ID   LPLD_THEIA              Reviewed;         453 AA.
AC   D3T426;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Alpha-galacturonidase;
DE            EC=3.2.1.67;
GN   OrderedLocusNames=Thit_1733;
OS   Thermoanaerobacter italicus (strain DSM 9252 / Ab9).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=580331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9252 / JCM 16815 / Ab9;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Hemme C.L., Woyke T.;
RT   "Complete sequence of Thermoanaerobacter italicus Ab9.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC   STRAIN=DSM 9252 / JCM 16815 / Ab9;
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; CP001936; ADD02978.1; -; Genomic_DNA.
DR   RefSeq; WP_012995698.1; NC_013921.1.
DR   AlphaFoldDB; D3T426; -.
DR   SMR; D3T426; -.
DR   STRING; 580331.Thit_1733; -.
DR   CAZy; GH4; Glycoside Hydrolase Family 4.
DR   PRIDE; D3T426; -.
DR   EnsemblBacteria; ADD02978; ADD02978; Thit_1733.
DR   KEGG; tit:Thit_1733; -.
DR   eggNOG; COG1486; Bacteria.
DR   HOGENOM; CLU_045951_1_1_9; -.
DR   OMA; CHEVFST; -.
DR   OrthoDB; 277080at2; -.
DR   Proteomes; UP000001552; 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..453
FT                   /note="Alpha-galacturonidase"
FT                   /id="PRO_0000422164"
FT   ACT_SITE        174
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         11..72
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         209
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   453 AA;  51789 MW;  DC487F168E7F0328 CRC64;
     MKYNGDKVEG IKIAYIGGGS RGWAWRLMSD LALEQSLSGT VYLYDIDYEA AKTNEIIGNN
     LKSQWEYKSV DSMEEALKGA DFVIISILPG TFNEMMSDVH TPEKFGIYQS VGDTTGPGGL
     FRALRTIPLY VEFANKIKKY CPEAWVINYT NPMALCVKTL YETFPKIKAF GCCHEVFSTQ
     NLIAKAAKEI EGIECSREDI RTNVLGINHF TWIDKATYKN IDLIPVYKKF VEKYFESGYE
     DRGDWKESYF NSANKVKFDL FNKYGIIAAA GDRHLAEFIP FFGYLENPEA VAKWKFHLTP
     VSWRIKNREE LIKKSKKMAK GEEKFEIEPS GEEGVKQMKA LLGLGDLITN VNLPNRGQME
     GVEFNTVVET NAFFTKDRVQ PIISGKLPDT VNMLLSPHVL NQKMIFEAAI KKDKELVFHA
     FLNDPFVRKL TYSDAKKLFN EMFDNAREYL KGW