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Q7TTX6

- PUR9_SYNPX

UniProt

Q7TTX6 - PUR9_SYNPX

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Protein

Bifunctional purine biosynthesis protein PurH

Gene
purH, SYNW0249
Organism
Synechococcus sp. (strain WH8102)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotation
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotation

Pathwayi

GO - Molecular functioni

  1. IMP cyclohydrolase activity Source: UniProtKB-HAMAP
  2. phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein PurH
Including the following 2 domains:
Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC:2.1.2.3)
Alternative name(s):
AICAR transformylase
IMP cyclohydrolase (EC:3.5.4.10)
Alternative name(s):
ATIC
IMP synthase
Inosinicase
Gene namesi
Name:purH
Ordered Locus Names:SYNW0249
OrganismiSynechococcus sp. (strain WH8102)
Taxonomic identifieri84588 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000001422: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 516516Bifunctional purine biosynthesis protein PurHUniRule annotationPRO_1000018979Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi84588.SYNW0249.

Structurei

3D structure databases

ProteinModelPortaliQ7TTX6.

Family & Domainsi

Domaini

The IMP cyclohydrolase activity resides in the N-terminal region By similarity.UniRule annotation

Sequence similaritiesi

Belongs to the PurH family.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230373.
KOiK00602.
OMAiRAFKTDP.
OrthoDBiEOG6QCDFF.

Family and domain databases

Gene3Di3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPiMF_00139. PurH.
InterProiIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERiPTHR11692. PTHR11692. 1 hit.
PfamiPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFiPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTiSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR00355. purH. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7TTX6-1 [UniParc]FASTAAdd to Basket

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MAPFALLSVS DKNGVVALAE ALHRTHGYAL LSSGGTAKVL EDAGLPVTRM    50
SEHNGAPEIL GGRVKTLHPR VHGGILAKRG DAAHQADLEQ QGIPAIDLVV 100
VNLYPFRETV ARADVTWDQA IENIDIGGPA MVRAAAKNHA DVAVLTSPDQ 150
YSSVLAAMAE SAGRVPADLC RQLALEAFQH TAAYDTAISR WMAGEVELVS 200
SPWLEAVPLR QTLRYGENPH QKARWFSHPR QGWGGAIQLQ GKELSTNNLL 250
DLEAALATVR EFGYGPNAVG PAAVVVKHTN PCGVAVGPVV ASALTRALDA 300
DRVSAFGGIV AINGPVEAAA ARELTGLFLE CVVAPSFSPE AREILAAKAN 350
LRLLELSPDA IAAAGPDHVR SILGGLLVQD LDDQVMTPDQ WTLATKRPPT 400
AQEKQDLEFA WRLVRHVRSN AIVVARDGQS LGVGAGQMNR VGSARIALEA 450
AAEKAKGAVL ASDGFFPFDD TVRLAASHGI TAVIHPGGSL RDGESVKACD 500
ELGLAMLLTG RRHFLH 516
Length:516
Mass (Da):54,509
Last modified:October 1, 2003 - v1
Checksum:i08B81AE6969A885A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX569689 Genomic DNA. Translation: CAE06764.1.
RefSeqiNP_896344.1. NC_005070.1.
WP_011127125.1. NC_005070.1.

Genome annotation databases

EnsemblBacteriaiCAE06764; CAE06764; SYNW0249.
GeneIDi1730253.
KEGGisyw:SYNW0249.
PATRICi23831877. VBISynSp27240_0252.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX569689 Genomic DNA. Translation: CAE06764.1 .
RefSeqi NP_896344.1. NC_005070.1.
WP_011127125.1. NC_005070.1.

3D structure databases

ProteinModelPortali Q7TTX6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 84588.SYNW0249.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE06764 ; CAE06764 ; SYNW0249 .
GeneIDi 1730253.
KEGGi syw:SYNW0249.
PATRICi 23831877. VBISynSp27240_0252.

Phylogenomic databases

eggNOGi COG0138.
HOGENOMi HOG000230373.
KOi K00602.
OMAi RAFKTDP.
OrthoDBi EOG6QCDFF.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .

Family and domain databases

Gene3Di 3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPi MF_00139. PurH.
InterProi IPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view ]
PANTHERi PTHR11692. PTHR11692. 1 hit.
Pfami PF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view ]
PIRSFi PIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTi SM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view ]
SUPFAMi SSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsi TIGR00355. purH. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: WH8102.

Entry informationi

Entry nameiPUR9_SYNPX
AccessioniPrimary (citable) accession number: Q7TTX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 1, 2003
Last modified: September 3, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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