ID A0A1H8BC20_9BACT Unreviewed; 491 AA.
AC A0A1H8BC20;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Polygalacturonase {ECO:0000313|EMBL:SEM80383.1};
GN ORFNames=SAMN04487902_103311 {ECO:0000313|EMBL:SEM80383.1};
OS Prevotella sp. ne3005.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1761887 {ECO:0000313|EMBL:SEM80383.1, ECO:0000313|Proteomes:UP000199132};
RN [1] {ECO:0000313|Proteomes:UP000199132}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NE3005 {ECO:0000313|Proteomes:UP000199132};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose
CC residues in alpha-D-galactosides, including galactose
CC oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC Evidence={ECO:0000256|ARBA:ARBA00001255};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing branched (1->3)-alpha-D-
CC galactosidic residues, producing free D-galactose.; EC=3.2.1.n1;
CC Evidence={ECO:0000256|ARBA:ARBA00001271};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family.
CC {ECO:0000256|ARBA:ARBA00008834, ECO:0000256|RuleBase:RU361169}.
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DR EMBL; FOCK01000003; SEM80383.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8BC20; -.
DR STRING; 1761887.SAMN04487902_103311; -.
DR OrthoDB; 9795222at2; -.
DR Proteomes; UP000199132; Unassembled WGS sequence.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR000743; Glyco_hydro_28.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR PANTHER; PTHR31339; PECTIN LYASE-RELATED; 1.
DR PANTHER; PTHR31339:SF9; PLASMIN AND FIBRONECTIN-BINDING PROTEIN A; 1.
DR Pfam; PF00295; Glyco_hydro_28; 1.
DR SMART; SM00710; PbH1; 7.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361169};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361169};
KW Reference proteome {ECO:0000313|Proteomes:UP000199132};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..491
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011445871"
SQ SEQUENCE 491 AA; 54434 MW; 2E3A6F9C90C52E1B CRC64;
MKRNLLLALS FTICLLSFSL ARAQQNVRDF GAVGDGRHID SPAINAAIQK AASNGDTVVL
PKGIWLCYSL HLESGVTLRL ENGAVLKAAP VTDTEGYDEA EHNSSSYQDF GHSHWHNSLI
WGENLHDVTL DGEGLIDGTG VLSRGEPRRN YTGKPWANKA LALRDCQRVT IRGVSFLNCG
HFAMLLTGVD DLLIENVKAD SNRDGFDIDC CERVIIRNCH VNTLNDDAIV LKCSYALGRP
KPTEHVLIEN CHVSGYDIGT YLDGTKTTNM LKAPDGDGPT GRIKLGTESN GGFRHITIRN
CTFTHCRGLA LETVDGAAME DINVSDITMT DICNSPIYIR LGDRMRAPEG FHSSTVDHIS
IRNIRVADAD SRYACLIAGV RNHPVRNVRI ENLNVQFRGG LTLDDVREQR GRNPFFIPEA
RKATERGEAN YPEPSAHGIQ PAWGFSISHA ENIYLKNIHL ETIHQDERPA FFMKETKNIR
RKKVSTLNPI K
//
