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Q3JC90 (PUR9_NITOC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional purine biosynthesis protein PurH

Including the following 2 domains:

  1. Phosphoribosylaminoimidazolecarboxamide formyltransferase
    EC=2.1.2.3
    Alternative name(s):
    AICAR transformylase
  2. IMP cyclohydrolase
    EC=3.5.4.10
    Alternative name(s):
    ATIC
    IMP synthase
    Inosinicase
Gene names
Name:purH
Ordered Locus Names:Noc_1048
OrganismNitrosococcus oceani (strain ATCC 19707 / NCIMB 11848) [Complete proteome] [HAMAP]
Taxonomic identifier323261 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesChromatiaceaeNitrosococcus

Protein attributes

Sequence length522 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-Rule MF_00139

IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule 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-Rule 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-Rule MF_00139

Sequence similarities

Belongs to the PurH family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 522522Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000057900

Sequences

Sequence LengthMass (Da)Tools
Q3JC90 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 5254E72DFC445927

FASTA52256,313
        10         20         30         40         50         60 
MKPIARALIS VSDKTGIVPF AHRLQARGVK ILSTGGSAQL LQKNNIGATE ISTYTGFPEM 

        70         80         90        100        110        120 
MGGRIKTLHP KIHGGILGRR ETDATTMAEY NIAPIDLVAV NLYPFEQTVA KPDCDLATAI 

       130        140        150        160        170        180 
ENIDIGGPTL LRAAAKNHAA VTVIVDPDDY ERVLREMEAN GGALSSSTRF ELAVKSFEHT 

       190        200        210        220        230        240 
ARYDATIANY LGALTPNGEK SAFPRSYNIQ FAKKQEMRYG ENPHQRAAFY VEQPPPAGTI 

       250        260        270        280        290        300 
ATAQQLQGKT LSFNNIADTD AALACVKAFR EAPTCVIVKH ANPCGVATGI NLQEAYERAY 

       310        320        330        340        350        360 
AADPVSAFGG IIAFNEPLDP TTAKTIIKRQ FAEVIIAPAV TTTAQEILTS KPNIRVLACG 

       370        380        390        400        410        420 
EWSSQTAAGW DYKRIVGGLL LQDQDTDTVP LEALQTVTER SPTPQELKDL LFAWQVVKFV 

       430        440        450        460        470        480 
KSNAIVYAKN GRTIGVGAGQ TSRVMSSQIA ELKAKEAGFS TQNAVLASDA FFPFRDGLEA 

       490        500        510        520 
AAKAGICAVI QPGGSRRDKE VIAAANEWDM AMLFTGMRHF RH 

« Hide

References

[1]"Complete genome sequence of the marine, chemolithoautotrophic, ammonia-oxidizing bacterium Nitrosococcus oceani ATCC 19707."
Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J., Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T., Vergez L.M., Ward B.B.
Appl. Environ. Microbiol. 72:6299-6315(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19707 / NCIMB 11848.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000127 Genomic DNA. Translation: ABA57556.1.
RefSeqYP_343086.1. NC_007484.1.

3D structure databases

ProteinModelPortalQ3JC90.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323261.Noc_1048.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA57556; ABA57556; Noc_1048.
GeneID3707231.
KEGGnoc:Noc_1048.
PATRIC22706020. VBINitOce57959_1243.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycNOCE323261:GCI3-1063-MONOMER.
UniPathwayUPA00074; UER00133.
UPA00074; UER00135.

Family and domain databases

Gene3D3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPMF_00139. PurH.
InterProIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERPTHR11692. PTHR11692. 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]
SUPFAMSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR9_NITOC
AccessionPrimary (citable) accession number: Q3JC90
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 8, 2005
Last modified: May 14, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways