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Database: UniProt
Entry: R6EWW0_9BACT
LinkDB: R6EWW0_9BACT
Original site: R6EWW0_9BACT 
ID   R6EWW0_9BACT            Unreviewed;       856 AA.
AC   R6EWW0;
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=Putative exo-poly-alpha-D-galacturonosidase {ECO:0000313|EMBL:CDA94397.1};
GN   ORFNames=BN487_00955 {ECO:0000313|EMBL:CDA94397.1};
OS   Prevotella sp. CAG:1320.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262922 {ECO:0000313|EMBL:CDA94397.1, ECO:0000313|Proteomes:UP000018111};
RN   [1] {ECO:0000313|EMBL:CDA94397.1, ECO:0000313|Proteomes:UP000018111}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:1320 {ECO:0000313|Proteomes:UP000018111};
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:CDA94397.1}.
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DR   EMBL; CBCU010000039; CDA94397.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6EWW0; -.
DR   STRING; 1262922.BN487_00955; -.
DR   Proteomes; UP000018111; 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; 1.50.10.10; -; 1.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR000743; Glyco_hydro_28.
DR   InterPro; IPR010905; Glyco_hydro_88.
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   Pfam; PF07470; Glyco_hydro_88; 1.
DR   SMART; SM00710; PbH1; 5.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 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:UP000018111};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..856
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004417216"
SQ   SEQUENCE   856 AA;  97027 MW;  C91C08A4EF5C046A CRC64;
     MRKLKTLLLA MLLPVCALAS GWDDNEYKQI EASVQQPQID TKRYPVTDYG AKTTATAAQN
     QKAINKAISA ASSKGGGQVI IPAGTWKTGA ITLRSKVNLV VEEGATLQFV FDTDLYPLVK
     TSWEGIGCWN YQPCIYANGA TDIAITGKGT INGGGSNDTW WKMCGKDRFG YVEGETKEAQ
     NLGSRARLLR YAEDGVEWDE RKFGKGQGLR PQLINFLYCD RILIKDVKLY DSPFWVIHPL
     LSKNITVDGV YIWNEGPNGD GCDPEGCENV LIQNCVFHTG DDCIAIKSGR NNDGRLWNQP
     SRNIIIRNCK MEDGHGGVVI GSEISGGCEN VYAEDCHMDS PELERVLRIK TNNCRGGLIQ
     NINMRNVTVG QCKEAVLKIN LDYEPKEECY RGFEPTVRNV SMENVTCQKS EYGVLVIGRN
     NVENVYDINV KDCEFNGVHK KPVQITGKTR DIKFDNLHIN GSLVLNEGEA PFERYSEWLA
     YSEMKRTPLS YLLDFAKKPR WSYVMGIELE GMLDTYEAYG GDSIMRYLEA YPAKMIDEKG
     NITGYKYEDF NLDNVRTAKF ILRMHNLEPA KNTEKALKTL FKQLEKQPRT KEGVYWHKAI
     YANQVWLDGI FMGLPFYTAY ATQTMKPKKA VKYLDDAVDQ IIKTDQRTYD KKTRLWKHAW
     DETREQFWAD KTTGQSQHTW ARALGWYTMA MIECLEAMPQ DYARRGEVVA LLRKAMKSVV
     DYQDPETGVW YDVMDVKDPR NYLESTASCM FAYVLLKGYR LGYLDESYRD AGVKAYQGII
     NEFIKVNDDK TISLTQCCAV SGLGPGPGPY VKKPNFKRDG SFDYYMSEPI RDNDAKGIGP
     FLWASLEMER QGLPTS
//
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