ID APT_BRUSU Reviewed; 181 AA.
AC P63543; G0KC24; Q8YIG8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Adenine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00004};
DE Short=APRT {ECO:0000255|HAMAP-Rule:MF_00004};
DE EC=2.4.2.7 {ECO:0000255|HAMAP-Rule:MF_00004};
GN Name=apt {ECO:0000255|HAMAP-Rule:MF_00004};
GN OrderedLocusNames=BR1540, BS1330_I1534;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
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=AAN30450.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AEM18866.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014291; AAN30450.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002997; AEM18866.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_002964645.1; NZ_KN046804.1.
DR AlphaFoldDB; P63543; -.
DR SMR; P63543; -.
DR GeneID; 55591180; -.
DR KEGG; bms:BR1540; -.
DR KEGG; bsi:BS1330_I1534; -.
DR PATRIC; fig|204722.21.peg.1829; -.
DR HOGENOM; CLU_063339_3_0_5; -.
DR PhylomeDB; P63543; -.
DR UniPathway; UPA00588; UER00646.
DR Proteomes; UP000007104; Chromosome I.
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; PTHR11776; ADENINE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11776:SF7; PRIBOSYLTRAN DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Glycosyltransferase; Purine salvage; Transferase.
FT CHAIN 1..181
FT /note="Adenine phosphoribosyltransferase"
FT /id="PRO_0000149365"
SQ SEQUENCE 181 AA; 19614 MW; 128ABF9D88C2A953 CRC64;
MESGFKVTLK DAIRTIPDYP KPGVQFRDVT TLMGNAQAFR RAVDELVYPY AGNRIDKVAG
IEARGFILGG AIAHQLSAGF VPIRKKGKLP RDTVRIAYSL EYGVDEMEMH RDAIEKGERV
VLVDDLIATG GTAEAAAKLL LQMGAEIVAA CFIIDLPDLG GRKKLEALGL PVRTLVAFEG
D
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