Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P67539 (PUR9_BRUME)

Last modified June 16, 2009. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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: BMEI0233
OrganismBrucella melitensis [Complete proteome] [HAMAP]
Taxonomic identifier29459 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length538 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 – 538538Bifunctional purine biosynthesis protein purH HAMAP MF_00139
PRO_0000192074

Sequences

Sequence LengthMass (Da)Tools
P67539-1 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 099349D5160AC19F

FASTA53856,481
        10         20         30         40         50         60 
MAVSSKHIPA PDLHRVRRAL LSVSDKTGLI DFAKALHANG VEILSTGGTA KSIAAAGIPV 

        70         80         90        100        110        120 
KDVSEITGFP EIMDGRVKTL HPAVHGGLLA VRNDPEHVAA MEEHGIGGID LAVINLYPFE 

       130        140        150        160        170        180 
EVRFKGGDYD TTVENIDIGG PAMIRASAKN HAYVATVVDP ADYADVVAEL EKHSGSLPLA 

       190        200        210        220        230        240 
FRKKLAAKAF SRTAAYDAAI SNWFAEAIDE ETPTYRAVAG KLHSVMRYGE NPHQTAGFYL 

       250        260        270        280        290        300 
TGEKRPGVAT ATQLQGKQLS YNNINDTDAA FELVAEFDPA RTAAVAIIKH ANPCGVAEAS 

       310        320        330        340        350        360 
TIKEAYLKAL ACDPVSAFGG IVALNRTLDE EAAEEIVKTF TEVIIAPDAT EGAQAIVAAK 

       370        380        390        400        410        420 
KNLRLLVTGG LPDPRAKGIA AKTVAGGLLV QSRDNGVVDD LDLKVVTKRA PTEAELNDLK 

       430        440        450        460        470        480 
FAFRVGKHVK SNAIVYVKDG ATVGIGAGQM SRVDSARIAA RKAEDAAEAA GLAAPLTKGC 

       490        500        510        520        530 
VVASDAFFPF ADGLLSAVEA GATAVIQPGG SMRDDEVIAA ADEHGIAMVM TGMRHFRH 

« Hide

Cross-references

Sequence databases

AE009466 Genomic DNA. Translation: AAL51415.1.
PIRAD3281.
RefSeqNP_539151.1.

3D structure databases

HSSPHSSP built from PDB template 1G8M based on UniProtKB P31335.
ModBaseSearch...

Genome annotation databases

GeneID1195945.
GenomeReviewsGene locus BMEI0233 in contig AE008917_GR.
KEGGbme:BMEI0233.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP67539.
OMAP67539. VVKHVKS.

Enzyme and pathway databases

BioCycBMEL224914:BMEI0233-MON.
BRENDA2.1.2.3. 277959.
3.5.4.10. 277959.

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_BRUME
AccessionPrimary (citable) accession number: P67539
Secondary accession number(s): Q8FYP8, Q8YJ53
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: June 16, 2009
This is version 30 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

Brucella melitensis

Brucella melitensis (strain 16M): entries and gene names

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