ID A0A1Y5S4A0_9RHOB Unreviewed; 177 AA.
AC A0A1Y5S4A0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011893, ECO:0000256|HAMAP-Rule:MF_00004};
DE Short=APRT {ECO:0000256|HAMAP-Rule:MF_00004};
DE EC=2.4.2.7 {ECO:0000256|ARBA:ARBA00011893, ECO:0000256|HAMAP-Rule:MF_00004};
GN Name=apt {ECO:0000256|HAMAP-Rule:MF_00004,
GN ECO:0000313|EMBL:SLN32052.1};
GN ORFNames=AQS8620_01054 {ECO:0000313|EMBL:SLN32052.1};
OS Aquimixticola soesokkakensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Aquimixticola.
OX NCBI_TaxID=1519096 {ECO:0000313|EMBL:SLN32052.1, ECO:0000313|Proteomes:UP000193862};
RN [1] {ECO:0000313|EMBL:SLN32052.1, ECO:0000313|Proteomes:UP000193862}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8620 {ECO:0000313|EMBL:SLN32052.1,
RC ECO:0000313|Proteomes:UP000193862};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation of
CC AMP, that is energically less costly than de novo synthesis.
CC {ECO:0000256|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:0000256|ARBA:ARBA00000868, ECO:0000256|HAMAP-
CC Rule:MF_00004};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC from adenine: step 1/1. {ECO:0000256|ARBA:ARBA00004659,
CC ECO:0000256|HAMAP-Rule:MF_00004}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_00004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00004}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000256|ARBA:ARBA00008391, ECO:0000256|HAMAP-
CC Rule:MF_00004}.
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DR EMBL; FWFS01000003; SLN32052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5S4A0; -.
DR OrthoDB; 9803963at2; -.
DR UniPathway; UPA00588; UER00646.
DR Proteomes; UP000193862; Unassembled WGS sequence.
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; PTHR11776; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11776:SF7; PRIBOSYLTRAN DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00004};
KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00004,
KW ECO:0000313|EMBL:SLN32052.1};
KW Purine salvage {ECO:0000256|ARBA:ARBA00022726, ECO:0000256|HAMAP-
KW Rule:MF_00004}; Reference proteome {ECO:0000313|Proteomes:UP000193862};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00004, ECO:0000313|EMBL:SLN32052.1}.
FT DOMAIN 40..154
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
SQ SEQUENCE 177 AA; 19043 MW; 1FF29DDF82CEBC11 CRC64;
MSKNVKDYIR TIADFPHEGI MFRDVTTLFA DPRGMRLAID QLLEPYVGQR IDKVVGLEAR
GFILGGAIAH QLAVGFVPIR KKGKLPGAVI SEAYTLEYGE AVVEVHDDAI QPGEKILLVD
DLLATGGTAS AGVKLIERLG GKIVGCAFVI DLPEIGGRKV LEDMGYDIHA LCAFSGH
//
