ID LPLD_LACP7 Reviewed; 466 AA.
AC A9KTB9;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Alpha-galacturonidase;
DE EC=3.2.1.67;
GN OrderedLocusNames=Cphy_3396;
OS Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
OS (Clostridium phytofermentans).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=357809;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700394 / DSM 18823 / ISDg;
RA Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC STRAIN=ATCC 700394 / DSM 18823 / ISDg;
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; CP000885; ABX43749.1; -; Genomic_DNA.
DR RefSeq; WP_012201398.1; NC_010001.1.
DR AlphaFoldDB; A9KTB9; -.
DR SMR; A9KTB9; -.
DR STRING; 357809.Cphy_3396; -.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
DR KEGG; cpy:Cphy_3396; -.
DR eggNOG; COG1486; Bacteria.
DR HOGENOM; CLU_045951_1_1_9; -.
DR OrthoDB; 9808275at2; -.
DR Proteomes; UP000000370; 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 Gene3D; 3.90.1820.10; AglA-like glucosidase; 1.
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; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1.
DR PANTHER; PTHR32092:SF2; ALPHA-GALACTURONIDASE; 1.
DR Pfam; PF02056; Glyco_hydro_4; 1.
DR Pfam; PF11975; Glyco_hydro_4C; 1.
DR PRINTS; PR00732; GLHYDRLASE4.
DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycosidase; Hydrolase; Manganese; Metal-binding;
KW NAD; Reference proteome.
FT CHAIN 1..466
FT /note="Alpha-galacturonidase"
FT /id="PRO_0000422162"
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 466 AA; 52933 MW; 3C97B1E2C2AD40EB CRC64;
MKYNNGKVSD VKIAYIGGGS RGWAWTFMTD LAMEPNMSGK ISLYDIDQEA AKNNEIIGNM
ITRRDDTVGK WNYETANTME AALTGADFVV ISILPGTFDE MEADVHMPER LGIYQSVGDT
AGPGGMMRAL RTIPMFVTIA NAIKEYSPKA WVINYTNPMS MCVKTLYHVF PEIKAFGCCH
EVFGTQKVLK GIAEQELKID RIDRNDIHVN VLGINHFTWF NYASYQGIDL FPIYCKYIED
HFEEGFEEKD ENWANASFAC KHRVKFDLFN EFGLIAAAGD RHLTEFMPSE RYLKDKETVA
DWNFGLTTVE WRKKDLEDRL NKSHRLVSGE EEIKLEPSGE EGILLIKALC GLTRVISNVN
IPNTNLQIEN LPSTAIVETN AVFERDSIRP IMAGEMPENV VKLTMPHILN HEYIMEAALT
FDKSLVVKAF EQDPLVKDMA TKEEVEKLVE DMLDATKAYL PKEWNL
//
