GenomeNet

Database: UniProt
Entry: I6ZVG1_MELRP
LinkDB: I6ZVG1_MELRP
Original site: I6ZVG1_MELRP 
ID   I6ZVG1_MELRP            Unreviewed;       173 AA.
AC   I6ZVG1;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 57.
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   OrderedLocusNames=MROS_2759 {ECO:0000313|EMBL:AFN75989.1};
OS   Melioribacter roseus (strain JCM 17771 / P3M-2).
OC   Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC   Melioribacteraceae; Melioribacter.
OX   NCBI_TaxID=1191523 {ECO:0000313|EMBL:AFN75989.1, ECO:0000313|Proteomes:UP000009011};
RN   [1] {ECO:0000313|EMBL:AFN75989.1, ECO:0000313|Proteomes:UP000009011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 17771 / P3M-2 {ECO:0000313|Proteomes:UP000009011};
RX   PubMed=23301019; DOI=10.1371/journal.pone.0053047;
RA   Kadnikov V.V., Mardanov A.V., Podosokorskaya O.A., Gavrilov S.N.,
RA   Kublanov I.V., Beletsky A.V., Bonch-Osmolovskaya E.A., Ravin N.V.;
RT   "Genomic analysis of Melioribacter roseus, facultatively anaerobic
RT   organotrophic bacterium representing a novel deep lineage within
RT   Bacteriodetes/Chlorobi group.";
RL   PLoS ONE 8:E53047-E53047(2013).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003557; AFN75989.1; -; Genomic_DNA.
DR   RefSeq; WP_014857419.1; NC_018178.1.
DR   AlphaFoldDB; I6ZVG1; -.
DR   STRING; 1191523.MROS_2759; -.
DR   GeneID; 78567653; -.
DR   KEGG; mro:MROS_2759; -.
DR   PATRIC; fig|1191523.3.peg.2896; -.
DR   eggNOG; COG0503; Bacteria.
DR   HOGENOM; CLU_063339_3_0_10; -.
DR   OMA; QAYDLEY; -.
DR   OrthoDB; 9803963at2; -.
DR   UniPathway; UPA00588; UER00646.
DR   Proteomes; UP000009011; 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 {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:UP000009011};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00004}.
FT   DOMAIN          39..148
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
SQ   SEQUENCE   173 AA;  19206 MW;  8D6A5AC9567E45E3 CRC64;
     MDLKDYIRTV PDFPKKGIMF RDVTTLLKDG RALNYAVDRL YEISKDRGIT KVVGIESRGF
     ILGAALALKL NAGFVPVRKP GKLPAEKLAE TYELEYGSDT IEIHKDAIQK GDIVLMHDDL
     LATGGTMEAA CKLVEKLGGK IVQISFLIEL SFLKGRDKLS GYEIHSLIDY DSE
//
DBGET integrated database retrieval system