Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q0VMY5 (PUR9_ALCBS)

Last modified February 9, 2010. Version 31. 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: ABO_2015
OrganismAlcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]
Taxonomic identifier393595 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesAlcanivoracaceaeAlcanivorax

Protein attributes

Sequence length525 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 – 525525Bifunctional purine biosynthesis protein purH HAMAP MF_00139
PRO_1000057892

Sequences

Sequence LengthMass (Da)Tools
Q0VMY5-1 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 4C40FF4E3C0E576D

FASTA52556,122
        10         20         30         40         50         60 
MSNVERALIS VSDKTGIVEF AQALADKGVE LLSTGGTFKK LQEAGIAVRE VSDYTGFPEM 

        70         80         90        100        110        120 
MAGRVKTLHP KVHGGILGRR GQDEQVMADN DISPIDLVVV NLYPFEATVA NPDCSLEDAI 

       130        140        150        160        170        180 
ENIDIGGPTM VRSAAKNNAS VGIVTDAADY QRVLDDMAAN NGALSDDLRF DLAIKAFEHT 

       190        200        210        220        230        240 
AAYDSAIANY FGKKVEGQDG MSNLDFPRTI NLNFEKTQNM RYGENPHQKA AFYTERNPAP 

       250        260        270        280        290        300 
ASIATAKQLQ GKELSYNNIA DTDAALECVK GFTKPACVIV KHANPCGVAV SLDGITTAYD 

       310        320        330        340        350        360 
LAFATDTESA FGGIIAFNRK LDAATAQAIV DRQFVEVIIA PSATEEALAI TAAKKNVRVL 

       370        380        390        400        410        420 
VCGEMEGVAA SGLDYKRVNG GLLVQDRDLG MITEGELKVV TKRAPTEAEM HDLIFAWKVA 

       430        440        450        460        470        480 
KFVKSNAIVY AKDRQTVGVG AGQMSRVNSA RIAAIKAEHA GLQVKGSVMA SDAFFPFRDG 

       490        500        510        520 
IDNAAKVGIS CVIQPGGSIR DEEVIAAADE AGMAMVFTGM RHFRH 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM286690 Genomic DNA. Translation: CAL17463.1.
RefSeqYP_693735.1.

3D structure databases

SMRQ0VMY5. Positions 4-525.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0VMY5.

Genome annotation databases

GeneID4211146.
GenomeReviewsGene locus ABO_2015 in contig AM286690_GR.
KEGGabo:ABO_2015.
NMPDRfig|393595.12.peg.2017.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHBG498048.
OMAVVKHVKS.
PhylomeDBQ0VMY5.

Enzyme and pathway databases

BioCycABOR393595:ABO_2015-MONOMER.

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_ALCBS
AccessionPrimary (citable) accession number: Q0VMY5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: September 5, 2006
Last modified: February 9, 2010
This is version 31 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