ID   ADPRH_TREMD             Reviewed;         261 AA.
AC   Q93RG0;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Protein-ADP-ribose hydrolase {ECO:0000250|UniProtKB:P67343};
DE            Short=SpyMacroD {ECO:0000250|UniProtKB:P0DN70};
DE            EC=3.2.1.- {ECO:0000250|UniProtKB:P67343};
OS   Treponema medium.
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=58231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 700293;
RA   Fukunaga M.;
RT   "A phylogenetic analysis of a human oral spirochete Treponema medium by
RT   flagellar genes.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ADP-ribose glycohydrolase that hydrolyzes ADP-ribosyl-
CC       cysteine bonds (By similarity). Specifically reverses the SirTM-
CC       mediated mono-ADP-ribosylation, by releasing ADP-ribose from the target
CC       protein. May be involved in the modulation of the response to host-
CC       derived oxidative stress. {ECO:0000250|UniProtKB:P0DN70,
CC       ECO:0000250|UniProtKB:P67343}.
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:0000250|UniProtKB:P67343};
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DR   EMBL; AB046578; BAB62246.1; -; Genomic_DNA.
DR   RefSeq; WP_016523496.1; NZ_CP031393.1.
DR   AlphaFoldDB; Q93RG0; -.
DR   SMR; Q93RG0; -.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd02906; Macro_1; 1.
DR   Gene3D; 3.40.220.10; -; 1.
DR   InterPro; IPR035801; Macro_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   3: Inferred from homology;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..261
FT                   /note="Protein-ADP-ribose hydrolase"
FT                   /id="PRO_0000089223"
FT   DOMAIN          74..261
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
SQ   SEQUENCE   261 AA;  29093 MW;  8DD9AD791356DD04 CRC64;
     MTQKERRIFL IEYLLRENPN YHGVQIPDDE DEQKILLRSL MNVRPPQHTS KEFLRIQDNY
     LQEAIRQHGI TGLADLKPVT GRGNGDWYVW RGDITTLKVD AIVNAANSGM TGCWQPCHAC
     IDNCIHTFAG VQLRTVCAGI MQEQGHEEPT GTAKITPAFN LPCKYVLHTV GPIISGQLTD
     RDCTLLANSY TSCLNLAAEN GVKSIAFCCI STGVFRFPAQ KAAEIAVATV EDWKAKNNSA
     MKIVFNVFSE KDEALYNKLM S