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A8G8G3 (PUR9_SERP5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. 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:Spro_0293
OrganismSerratia proteamaculans (strain 568) [Complete proteome] [HAMAP]
Taxonomic identifier399741 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

Protein attributes

Sequence length529 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 – 529529Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000057913

Sequences

Sequence LengthMass (Da)Tools
A8G8G3 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 964F4C267E8240A9

FASTA52957,335
        10         20         30         40         50         60 
MQQPRPIRRA LLSVSDKAGI VEFAEALSQR GVELLSTGGT ARLLADAGLP VTEVSDYTGF 

        70         80         90        100        110        120 
PEMMDGRVKT LHPKVHGGIL GRRGQDDAIM GQHDIKPIDM VVVNLYPFAQ TVARPNCSLE 

       130        140        150        160        170        180 
DAVENIDIGG PTMVRSAAKN HKDVAIVVKS SDYAAIITEM DNNDGSLQYT TRFDLAIKAF 

       190        200        210        220        230        240 
EHTAAYDSMI ANYFGALVPA YHGDTEQPAG RFPRTLNLNY IKKQDMRYGE NSHQQAAFYI 

       250        260        270        280        290        300 
EENVQEASVA TAEQLQGKAL SYNNIADTDA ALECVKEFAE PACVIVKHAN PCGVAIGDDI 

       310        320        330        340        350        360 
LSAYERAYQT DPTSAFGGII AFNRELDAAT AQAIISRQFV EVIIAPSISQ EARSLLAAKQ 

       370        380        390        400        410        420 
NVRVLACGQW QQRIAALDFK RVNGGLLVQD RDLGMVSEGD LRVVSERQPT AQELRDALFC 

       430        440        450        460        470        480 
WKVAKFVKSN AIVYARDNMT IGIGAGQMSR VYSAKIAGIK AADEGLEVKG SAMASDAFFP 

       490        500        510        520 
FRDGIDAAAA VGISCVIQPG GSIRDDEVIA AANEHGIAMI FTDMRHFRH 

« Hide

References

[1]"Complete sequence of chromosome of Serratia proteamaculans 568."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. expand/collapse author list , Taghavi S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 568.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000826 Genomic DNA. Translation: ABV39403.1.
RefSeqYP_001476531.1. NC_009832.1.

3D structure databases

ProteinModelPortalA8G8G3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING399741.Spro_0293.

Proteomic databases

PRIDEA8G8G3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV39403; ABV39403; Spro_0293.
GeneID5607182.
KEGGspe:Spro_0293.
PATRIC32413222. VBISerPro44537_0334.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycSPRO399741:GI55-307-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_SERP5
AccessionPrimary (citable) accession number: A8G8G3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 13, 2007
Last modified: May 14, 2014
This is version 45 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