POA1_YEAST
ID POA1_YEAST Reviewed; 177 AA.
AC P38218; D6VQ24;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=ADP-ribose 1''-phosphate phosphatase;
DE EC=3.1.3.84;
DE EC=3.2.2.-;
DE AltName: Full=[Protein ADP-ribosylglutamate] hydrolase;
GN Name=POA1; OrderedLocusNames=YBR022W; ORFNames=YBR0304;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091864; DOI=10.1002/yea.320100010;
RA Smits P.H.M., de Haan M., Maat C., Grivell L.A.;
RT "The complete sequence of a 33 kb fragment on the right arm of chromosome
RT II from Saccharomyces cerevisiae reveals 16 open reading frames, including
RT ten new open reading frames, five previously identified genes and a
RT homologue of the SCO1 gene.";
RL Yeast 10:S75-S80(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION.
RX PubMed=10550052; DOI=10.1126/science.286.5442.1153;
RA Martzen M.R., McCraith S.M., Spinelli S.L., Torres F.M., Fields S.,
RA Grayhack E.J., Phizicky E.M.;
RT "A biochemical genomics approach for identifying genes by the activity of
RT their products.";
RL Science 286:1153-1155(1999).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP DOMAIN.
RX PubMed=15902274; DOI=10.1038/sj.emboj.7600664;
RA Karras G.I., Kustatscher G., Buhecha H.R., Allen M.D., Pugieux C., Sait F.,
RA Bycroft M., Ladurner A.G.;
RT "The macro domain is an ADP-ribose binding module.";
RL EMBO J. 24:1911-1920(2005).
RN [8]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15684411; DOI=10.1093/nar/gki211;
RA Shull N.P., Spinelli S.L., Phizicky E.M.;
RT "A highly specific phosphatase that acts on ADP-ribose 1''-phosphate, a
RT metabolite of tRNA splicing in Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 33:650-660(2005).
RN [9]
RP FUNCTION.
RX PubMed=23474712; DOI=10.1038/nsmb.2523;
RA Jankevicius G., Hassler M., Golia B., Rybin V., Zacharias M., Timinszky G.,
RA Ladurner A.G.;
RT "A family of macrodomain proteins reverses cellular mono-ADP-
RT ribosylation.";
RL Nat. Struct. Mol. Biol. 20:508-514(2013).
CC -!- FUNCTION: Highly specific phosphatase involved in the metabolism of
CC ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of
CC tRNA splicing. Removes ADP-ribose from glutamate residues in proteins
CC bearing a single ADP-ribose moiety. Inactive towards proteins bearing
CC poly-ADP-ribose. {ECO:0000269|PubMed:10550052,
CC ECO:0000269|PubMed:15684411, ECO:0000269|PubMed:23474712}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP-beta-D-ribose 1''-phosphate + H2O = ADP-D-ribose +
CC phosphate; Xref=Rhea:RHEA:25029, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57967, ChEBI:CHEBI:58753; EC=3.1.3.84;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.8 uM for ADP-ribose 1''-phosphate {ECO:0000269|PubMed:15684411};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:15684411};
CC -!- MISCELLANEOUS: Present with 1170 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the POA1 family. {ECO:0000305}.
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DR EMBL; Z35891; CAA84964.1; -; Genomic_DNA.
DR EMBL; X76078; CAA53679.1; -; Genomic_DNA.
DR EMBL; AY557705; AAS56031.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07144.1; -; Genomic_DNA.
DR PIR; S45878; S45878.
DR RefSeq; NP_009578.1; NM_001178370.1.
DR PDB; 6LFQ; X-ray; 2.36 A; A=1-177.
DR PDB; 6LFR; X-ray; 1.78 A; A=1-177.
DR PDB; 6LFS; X-ray; 1.87 A; A=1-177.
DR PDB; 6LFT; X-ray; 1.57 A; A=1-177.
DR PDB; 6LFU; X-ray; 3.12 A; A/B=1-177.
DR PDBsum; 6LFQ; -.
DR PDBsum; 6LFR; -.
DR PDBsum; 6LFS; -.
DR PDBsum; 6LFT; -.
DR PDBsum; 6LFU; -.
DR AlphaFoldDB; P38218; -.
DR SMR; P38218; -.
DR BioGRID; 32725; 39.
DR IntAct; P38218; 1.
DR STRING; 4932.YBR022W; -.
DR iPTMnet; P38218; -.
DR MaxQB; P38218; -.
DR PaxDb; P38218; -.
DR PRIDE; P38218; -.
DR EnsemblFungi; YBR022W_mRNA; YBR022W; YBR022W.
DR GeneID; 852310; -.
DR KEGG; sce:YBR022W; -.
DR SGD; S000000226; POA1.
DR VEuPathDB; FungiDB:YBR022W; -.
DR eggNOG; ENOG502S60W; Eukaryota.
DR HOGENOM; CLU_054419_1_2_1; -.
DR OMA; IFGVPWE; -.
DR BioCyc; MetaCyc:G3O-29003-MON; -.
DR BioCyc; YEAST:G3O-29003-MON; -.
DR BRENDA; 3.1.3.84; 984.
DR PRO; PR:P38218; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38218; protein.
DR GO; GO:0047407; F:ADP-ribosyl-[dinitrogen reductase] hydrolase activity; IDA:SGD.
DR GO; GO:0016791; F:phosphatase activity; IDA:SGD.
DR GO; GO:0140291; P:peptidyl-glutamate ADP-deribosylation; IBA:GO_Central.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; TAS:SGD.
DR Gene3D; 3.40.220.10; -; 1.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR Pfam; PF01661; Macro; 1.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..177
FT /note="ADP-ribose 1''-phosphate phosphatase"
FT /id="PRO_0000202470"
FT DOMAIN 1..177
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT BINDING 9..11
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 24..26
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 31..36
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 147..153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:6LFT"
FT STRAND 19..29
FT /evidence="ECO:0007829|PDB:6LFT"
FT HELIX 34..42
FT /evidence="ECO:0007829|PDB:6LFT"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:6LFT"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:6LFT"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:6LFT"
FT STRAND 76..86
FT /evidence="ECO:0007829|PDB:6LFT"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:6LFT"
FT HELIX 94..113
FT /evidence="ECO:0007829|PDB:6LFT"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:6LFT"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:6LFT"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:6LFT"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:6LFT"
FT HELIX 156..164
FT /evidence="ECO:0007829|PDB:6LFT"
FT TURN 165..169
FT /evidence="ECO:0007829|PDB:6LFT"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:6LFT"
SQ SEQUENCE 177 AA; 19938 MW; 006E55E9E598887A CRC64;
MSNITYVKGN ILKPKSYARI LIHSCNCNGS WGGGIAYQLA LRYPKAEKDY VEVCEKYGSN
LLGKCILLPS YENSDLLICC LFTSSFGGSS HGEKQSILNY TKLALDKLKT FREAKDKTRT
SEDSIGDYLN GHIKYPIGEY KLEMPQINSG IFGVPWKETE RVLEEFSGDM SFTVYQL
