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Database: UniProt
Entry: A0A023BRV2_9FLAO
LinkDB: A0A023BRV2_9FLAO
Original site: A0A023BRV2_9FLAO 
ID   A0A023BRV2_9FLAO        Unreviewed;       170 AA.
AC   A0A023BRV2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
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   ORFNames=ATO12_21525 {ECO:0000313|EMBL:EZH72717.1};
OS   Aquimarina atlantica.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Aquimarina.
OX   NCBI_TaxID=1317122 {ECO:0000313|EMBL:EZH72717.1, ECO:0000313|Proteomes:UP000023541};
RN   [1] {ECO:0000313|EMBL:EZH72717.1, ECO:0000313|Proteomes:UP000023541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II-S11-z7 {ECO:0000313|EMBL:EZH72717.1,
RC   ECO:0000313|Proteomes:UP000023541};
RA   Lai Q.;
RT   "Aquimarina sp. 22II-S11-z7 Genome Sequencing.";
RL   Submitted (APR-2014) 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|ARBA:ARBA00003968, 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|HAMAP-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EZH72717.1}.
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DR   EMBL; AQRA01000007; EZH72717.1; -; Genomic_DNA.
DR   RefSeq; WP_034243986.1; NZ_AQRA01000007.1.
DR   AlphaFoldDB; A0A023BRV2; -.
DR   STRING; 1317122.ATO12_21525; -.
DR   eggNOG; COG0503; Bacteria.
DR   OrthoDB; 9803963at2; -.
DR   UniPathway; UPA00588; UER00646.
DR   Proteomes; UP000023541; 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; 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00004};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00004};
KW   Purine salvage {ECO:0000256|ARBA:ARBA00022726, ECO:0000256|HAMAP-
KW   Rule:MF_00004}; Reference proteome {ECO:0000313|Proteomes:UP000023541};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00004}.
FT   DOMAIN          37..145
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
SQ   SEQUENCE   170 AA;  18595 MW;  9178FCE6D177A753 CRC64;
     MNIQDYIRDI SDFPKPGILF KDITPLLANH KALVSCADQL VGLCPDGVKI DKVIGIEARG
     FIIGSMIAER LQAGFIPVRK KGKLPYDVKS KSYGLEYGED TLEIHIDAIK AGEHVLIHDD
     VLATGGTAKA VCDLVKELGG VVVQCNFIME LEFLNGKDKL DVPRSALLKY
//
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