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Database: UniProt
Entry: R6QR62_9BACT
LinkDB: R6QR62_9BACT
Original site: R6QR62_9BACT 
ID   R6QR62_9BACT            Unreviewed;       524 AA.
AC   R6QR62;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Exo-poly-alpha-D-galacturonosidase {ECO:0000313|EMBL:CDC24427.1};
GN   ORFNames=BN637_00072 {ECO:0000313|EMBL:CDC24427.1};
OS   Prevotella sp. CAG:386.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262925 {ECO:0000313|EMBL:CDC24427.1, ECO:0000313|Proteomes:UP000018046};
RN   [1] {ECO:0000313|EMBL:CDC24427.1, ECO:0000313|Proteomes:UP000018046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:386 {ECO:0000313|Proteomes:UP000018046};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDC24427.1}.
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DR   EMBL; CBEZ010000035; CDC24427.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6QR62; -.
DR   STRING; 1262925.BN637_00072; -.
DR   Proteomes; UP000018046; 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; 5.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   PROSITE; PS00502; POLYGALACTURONASE; 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:UP000018046};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..524
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004416719"
SQ   SEQUENCE   524 AA;  57734 MW;  45E765B0EEEF00A0 CRC64;
     MKKLFSLVCT CLLAMSMQAA ETDKYDALYE NLPFQMEKVT RPQFPANEVN LKDFGAVGDG
     STLCTEAFSK AIEALSQKGG GKLIVPQGVW FTGPITLKSN INLHIEKGGI ILFSPDDALY
     PFVKTSFEGL DTRRCQSPIS GNGLTNVAIT GQGAIDGNGE YWRPLKKQKV TDAQWKAITS
     RGGAYKRKDY WFPSEGALKA DNSANMNVPA EPTSEEGWNE IKRFLRPVMV SLVNCKNVWF
     NGVIFQNSPA WNIHPLMCEN VLIEDVLVRN PAYAQNGDGL DLESCKNALI VNSTFDVGDD
     GICIKSGKDA DGRKRGIPCE NVIVDGCTVF KGHGGFVVGS EMSGGVKNVM VTNCQFLGTD
     VGLRFKSTRG RGGVVENIFI KNMSMFDIQT DVITFDLYYG GKSAVEVLND GDEAKNQKVE
     KFKVNETTPC FRNIDIDHVI CRTARRAAYF NGLPEMPVQN ISIKDLEVNN AEQGIVINRT
     ENVKLENIKV TAKTHTFDAK NSKNVSVNSK TYKKIDEKGI TLDF
//
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