APT_YERPS
ID APT_YERPS Reviewed; 187 AA.
AC Q66DQ2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 100.
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=YPTB0991;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH20231.1; -; Genomic_DNA.
DR RefSeq; WP_011191877.1; NZ_CP009712.1.
DR PDB; 4MB6; X-ray; 1.81 A; A=1-187.
DR PDB; 5B6H; X-ray; 1.90 A; A=7-187.
DR PDB; 5Y07; X-ray; 2.07 A; A/B=1-187.
DR PDB; 5Y4A; X-ray; 2.34 A; A/B=1-187.
DR PDB; 5ZC7; X-ray; 2.00 A; A/B=1-187.
DR PDB; 5ZMI; X-ray; 2.05 A; A=1-187.
DR PDB; 5ZNQ; X-ray; 1.75 A; A/B=1-187.
DR PDB; 5ZOC; X-ray; 1.98 A; A=1-187.
DR PDBsum; 4MB6; -.
DR PDBsum; 5B6H; -.
DR PDBsum; 5Y07; -.
DR PDBsum; 5Y4A; -.
DR PDBsum; 5ZC7; -.
DR PDBsum; 5ZMI; -.
DR PDBsum; 5ZNQ; -.
DR PDBsum; 5ZOC; -.
DR AlphaFoldDB; Q66DQ2; -.
DR SMR; Q66DQ2; -.
DR EnsemblBacteria; CAH20231; CAH20231; YPTB0991.
DR GeneID; 66842583; -.
DR KEGG; ypo:BZ17_1557; -.
DR KEGG; yps:YPTB0991; -.
DR PATRIC; fig|273123.14.peg.1652; -.
DR OMA; KPGIVFR; -.
DR UniPathway; UPA00588; UER00646.
DR Proteomes; UP000001011; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Glycosyltransferase; Purine salvage; Transferase.
FT CHAIN 1..187
FT /note="Adenine phosphoribosyltransferase"
FT /id="PRO_0000149493"
FT HELIX 7..18
FT /evidence="ECO:0007829|PDB:5ZNQ"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:5ZNQ"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:5ZC7"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:5ZNQ"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:5ZNQ"
FT HELIX 42..55
FT /evidence="ECO:0007829|PDB:5ZNQ"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:5ZNQ"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:5ZNQ"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:5ZNQ"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:5ZNQ"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:5ZNQ"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:5ZNQ"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:5ZNQ"
FT STRAND 125..135
FT /evidence="ECO:0007829|PDB:5ZNQ"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:5ZNQ"
FT STRAND 152..161
FT /evidence="ECO:0007829|PDB:5ZNQ"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:5ZNQ"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:5ZNQ"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:5ZNQ"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:5ZNQ"
SQ SEQUENCE 187 AA; 20143 MW; B7F85565F1737C15 CRC64;
MTVSASKTAQ QLKYIKDSIK TIPDYPKAGI LFRDVTSLLE NPKAYSASIE LLSEHYSESG
VTKVVGTEAR GFLFGAPVAL ALGVGFVPVR KPGKLPRETI SESYELEYGT DTLEIHTDSI
QPGDKVLVVD DLLATGGTIE ATVKLIRRLG GEVVHAAFII NLPELGGEAR LTQQGIHCYS
LVSFDGH
