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Q7TTX6 (PUR9_SYNPX) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. 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:SYNW0249
OrganismSynechococcus sp. (strain WH8102) [Complete proteome] [HAMAP]
Taxonomic identifier84588 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length516 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 – 516516Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000018979

Sequences

Sequence LengthMass (Da)Tools
Q7TTX6 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 08B81AE6969A885A

FASTA51654,509
        10         20         30         40         50         60 
MAPFALLSVS DKNGVVALAE ALHRTHGYAL LSSGGTAKVL EDAGLPVTRM SEHNGAPEIL 

        70         80         90        100        110        120 
GGRVKTLHPR VHGGILAKRG DAAHQADLEQ QGIPAIDLVV VNLYPFRETV ARADVTWDQA 

       130        140        150        160        170        180 
IENIDIGGPA MVRAAAKNHA DVAVLTSPDQ YSSVLAAMAE SAGRVPADLC RQLALEAFQH 

       190        200        210        220        230        240 
TAAYDTAISR WMAGEVELVS SPWLEAVPLR QTLRYGENPH QKARWFSHPR QGWGGAIQLQ 

       250        260        270        280        290        300 
GKELSTNNLL DLEAALATVR EFGYGPNAVG PAAVVVKHTN PCGVAVGPVV ASALTRALDA 

       310        320        330        340        350        360 
DRVSAFGGIV AINGPVEAAA ARELTGLFLE CVVAPSFSPE AREILAAKAN LRLLELSPDA 

       370        380        390        400        410        420 
IAAAGPDHVR SILGGLLVQD LDDQVMTPDQ WTLATKRPPT AQEKQDLEFA WRLVRHVRSN 

       430        440        450        460        470        480 
AIVVARDGQS LGVGAGQMNR VGSARIALEA AAEKAKGAVL ASDGFFPFDD TVRLAASHGI 

       490        500        510 
TAVIHPGGSL RDGESVKACD ELGLAMLLTG RRHFLH 

« Hide

References

[1]"The genome of a motile marine Synechococcus."
Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P., Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T., Dufresne A., Partensky F., Webb E.A., Waterbury J.
Nature 424:1037-1042(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WH8102.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX569689 Genomic DNA. Translation: CAE06764.1.
RefSeqNP_896344.1. NC_005070.1.

3D structure databases

ProteinModelPortalQ7TTX6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING84588.SYNW0249.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE06764; CAE06764; SYNW0249.
GeneID1730253.
KEGGsyw:SYNW0249.
PATRIC23831877. VBISynSp27240_0252.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

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_SYNPX
AccessionPrimary (citable) accession number: Q7TTX6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 64 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