APT_BORA1
ID APT_BORA1 Reviewed; 182 AA.
AC Q2KUE4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 88.
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}; OrderedLocusNames=BAV3106;
OS Bordetella avium (strain 197N).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N;
RX PubMed=16885469; DOI=10.1128/jb.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(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}.
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DR EMBL; AM167904; CAJ50716.1; -; Genomic_DNA.
DR RefSeq; WP_012418744.1; NC_010645.1.
DR AlphaFoldDB; Q2KUE4; -.
DR SMR; Q2KUE4; -.
DR STRING; 360910.BAV3106; -.
DR EnsemblBacteria; CAJ50716; CAJ50716; BAV3106.
DR GeneID; 41394942; -.
DR KEGG; bav:BAV3106; -.
DR eggNOG; COG0503; Bacteria.
DR HOGENOM; CLU_063339_3_0_4; -.
DR OMA; KPGIVFR; -.
DR OrthoDB; 1532478at2; -.
DR UniPathway; UPA00588; UER00646.
DR Proteomes; UP000001977; 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..182
FT /note="Adenine phosphoribosyltransferase"
FT /id="PRO_1000000259"
SQ SEQUENCE 182 AA; 20131 MW; 224AA2F240F2F124 CRC64;
MQTDYAEVVR RTIRSVPDWP VPGVTFRDIT PVLQDPRTFR ALVDLFVYRY MRQRLDLVAG
VDARGFILGS VLAYELNLGF VPVRKKGKLP YRTVAEEYSL EYGNATVEIH TDAVRTGQRV
LLVDDLIATG GTMVAAIKLL QRLGANVVEA AAIIDLPYIG GSQHIAETGT PLYTVCQFSA
TD