQRQPTTME IQDALFCWKV 

       430        440        450        460        470        480 
VKFVKSNAIV YARNQRTIGI GAGQMSRIDS AKIASIKAID NKLNIRGSTM ASDAFFPFRD 

       490        500        510        520 
GLDSAAKVGV SCVIQPGGSI RDQEVITAAN EHNIAMIFTN IRHFRH 

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References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000238 Genomic DNA. Translation: ABF13814.1.
RefSeqYP_588513.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4056143.
GenomeReviewsGene locus BCI_0035 in contig CP000238_GR.
KEGGbci:BCI_0035.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1LU51.
OMAQ1LU51. VVKHVKS.

Family and domain databases

HAMAPMF_00139.
[Tree]
InterProIPR002695. AICARFT_IMPCHas.
IPR013982. AICARFT_IMPCHas_formly.
IPR011607. MGS.
[Graphical view]
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.
[Graphical view]
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR9_BAUCH
AccessionPrimary (citable) accession number: Q1LU51
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 30, 2006
Last modified: June 16, 2009
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents