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Reviewed, UniProtKB/Swiss-Prot A1UR09 (PUR9_BARBK)

Last modified February 9, 2010. Version 24. 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: BARBAKC583_0074
OrganismBartonella bacilliformis (strain ATCC 35685 / KC583) [Complete proteome] [HAMAP]
Taxonomic identifier360095 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length538 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 – 538538Bifunctional purine biosynthesis protein purH HAMAP MF_00139
PRO_1000018844

Sequences

Sequence LengthMass (Da)Tools
A1UR09-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: C481387E41485124

FASTA53858,021
        10         20         30         40         50         60 
MVVVSQNYPT PDLHRVRRAL LSVFDKTGLV EFAQELHAYG IELISTGGTS ESLIAAGLPV 

        70         80         90        100        110        120 
KDVSEVTGFP QIMDGRVKTL HPLIHGGLLG VRDDPSHKAA MEKHGICGID LVVVNLYPFE 

       130        140        150        160        170        180 
KTWQSGADSQ TIIENIDIGG PAMIRAAAKN HAYTGVVTAV SDYDVVLAEL KQHNGCLSFS 

       190        200        210        220        230        240 
LRRQLAARAY EHTAAYDAAI AAWFAQDLEV EMPSWQNFSG HFESMMRYGE NPHQRAAFYR 

       250        260        270        280        290        300 
TRDTRFGVAT AKVLQGKELS YNNMNDADAA FELVAEFDPQ RTAAVALIKH ANPCGVAEGQ 

       310        320        330        340        350        360 
SLKEAYLKAL MCDSVSAFGG IVALNQPLDE ECAAEIVKLF TEVIIAPDAT EAACNIIAQK 

       370        380        390        400        410        420 
KNLRLLITGG VPDPRCGGLT VKTLAGGVLV QSRDNAVVDD FDLQIVTKRA PSQDEMRDLQ 

       430        440        450        460        470        480 
FAFRVVKHVK SNAIVYAKNS ATVGIGAGQM SRLDSARIAV HKAEDNAKRM GLTESLTRGS 

       490        500        510        520        530 
VVASDAFFPF ADGLISAAEA GVTAVIQPGG SIRDQEVIEA ADARGLAMVF TGVRHFRH 

« Hide

References

[1]Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S., Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R., Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J., Fraser-Ligget C., Seshadri R.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000524 Genomic DNA. Translation: ABM45521.1.
RefSeqYP_988412.1.

3D structure databases

SMRA1UR09. Positions 16-538.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1UR09.

Genome annotation databases

GeneID4684296.
GenomeReviewsGene locus BARBAKC583_0074 in contig CP000524_GR.
KEGGbbk:BARBAKC583_0074.
NMPDRfig|360095.3.peg.1045.
TIGRBARBAKC583_0074.

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHBG498048.
OMAVVKHVKS.

Family and domain databases

HAMAPMF_00139. PurH.
[Tree]
InterProIPR002695. AICARFT_IMPCHas.
IPR013982. AICARFT_IMPCHase_bienz.
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.
SM00851. MGS. 1 hit.
[Graphical view]
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR9_BARBK
AccessionPrimary (citable) accession number: A1UR09
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: February 9, 2010
This is version 24 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