ID APT_CHRFK Reviewed; 171 AA.
AC A0LYK2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004};
DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004};
DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004};
GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004}; OrderedLocusNames=GFO_0464;
OS Christiangramia forsetii (strain DSM 17595 / CGMCC 1.15422 / KT0803)
OS (Gramella forsetii).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Christiangramia.
OX NCBI_TaxID=411154;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17595 / CGMCC 1.15422 / KT0803;
RX PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA Gloeckner F.O.;
RT "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT reveals adaptations to degradation of polymeric organic matter.";
RL Environ. Microbiol. 8:2201-2213(2006).
CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation of
CC AMP, that is energically less costly than de novo synthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00004}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate +
CC adenine; Xref=Rhea:RHEA:16609, ChEBI:CHEBI:16708, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58017, ChEBI:CHEBI:456215; EC=2.4.2.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00004};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000255|HAMAP-Rule:MF_00004}.
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DR EMBL; CU207366; CAL65447.1; -; Genomic_DNA.
DR RefSeq; WP_011708385.1; NC_008571.1.
DR AlphaFoldDB; A0LYK2; -.
DR SMR; A0LYK2; -.
DR STRING; 411154.GFO_0464; -.
DR KEGG; gfo:GFO_0464; -.
DR eggNOG; COG0503; Bacteria.
DR HOGENOM; CLU_063339_3_0_10; -.
DR OrthoDB; 9803963at2; -.
DR UniPathway; UPA00588; UER00646.
DR Proteomes; UP000000755; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-UniRule.
DR GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR HAMAP; MF_00004; Aden_phosphoribosyltr; 1.
DR InterPro; IPR005764; Ade_phspho_trans.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR NCBIfam; TIGR01090; apt; 1.
DR PANTHER; PTHR32315; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR32315:SF3; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Glycosyltransferase; Purine salvage; Transferase.
FT CHAIN 1..171
FT /note="Adenine phosphoribosyltransferase"
FT /id="PRO_0000329347"
SQ SEQUENCE 171 AA; 19102 MW; 7DDAD2787D64F82C CRC64;
MELKSYVREI ADFPKKGVSY KDITPLLLDP EAMRLAVKLF MKNLPHGKID KVVGIESRGF
FFATMLAEKL NAGFIPVRKP GKLPHRTHKE NYDLEYGSDS LEIHEDAIKK GEKVLLHDDV
LATGGTAAAT CKLIEKCGGE IVQCNFLVEL EFLKGVDKLK GYDVCSLIKY S
//
