APT1_RHIEC
ID APT1_RHIEC Reviewed; 180 AA.
AC Q2K5T4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Adenine phosphoribosyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_00004};
DE Short=APRT 1 {ECO:0000255|HAMAP-Rule:MF_00004};
DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004};
GN Name=apt1 {ECO:0000255|HAMAP-Rule:MF_00004}; OrderedLocusNames=RHE_CH03035;
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251;
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation of
CC AMP, that is energically less costly than de novo synthesis.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00004};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC from adenine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00004}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00004}.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000255|HAMAP-Rule:MF_00004}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABC91802.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000133; ABC91802.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_020921912.1; NC_007761.1.
DR AlphaFoldDB; Q2K5T4; -.
DR SMR; Q2K5T4; -.
DR STRING; 347834.RHE_CH03035; -.
DR EnsemblBacteria; ABC91802; ABC91802; RHE_CH03035.
DR GeneID; 58690547; -.
DR GeneID; 61481469; -.
DR KEGG; ret:RHE_CH03035; -.
DR eggNOG; COG0503; Bacteria.
DR HOGENOM; CLU_063339_3_0_5; -.
DR UniPathway; UPA00588; UER00646.
DR Proteomes; UP000001936; 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 Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01090; apt; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Glycosyltransferase; Purine salvage; Reference proteome;
KW Transferase.
FT CHAIN 1..180
FT /note="Adenine phosphoribosyltransferase 1"
FT /id="PRO_0000334715"
SQ SEQUENCE 180 AA; 19329 MW; D098E64A638F310D CRC64;
MGNTISELAA SIRSIPDYPN PGIIFRDITT LLGNPRAFRR AVDELVQPYA GTKVDKIAGM
EARGFILGGA VAHQLSSGFV PIRKKGKLPH DTVRIAYSLE YGVDEMEMHR DAVQPGEKVI
LVDDLIATGG TAVGATQLLR QIGAEVVGAC FVIDLPDLGG RRKLEELGVV VHTLVEFSGH
