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Reviewed, UniProtKB/Swiss-Prot A7ZCZ7 (PUR9_CAMC1)

Last modified February 9, 2010. Version 16. 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: Ccon26_07810
ORF Names: CCC13826_1632
OrganismCampylobacter concisus (strain 13826) [Complete proteome] [HAMAP]
Taxonomic identifier360104 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length510 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 – 510510Bifunctional purine biosynthesis protein purH HAMAP MF_00139
PRO_1000018867

Sequences

Sequence LengthMass (Da)Tools
A7ZCZ7-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: DF4AFCA8C9A9B2AC

FASTA51056,510
        10         20         30         40         50         60 
MRALLSVSDK EGIVEFAKGL EELDWQILST GGTYKLLKAE GVKATEVSEF TASPEMFEGR 

        70         80         90        100        110        120 
VKTLHPKVHG GILHKRDDAT HVAQAKEHGI EGIDLVCVNL YPFKETTIRT DDFAEIIENI 

       130        140        150        160        170        180 
DIGGPAMVRS AAKNFKDVLI VTSVLDYDEI LKRLKEKSDD YEFRRSLMIK AFEHTAAYDS 

       190        200        210        220        230        240 
MIANYMNDRF NGGFGDARFI VGSKVFDTRY GENPHQKGAL YEFDYFFTNN FRALKGEASF 

       250        260        270        280        290        300 
NNMTDINGAL MLATSFDDAP AVAIIKHANP CGFAVKDTLL ESYVAALKCD PISAYGGVVA 

       310        320        330        340        350        360 
INGTLDEELA KKINEIYVEV IIAANVDDAA LKVFESKKRI KIFTQDNKFL VRANDKFDFK 

       370        380        390        400        410        420 
HIDGGFVFQE RDFVKDEELE NMKQMSKKFA TGSELKDAQI AWKVAALTKS NCVVYVKDGA 

       430        440        450        460        470        480 
MVAIGMGMTS RVDAARAAVA KAKELKIDLS GCVLASEAFF PFRDSIDIAS KVGVKCVIEP 

       490        500        510 
GGSIRDDEVI EAADEHGMSL YFTGVRHFLH 

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References

[1]"Genome sequence of Campylobacter concisus 13826 isolated from human feces."
Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., On S., Nelson K.E.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000792 Genomic DNA. Translation: EAT97421.1.
RefSeqYP_001466655.1.

3D structure databases

SMRA7ZCZ7. Positions 2-510.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7ZCZ7.

Genome annotation databases

GeneID5596305.
GenomeReviewsGene locus Ccon26_07810 in contig CP000792_GR.
KEGGcco:CCC13826_1632.

Organism-specific databases

CMRSearch...

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_CAMC1
AccessionPrimary (citable) accession number: A7ZCZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 23, 2007
Last modified: February 9, 2010
This is version 16 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