ID   LPLD_THESW              Reviewed;         465 AA.
AC   I3VRU1;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Alpha-galacturonidase;
DE            EC=3.2.1.67;
GN   OrderedLocusNames=Tsac_0200;
OS   Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis; Thermoanaerobacterium.
OX   NCBI_TaxID=1094508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8691 / JW/SL-YS485;
RA   Brown S.D., Land M.L., Herring C.D.;
RT   "Thermoanaerobacterium saccharolyticum JW/SL-YS485.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC   STRAIN=DSM 8691 / JW/SL-YS485;
RX   PubMed=23416295; DOI=10.1016/j.febslet.2013.02.004;
RA   Thompson J., Pikis A., Rich J., Hall B.G., Withers S.G.;
RT   "alpha-Galacturonidase(s): A new class of Family 4 glycoside hydrolases
RT   with strict specificity and a unique CHEV active site motif.";
RL   FEBS Lett. 587:799-803(2013).
CC   -!- FUNCTION: Alpha-galacturonidase able to catalyze the hydrolysis of the
CC       chromogenic substrate p-nitrophenyl-alpha-D-galacturonic acid
CC       (pNPalphaGalUA). It is probable that alpha-1,4-di-galacturonate
CC       (GalUA(2)) is the naturally occurring substrate.
CC       {ECO:0000269|PubMed:23416295}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-galacturonosyl](n) + H2O = [(1->4)-alpha-D-
CC         galacturonosyl](n-1) + alpha-D-galacturonate; Xref=Rhea:RHEA:14117,
CC         Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14572, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:58658, ChEBI:CHEBI:140523; EC=3.2.1.67;
CC         Evidence={ECO:0000269|PubMed:23416295};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000305|PubMed:23416295};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000305|PubMed:23416295};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000305|PubMed:23416295};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family. {ECO:0000305}.
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DR   EMBL; CP003184; AFK85236.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3VRU1; -.
DR   SMR; I3VRU1; -.
DR   STRING; 1094508.Tsac_0200; -.
DR   CAZy; GH4; Glycoside Hydrolase Family 4.
DR   EnsemblBacteria; AFK85236; AFK85236; Tsac_0200.
DR   KEGG; tsh:Tsac_0200; -.
DR   PATRIC; fig|1094508.3.peg.200; -.
DR   eggNOG; COG1486; Bacteria.
DR   OMA; EMYSDVH; -.
DR   BioCyc; TSAC1094508:GLMA-202-MON; -.
DR   Proteomes; UP000006178; Chromosome.
DR   GO; GO:0047911; F:galacturan 1,4-alpha-galacturonidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001088; Glyco_hydro_4.
DR   InterPro; IPR022616; Glyco_hydro_4_C.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR32092; PTHR32092; 1.
DR   Pfam; PF02056; Glyco_hydro_4; 1.
DR   Pfam; PF11975; Glyco_hydro_4C; 1.
DR   PRINTS; PR00732; GLHYDRLASE4.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase; Manganese; Metal-binding;
KW   NAD.
FT   CHAIN           1..465
FT                   /note="Alpha-galacturonidase"
FT                   /id="PRO_0000422163"
FT   ACT_SITE        180
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         11..78
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         216
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   465 AA;  52826 MW;  EB3DC69C66A9CE3C CRC64;
     MRYTDGKVHD ITIAYIGGGS RGWAWNLMTD LAKEESISGT VKLYDIDYDA AHDNEIIGNA
     LSMRQDVKGK WLYKACETLE ESLKGADFVI ISILPGTFDE MESDVHAPEK YGIYQSVGDT
     VGPGGIVRAL RTIPMFVDIA NAIKEHCPDA WVINYTNPMT LCVRTLYEIF PQIKAFGCCH
     EVFGTQKLLS RALQDIEGIE NVPREEIKIN VLGINHFTWI DNARYKDIDL MYVYKQFVNK
     YYESGFVSDA NNNWMNNSFV SAERVKFDLF LRYGVIAAAG DRHLAEFVPG YWYLKDPETV
     REWMFGLTTV SWRKEDLKRR LERSKRLKTG EEKFELKETG EEGVRQIKAL LGLGDLVTNV
     NMPNHGQIEG IPYGAVVETN ALFSGNKLKP VLSGKLPDNV NSLVLRQVYN QETTLKAALK
     RDFDLAFSAF VNDPLVTISL KDAKKLFKEM LENTKKYLDG WKIKA