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Q116T4 (PUR9_TRIEI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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:Tery_1128
OrganismTrichodesmium erythraeum (strain IMS101) [Complete proteome] [HAMAP]
Taxonomic identifier203124 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesTrichodesmium

Protein attributes

Sequence length517 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 – 517517Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018984

Sequences

Sequence LengthMass (Da)Tools
Q116T4 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 30B1AB24FF63B165

FASTA51756,371
        10         20         30         40         50         60 
MKRLALLSTS DKTGLIDLAK SLVTEFDYEI ISSGGTAKTL KDAGIYVTKV SDYTGFPEIL 

        70         80         90        100        110        120 
GGRVKTLHPR IHGGILARKD LPQDVEELNA NNIRPIDLVV VNLYPFEETI SKPEVTLAEA 

       130        140        150        160        170        180 
IEKIDIGGPA MLRASAKNFA HLTVLCNHFQ YNSYLEELRK NAGEVSLEFR QKCALAGFKH 

       190        200        210        220        230        240 
TATYDQAIAT YLQEQQTTSE SEKSEKEIFF LSGKKIKTLR YGENPHQYAT WYQRGINASG 

       250        260        270        280        290        300 
WGASKIIQGK ELSYNNLVDL EAARRIIIEF SDAPTVAILK HTNPCGVAVD ETILAAYERA 

       310        320        330        340        350        360 
FAGDSVSAFG GIVALNKSID AATAKAMTKT FLECVVAPGC EPEAEKIFKS KSKLRVLISP 

       370        380        390        400        410        420 
YFKQSEPETI KVISGGFLVQ DTDDTIDNYS DWKIVTEKQP TTEQIEELMF AWKVVKHVKS 

       430        440        450        460        470        480 
NAIVVTKNRA TVGIGAGQMN RVGAVKIALE QAGEKAIGGV LASDAFFPFD DSVKTAAAAG 

       490        500        510 
VTAIIQPGGS LKDKDSIAAA NELGLIMILT GIRHFLH 

« Hide

References

[1]"Complete sequence of Trichodesmium erythraeum IMS101."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IMS101.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000393 Genomic DNA. Translation: ABG50490.1.
RefSeqYP_720963.1. NC_008312.1.

3D structure databases

ProteinModelPortalQ116T4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203124.Tery_1128.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG50490; ABG50490; Tery_1128.
GeneID4242860.
KEGGter:Tery_1128.
PATRIC23985949. VBITriEry99848_1413.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycTERY203124:GJDR-1135-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_TRIEI
AccessionPrimary (citable) accession number: Q116T4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: February 19, 2014
This is version 59 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