ID C7RHS1_ANAPD Unreviewed; 172 AA.
AC C7RHS1;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
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=Apre_1004 {ECO:0000313|EMBL:ACV29032.1};
OS Anaerococcus prevotii (strain ATCC 9321 / DSM 20548 / JCM 6508 / NCTC 11806
OS / PC1) (Peptostreptococcus prevotii) (Peptococcus prevotii).
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerococcus.
OX NCBI_TaxID=525919 {ECO:0000313|EMBL:ACV29032.1, ECO:0000313|Proteomes:UP000002294};
RN [1] {ECO:0000313|EMBL:ACV29032.1, ECO:0000313|Proteomes:UP000002294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9321 / DSM 20548 / JCM 6508 / NCTC 11806 / PC1
RC {ECO:0000313|Proteomes:UP000002294};
RX PubMed=21304652; DOI=10.4056/sigs.24194;
RA Labutti K., Pukall R., Steenblock K., Glavina Del Rio T., Tice H.,
RA Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L.,
RA Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA Saunders E., Brettin T., Detter J.C., Han C., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Anaerococcus prevotii type strain (PC1).";
RL Stand. Genomic Sci. 1:159-165(2009).
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; CP001708; ACV29032.1; -; Genomic_DNA.
DR RefSeq; WP_015777935.1; NC_013171.1.
DR AlphaFoldDB; C7RHS1; -.
DR STRING; 525919.Apre_1004; -.
DR KEGG; apr:Apre_1004; -.
DR eggNOG; COG0503; Bacteria.
DR HOGENOM; CLU_063339_3_0_9; -.
DR OrthoDB; 9803963at2; -.
DR UniPathway; UPA00588; UER00646.
DR Proteomes; UP000002294; 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 Coiled coil {ECO:0000256|SAM:Coils};
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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00004}.
FT DOMAIN 30..165
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
FT COILED 23..50
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 172 AA; 19366 MW; A0400F873C18E76C CRC64;
MDLKSKIRVI EDYPTEGISF KDITTLLRDK DAFRETIDQL EEKLKDYDFD YIAGIESRGL
IFGAPLADRL SKGFIPIRKP GKLPGEIEKV SYELEYGSNE LEMHKDALEE GERVVILDDL
IATGGSAKAA AKLVEAVGGK VACFEFLIEL TDLKGRDYLK DYDVISLIKY NH
//
