ID   Q967M2_GIAIN            Unreviewed;       180 AA.
AC   Q967M2; A8BXA3;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=adenine phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00011893};
DE            EC=2.4.2.7 {ECO:0000256|ARBA:ARBA00011893};
GN   ORFNames=DHA2_112885 {ECO:0000313|EMBL:ESU38582.1};
OS   Giardia intestinalis (Giardia lamblia).
OC   Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX   NCBI_TaxID=5741 {ECO:0000313|EMBL:AAK56310.1};
RN   [1] {ECO:0000313|EMBL:AAK56310.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12171924; DOI=10.1074/jbc.M205595200;
RA   Sarver A.E., Wang C.C.;
RT   "The adenine phosphoribosyltransferase from Giardia lamblia has a unique
RT   reaction mechanism and unusual substrate binding properties.";
RL   J. Biol. Chem. 277:39973-39980(2002).
RN   [2] {ECO:0007829|PDB:1L1Q, ECO:0007829|PDB:1L1R}
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), AND ACTIVE SITE.
RX   PubMed=12171925; DOI=10.1074/jbc.M205596200;
RA   Shi W., Sarver A.E., Wang C.C., Tanaka K.S., Almo S.C., Schramm V.L.;
RT   "Closed site complexes of adenine phosphoribosyltransferase from Giardia
RT   lamblia reveal a mechanism of ribosyl migration.";
RL   J. Biol. Chem. 277:39981-39988(2002).
RN   [3] {ECO:0000313|Proteomes:UP000018320}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DH {ECO:0000313|Proteomes:UP000018320};
RA   Adam R., Dahlstrom E., Martens C., Bruno D., Barbian K., Porcella S.F.,
RA   Nash T.;
RT   "Genome sequencing of Giardia lamblia Genotypes A2 and B isolates (DH and
RT   GS) and comparative analysis with the genomes of Genotypes A1 and E (WB and
RT   Pig).";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:ESU38582.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DH {ECO:0000313|EMBL:ESU38582.1};
RA   Feng W., Liu Z., Li S., Tang W., Yang J.;
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:ESU38582.1, ECO:0000313|Proteomes:UP000018320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DH {ECO:0000313|EMBL:ESU38582.1,
RC   ECO:0000313|Proteomes:UP000018320};
RX   PubMed=24307482; DOI=10.1093/gbe/evt197;
RA   Adam R.D., Dahlstrom E.W., Martens C.A., Bruno D.P., Barbian K.D.,
RA   Ricklefs S.M., Hernandez M.M., Narla N.P., Patel R.B., Porcella S.F.,
RA   Nash T.E.;
RT   "Genome sequencing of Giardia lamblia genotypes A2 and B isolates (DH and
RT   GS) and comparative analysis with the genomes of genotypes A1 and E (WB and
RT   Pig).";
RL   Genome Biol. Evol. 5:2498-2511(2013).
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:0000256|ARBA:ARBA00000868};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC       from adenine: step 1/1. {ECO:0000256|ARBA:ARBA00004659}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase
CC       family. {ECO:0000256|ARBA:ARBA00008391}.
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DR   EMBL; AF378363; AAK56310.1; -; mRNA.
DR   EMBL; AHGT01000011; ESU38582.1; -; Genomic_DNA.
DR   RefSeq; XP_001704321.1; XM_001704269.1.
DR   PDB; 1L1Q; X-ray; 1.85 A; A=1-180.
DR   PDB; 1L1R; X-ray; 1.95 A; A=1-180.
DR   PDBsum; 1L1Q; -.
DR   PDBsum; 1L1R; -.
DR   AlphaFoldDB; Q967M2; -.
DR   SMR; Q967M2; -.
DR   EnsemblProtists; ESU38582; ESU38582; DHA2_112885.
DR   GeneID; 5697213; -.
DR   KEGG; gla:GL50803_00112885; -.
DR   VEuPathDB; GiardiaDB:DHA2_112885; -.
DR   VEuPathDB; GiardiaDB:GL50581_2965; -.
DR   VEuPathDB; GiardiaDB:GL50803_00112885; -.
DR   VEuPathDB; GiardiaDB:QR46_2132; -.
DR   OrthoDB; 231465at2759; -.
DR   BRENDA; 2.4.2.7; 2401.
DR   EvolutionaryTrace; Q967M2; -.
DR   Proteomes; UP000018320; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
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.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:1L1Q, ECO:0007829|PDB:1L1R};
KW   Glycosyltransferase {ECO:0000313|EMBL:AAK56310.1};
KW   Transferase {ECO:0000313|EMBL:AAK56310.1}.
FT   DOMAIN          29..177
FT                   /note="Phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00156"
FT   ACT_SITE        100
FT                   /note="EMO_00068 proton donor,EMO_00066 proton
FT                   acceptor,EMO_00066 proton acceptor,EMO_00068 proton donor"
FT                   /evidence="ECO:0007829|PDB:1L1R"
FT   SITE            63
FT                   /note="EMO_00033 electrostatic stabiliser"
FT                   /evidence="ECO:0007829|PDB:1L1R"
SQ   SEQUENCE   180 AA;  19436 MW;  E9426D7975C0CE5C CRC64;
     MTMSVADAHA LIKTIPDFPT KGIAFKDLSD ILSTPAALDA VRKEVTAHYK DVPITKVVGI
     ESRGFILGGI VANSLGVGFV ALRKAGKLPG DVCKCTFDME YQKGVTIEVQ KRQLGPHDVV
     LLHDDVLATG GTLLAAIELC ETAGVKPENI YINVLYEIEA LKGREKVGQK CTRLFSVIRE
//