APT_ECOLI
ID APT_ECOLI Reviewed; 183 AA.
AC P69503; P07672; P09993; P77121; Q2MBV8;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=b0469, JW0458;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3527873; DOI=10.1016/0378-1119(86)90218-0;
RA Hershey H.V., Taylor M.W.;
RT "Nucleotide sequence and deduced amino acid sequence of Escherichia coli
RT adenine phosphoribosyltransferase and comparison with other analogous
RT enzymes.";
RL Gene 43:287-293(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-7.
RX PubMed=9573169; DOI=10.1128/jb.180.10.2779-2781.1998;
RA Zhang X., Zhu L., Deutscher M.P.;
RT "Oligoribonuclease is encoded by a highly conserved gene in the 3'-5'
RT exonuclease superfamily.";
RL J. Bacteriol. 180:2779-2781(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 40-183.
RX PubMed=3534795; DOI=10.1093/nar/14.20.8091;
RA Flower A.M., McHenry C.S.;
RT "The adjacent dnaZ and dnaX genes of Escherichia coli are contained within
RT one continuous open reading frame.";
RL Nucleic Acids Res. 14:8091-8101(1986).
CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation of
CC AMP, that is energically less costly than de novo synthesis.
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC family. {ECO:0000255|HAMAP-Rule:MF_00004}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40223.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M14040; AAA23455.1; -; Genomic_DNA.
DR EMBL; X04487; CAA28173.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40223.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73571.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76248.1; -; Genomic_DNA.
DR EMBL; M38777; AAA23456.1; -; Genomic_DNA.
DR PIR; A25635; RTECA.
DR RefSeq; NP_415002.1; NC_000913.3.
DR RefSeq; WP_000127356.1; NZ_STEB01000007.1.
DR PDB; 2DY0; X-ray; 1.25 A; A/B=1-183.
DR PDBsum; 2DY0; -.
DR AlphaFoldDB; P69503; -.
DR SMR; P69503; -.
DR BioGRID; 4261347; 8.
DR DIP; DIP-36165N; -.
DR IntAct; P69503; 5.
DR STRING; 511145.b0469; -.
DR SWISS-2DPAGE; P69503; -.
DR jPOST; P69503; -.
DR PaxDb; P69503; -.
DR PRIDE; P69503; -.
DR EnsemblBacteria; AAC73571; AAC73571; b0469.
DR EnsemblBacteria; BAE76248; BAE76248; BAE76248.
DR GeneID; 66671229; -.
DR GeneID; 945113; -.
DR KEGG; ecj:JW0458; -.
DR KEGG; eco:b0469; -.
DR PATRIC; fig|1411691.4.peg.1807; -.
DR EchoBASE; EB0049; -.
DR eggNOG; COG0503; Bacteria.
DR HOGENOM; CLU_063339_3_0_6; -.
DR InParanoid; P69503; -.
DR OMA; KPGIVFR; -.
DR PhylomeDB; P69503; -.
DR BioCyc; EcoCyc:ADENPRIBOSYLTRAN-MON; -.
DR BioCyc; MetaCyc:ADENPRIBOSYLTRAN-MON; -.
DR SABIO-RK; P69503; -.
DR UniPathway; UPA00588; UER00646.
DR EvolutionaryTrace; P69503; -.
DR PRO; PR:P69503; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003999; F:adenine phosphoribosyltransferase activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0006168; P:adenine salvage; IEA:UniProtKB-UniRule.
DR GO; GO:0044209; P:AMP salvage; IMP:EcoCyc.
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; Direct protein sequencing; Glycosyltransferase;
KW Purine salvage; Reference proteome; Transferase.
FT CHAIN 1..183
FT /note="Adenine phosphoribosyltransferase"
FT /id="PRO_0000149379"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:2DY0"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:2DY0"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2DY0"
FT HELIX 32..36
FT /evidence="ECO:0007829|PDB:2DY0"
FT HELIX 38..52
FT /evidence="ECO:0007829|PDB:2DY0"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:2DY0"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:2DY0"
FT HELIX 66..78
FT /evidence="ECO:0007829|PDB:2DY0"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:2DY0"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:2DY0"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:2DY0"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:2DY0"
FT STRAND 121..131
FT /evidence="ECO:0007829|PDB:2DY0"
FT HELIX 133..144
FT /evidence="ECO:0007829|PDB:2DY0"
FT STRAND 148..158
FT /evidence="ECO:0007829|PDB:2DY0"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:2DY0"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:2DY0"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:2DY0"
FT STRAND 173..180
FT /evidence="ECO:0007829|PDB:2DY0"
SQ SEQUENCE 183 AA; 19859 MW; AB45F0B5A219480D CRC64;
MTATAQQLEY LKNSIKSIQD YPKPGILFRD VTSLLEDPKA YALSIDLLVE RYKNAGITKV
VGTEARGFLF GAPVALGLGV GFVPVRKPGK LPRETISETY DLEYGTDQLE IHVDAIKPGD
KVLVVDDLLA TGGTIEATVK LIRRLGGEVA DAAFIINLFD LGGEQRLEKQ GITSYSLVPF
PGH
