Y1521_ARCFU
ID Y1521_ARCFU Reviewed; 192 AA.
AC O28751;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=ADP-ribose glycohydrolase AF_1521 {ECO:0000305};
DE AltName: Full=[Protein ADP-ribosylaspartate] hydrolase AF_1521 {ECO:0000305};
DE EC=3.2.2.- {ECO:0000269|PubMed:23474714};
DE AltName: Full=[Protein ADP-ribosylglutamate] hydrolase AF_1521 {ECO:0000305};
DE EC=3.2.2.- {ECO:0000269|PubMed:23474712, ECO:0000269|PubMed:23474714};
GN OrderedLocusNames=AF_1521;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23474714; DOI=10.1038/nsmb.2521;
RA Rosenthal F., Feijs K.L., Frugier E., Bonalli M., Forst A.H., Imhof R.,
RA Winkler H.C., Fischer D., Caflisch A., Hassa P.O., Luescher B.,
RA Hottiger M.O.;
RT "Macrodomain-containing proteins are new mono-ADP-ribosylhydrolases.";
RL Nat. Struct. Mol. Biol. 20:502-507(2013).
RN [3]
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).
RN [4]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLY-41 AND GLY-42.
RX PubMed=31599159; DOI=10.1021/acschembio.9b00429;
RA Stevens L.A., Kato J., Kasamatsu A., Oda H., Lee D.Y., Moss J.;
RT "The ARH and Macrodomain Families of alpha-ADP-ribose-acceptor Hydrolases
RT Catalyze alpha-NAD+ Hydrolysis.";
RL ACS Chem. Biol. 14:2576-2584(2019).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=12842467; DOI=10.1016/s0022-2836(03)00473-x;
RA Allen M.D., Buckle A.M., Cordell S.C., Lowe J., Bycroft M.;
RT "The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with
RT homology to the non-histone domain of macroH2A.";
RL J. Mol. Biol. 330:503-511(2003).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH ADP-RIBOSE, FUNCTION,
RP AND MUTAGENESIS OF ASP-20.
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 [7]
RP X-RAY CRYSTALLOGRAPHY (1.34 ANGSTROMS).
RX PubMed=16021622; DOI=10.1002/prot.20541;
RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G.,
RA Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S.,
RA Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D.,
RA Hendle J., Huber A., Hoda K., Kearins P., Kissinger C., Laubert B.,
RA Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M.,
RA Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M.,
RA Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S.,
RA Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J.,
RA Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.R.;
RT "Structural analysis of a set of proteins resulting from a bacterial
RT genomics project.";
RL Proteins 60:787-796(2005).
CC -!- FUNCTION: Removes ADP-ribose from aspartate and glutamate residues in
CC proteins bearing a single ADP-ribose moiety (PubMed:23474714,
CC PubMed:23474712). Inactive towards proteins bearing poly-ADP-ribose
CC (PubMed:23474714, PubMed:23474712). Catalyzes removal of a phosphate
CC group from ADP-ribose 1''-phosphate (Appr1p), but with low efficiency
CC (PubMed:15902274). {ECO:0000269|PubMed:15902274,
CC ECO:0000269|PubMed:23474712, ECO:0000269|PubMed:23474714}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + H2O = ADP-D-ribose
CC + H(+) + L-glutamyl-[protein]; Xref=Rhea:RHEA:58248, Rhea:RHEA-
CC COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:57967,
CC ChEBI:CHEBI:142540; Evidence={ECO:0000269|PubMed:23474712,
CC ECO:0000269|PubMed:23474714};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58249;
CC Evidence={ECO:0000269|PubMed:23474712, ECO:0000269|PubMed:23474714};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose
CC + H(+) + L-aspartyl-[protein]; Xref=Rhea:RHEA:54428, Rhea:RHEA-
CC COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29961, ChEBI:CHEBI:57967,
CC ChEBI:CHEBI:138102; Evidence={ECO:0000269|PubMed:23474714};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54429;
CC Evidence={ECO:0000269|PubMed:23474714};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-NAD(+) + H2O = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:68792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57967, ChEBI:CHEBI:77017;
CC Evidence={ECO:0000269|PubMed:31599159};
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB89725.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000782; AAB89725.1; ALT_INIT; Genomic_DNA.
