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Reviewed, UniProtKB/Swiss-Prot Q9ABY4 (PUR9_CAUCR)

Last modified June 16, 2009. Version 46. 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: CC_0086
OrganismCaulobacter crescentus (Caulobacter vibrioides) [Complete proteome] [HAMAP]
Taxonomic identifier155892 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaeCaulobacter

Protein attributes

Sequence length529 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 – 529529Bifunctional purine biosynthesis protein purH HAMAP MF_00139
PRO_0000192081

Sequences

Sequence LengthMass (Da)Tools
Q9ABY4-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 86196441DCD993D9

FASTA52955,238
        10         20         30         40         50         60 
MPAAPDYPSA PDLVAPKRAL LSVSDKTGLV DAAKILHAAG VELVSTGGTK AAIAAAGVPV 

        70         80         90        100        110        120 
KDVSDLTGFP EMMDGRVKTL HPVVHGGLLG VRDAADHAKA MADHGIGGID ILYVNLYPFE 

       130        140        150        160        170        180 
ATVAKGGSYA ECVENIDIGG PAMIRSAAKN HGYVAVCTDP SDLAEVLEAL KAGGTTLALR 

       190        200        210        220        230        240 
QQLAARAYAR TAAYDAAISA WFAEALGQDF PARKSIAGTL RQTMRYGENP HQKAAFYTFP 

       250        260        270        280        290        300 
NPRPGVATAT QLQGKELSYN NINDTDAAFE LIAEFDPAAG PAVAIIKHAN PCGVAVGATQ 

       310        320        330        340        350        360 
REAYERALAC DPTSAFGGIV AVNSRLTREA AEAMVEIFTE VVIAPEADED AIAVFAAKKN 

       370        380        390        400        410        420 
LRLLVTGGLP DALSTGDTFK SVAGGFLVQS RDDARIKASD LKIVTQRQPT EEEVRDMLFA 

       430        440        450        460        470        480 
FTVGKHVKSN AIVYARAGQT LGVGAGQMNR KDSARIAALR AADFGLDLKG CACASEAFFP 

       490        500        510        520 
FADGLIQAAE AGATAIIQPG GSMRDPEVIE AADKLGLTMA FTGVRVFRH 

« Hide

Cross-references

Sequence databases

AE005673 Genomic DNA. Translation: AAK22073.1.
PIRE87259.
RefSeqNP_418905.1.

3D structure databases

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

Genome annotation databases

GeneID944147.
GenomeReviewsGene locus CC_0086 in contig AE005673_GR.
KEGGccr:CC_0086.
NMPDRfig|190650.1.peg.85.
TIGRCC_0086.

Phylogenomic databases

HOGENOMQ9ABY4.
OMAQ9ABY4. VVKHVKS.

Enzyme and pathway databases

BRENDA2.1.2.3. 2191.
3.5.4.10. 2191.

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_CAUCR
AccessionPrimary (citable) accession number: Q9ABY4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: June 1, 2001
Last modified: June 16, 2009
This is version 46 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