ID D7N727_9FIRM Unreviewed; 173 AA.
AC D7N727;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 53.
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:EFI42690.1};
GN ORFNames=HMPREF0629_01352 {ECO:0000313|EMBL:EFI42690.1};
OS Peptoniphilus sp. oral taxon 386 str. F0131.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=575609 {ECO:0000313|EMBL:EFI42690.1, ECO:0000313|Proteomes:UP000004712};
RN [1] {ECO:0000313|EMBL:EFI42690.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0131 {ECO:0000313|EMBL:EFI42690.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA Izard J., Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Haas B.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Peptoniphilus sp. oral taxon 386 strain F0131.";
RL Submitted (FEB-2010) 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}.
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DR EMBL; GL349422; EFI42690.1; -; Genomic_DNA.
DR RefSeq; WP_009222625.1; NZ_GL349422.1.
DR AlphaFoldDB; D7N727; -.
DR STRING; 575609.HMPREF0629_01352; -.
DR eggNOG; COG0503; Bacteria.
DR HOGENOM; CLU_063339_3_0_9; -.
DR UniPathway; UPA00588; UER00646.
DR Proteomes; UP000004712; Miscellaneous, Scaffold supercont1.1.
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:UP000004712};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00004}.
FT DOMAIN 27..148
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
SQ SEQUENCE 173 AA; 19007 MW; 399DF90F3559E8A4 CRC64;
MYLADKVRAI YDYPIDGIIF RDITTLLQDG DAFKAAIDNL ISLHNNENID IIVGVEARGF
IVGAPVAYAL GCGFVPVRKP GKLPSEKVSA EYSLEYGENK VEMHVDAIKK GQRVLIVDDL
LATGGTSKAV IDLIEKLGGE VVALDFLIEL VDLKGREKLK PYNVNSILQF EEK
//