DR PIR; H69439; H69439.
DR RefSeq; WP_048064404.1; NC_000917.1.
DR PDB; 1HJZ; X-ray; 1.70 A; A/B=1-192.
DR PDB; 1VHU; X-ray; 1.34 A; A=1-192.
DR PDB; 2BFQ; X-ray; 1.50 A; A=1-192.
DR PDB; 2BFR; X-ray; 2.50 A; A=1-192.
DR PDB; 6FX7; X-ray; 1.82 A; A=1-192.
DR PDBsum; 1HJZ; -.
DR PDBsum; 1VHU; -.
DR PDBsum; 2BFQ; -.
DR PDBsum; 2BFR; -.
DR PDBsum; 6FX7; -.
DR AlphaFoldDB; O28751; -.
DR SMR; O28751; -.
DR STRING; 224325.AF_1521; -.
DR PRIDE; O28751; -.
DR DNASU; 1484749; -.
DR EnsemblBacteria; AAB89725; AAB89725; AF_1521.
DR GeneID; 1484749; -.
DR GeneID; 24795270; -.
DR KEGG; afu:AF_1521; -.
DR eggNOG; arCOG04225; Archaea.
DR HOGENOM; CLU_046550_5_1_2; -.
DR OMA; HYGKGLP; -.
DR OrthoDB; 78043at2157; -.
DR PhylomeDB; O28751; -.
DR EvolutionaryTrace; O28751; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0140293; F:ADP-ribosylglutamate hydrolase activity; IDA:UniProtKB.
DR GO; GO:0140291; P:peptidyl-glutamate ADP-deribosylation; IDA:UniProtKB.
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..192
FT /note="ADP-ribose glycohydrolase AF_1521"
FT /id="PRO_0000089227"
FT DOMAIN 1..192
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT BINDING 19..21
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15902274"
FT BINDING 32..34
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15902274"
FT BINDING 39..44
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15902274"
FT BINDING 140..146
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15902274"
FT MUTAGEN 20
FT /note="D->A: Strongly reduced affinity for ADP-ribose."
FT /evidence="ECO:0000269|PubMed:15902274"
FT MUTAGEN 41
FT /note="G->D: Abolishes hydrolase activity."
FT /evidence="ECO:0000269|PubMed:31599159"
FT MUTAGEN 42
FT /note="G->D: Abolishes hydrolase activity."
FT /evidence="ECO:0000269|PubMed:31599159"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:1VHU"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:1VHU"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:1VHU"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:1VHU"
FT HELIX 42..52
FT /evidence="ECO:0007829|PDB:1VHU"
FT HELIX 55..70
FT /evidence="ECO:0007829|PDB:1VHU"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1VHU"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:1VHU"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:1VHU"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:1VHU"
FT HELIX 110..130
FT /evidence="ECO:0007829|PDB:1VHU"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:1VHU"
FT HELIX 149..162
FT /evidence="ECO:0007829|PDB:1VHU"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:1VHU"
FT HELIX 178..191
FT /evidence="ECO:0007829|PDB:1VHU"
SQ SEQUENCE 192 AA; 20956 MW; 8C3A2FE26FE52311 CRC64;
MEVLFEAKVG DITLKLAQGD ITQYPAKAIV NAANKRLEHG GGVAYAIAKA CAGDAGLYTE
ISKKAMREQF GRDYIDHGEV VVTPAMNLEE RGIKYVFHTV GPICSGMWSE ELKEKLYKAF
LGPLEKAEEM GVESIAFPAV SAGIYGCDLE KVVETFLEAV KNFKGSAVKE VALVIYDRKS
AEVALKVFER SL
