APT_THEP3
ID APT_THEP3 Reviewed; 173 AA.
AC B0K969;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=Teth39_1027;
OS Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium
OS thermohydrosulfuricum).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=340099;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33223 / DSM 2355 / 39E;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J.,
RA Richardson P.;
RT "Complete sequence of Thermoanaerobacter pseudethanolicus 39E.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000924; ABY94682.1; -; Genomic_DNA.
DR RefSeq; WP_003869770.1; NC_010321.1.
DR PDB; 4LZA; X-ray; 1.84 A; A/B=1-173.
DR PDBsum; 4LZA; -.
DR AlphaFoldDB; B0K969; -.
DR SMR; B0K969; -.
DR STRING; 340099.Teth39_1027; -.
DR EnsemblBacteria; ABY94682; ABY94682; Teth39_1027.
DR KEGG; tpd:Teth39_1027; -.
DR eggNOG; COG0503; Bacteria.
DR HOGENOM; CLU_063339_3_0_9; -.
DR OMA; KPGIVFR; -.
DR UniPathway; UPA00588; UER00646.
DR Proteomes; UP000002156; 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;
KW Reference proteome; Transferase.
FT CHAIN 1..173
FT /note="Adenine phosphoribosyltransferase"
FT /id="PRO_1000089013"
FT HELIX 3..8
FT /evidence="ECO:0007829|PDB:4LZA"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:4LZA"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:4LZA"
FT HELIX 27..31
FT /evidence="ECO:0007829|PDB:4LZA"
FT HELIX 33..46
FT /evidence="ECO:0007829|PDB:4LZA"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:4LZA"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:4LZA"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:4LZA"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:4LZA"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:4LZA"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:4LZA"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:4LZA"
FT STRAND 116..126
FT /evidence="ECO:0007829|PDB:4LZA"
FT HELIX 128..139
FT /evidence="ECO:0007829|PDB:4LZA"
FT STRAND 143..152
FT /evidence="ECO:0007829|PDB:4LZA"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:4LZA"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:4LZA"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:4LZA"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:4LZA"
SQ SEQUENCE 173 AA; 19207 MW; FE563CBF6D203DE0 CRC64;
MTLEEIKMMI REIPDFPKKG IKFKDITPVL KDAKAFNYSI EMLAKALEGR KFDLIAAPEA
RGFLFGAPLA YRLGVGFVPV RKPGKLPAET LSYEYELEYG TDSLEIHKDA VLEGQRVVIV
DDLLATGGTI YASAKLVESL GGIVDSIIFL TELTFLDGRK KLDGYDIISL IKF
