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Protein

Adenine phosphoribosyltransferase

Gene

apt

Organism
Clostridium botulinum (strain Eklund 17B / Type B)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.UniRule annotation

Catalytic activityi

AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate.UniRule annotation

Pathwayi: AMP biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes AMP from adenine.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Adenine phosphoribosyltransferase (apt)
This subpathway is part of the pathway AMP biosynthesis via salvage pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from adenine, the pathway AMP biosynthesis via salvage pathway and in Purine metabolism.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosyltransferase, Transferase
Biological processPurine salvage

Enzyme and pathway databases

UniPathwayiUPA00588; UER00646.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenine phosphoribosyltransferaseUniRule annotation (EC:2.4.2.7UniRule annotation)
Short name:
APRTUniRule annotation
Gene namesi
Name:aptUniRule annotation
Ordered Locus Names:CLL_A1030
OrganismiClostridium botulinum (strain Eklund 17B / Type B)
Taxonomic identifieri935198 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000001195 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000889651 – 172Adenine phosphoribosyltransferaseAdd BLAST172

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB2TMZ9.
SMRiB2TMZ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the purine/pyrimidine phosphoribosyltransferase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000036776.
KOiK00759.
OMAiCAPIRKK.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
HAMAPiMF_00004. Aden_phosphoribosyltr. 1 hit.
InterProiView protein in InterPro
IPR005764. Ade_phspho_trans.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
PfamiView protein in Pfam
PF00156. Pribosyltran. 1 hit.
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR01090. apt. 1 hit.

Sequencei

Sequence statusi: Complete.

B2TMZ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLKEKIRII DGFPKEGISF KDITTLIGDG EGLKASIDMF VEYLKDKNVD
60 70 80 90 100
LIVGPEARGF IFGVPVAYAL GAGFVPVRKP GKLPGETISV NYDLEYGSDS
110 120 130 140 150
LQIHKDSIKK GQRVAIVDDL LATGGTVEGV AKLVEEAGGE VVSLAFLIEL
160 170
IDLKGRDKLG DYDVISLTQY DI
Length:172
Mass (Da):18,590
Last modified:July 1, 2008 - v1
Checksum:i3A5C28D50A29C877
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001056 Genomic DNA. Translation: ACD23451.1.
RefSeqiWP_012424264.1. NC_018648.1.

Genome annotation databases

EnsemblBacteriaiACD23451; ACD23451; CLL_A1030.
GeneIDi19964516.
KEGGicbk:CLL_A1030.
PATRICifig|935198.13.peg.979.

Similar proteinsi

Entry informationi

Entry nameiAPT_CLOBB
AccessioniPrimary (citable) accession number: B2TMZ9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: October 25, 2017
This is version 62 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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