ID F3PL08_9BACE Unreviewed; 452 AA.
AC F3PL08;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Polygalacturonase {ECO:0000313|EMBL:EGF50128.1};
GN ORFNames=HMPREF9445_02708 {ECO:0000313|EMBL:EGF50128.1};
OS Bacteroides clarus YIT 12056.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=762984 {ECO:0000313|EMBL:EGF50128.1, ECO:0000313|Proteomes:UP000010321};
RN [1] {ECO:0000313|EMBL:EGF50128.1, ECO:0000313|Proteomes:UP000010321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12056 {ECO:0000313|EMBL:EGF50128.1,
RC ECO:0000313|Proteomes:UP000010321};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2011) 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:EGF50128.1}.
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DR EMBL; AFBM01000030; EGF50128.1; -; Genomic_DNA.
DR RefSeq; WP_009122787.1; NZ_GL882598.1.
DR AlphaFoldDB; F3PL08; -.
DR STRING; 762984.SAMN05444376_0898; -.
DR GeneID; 61676717; -.
DR eggNOG; COG5434; Bacteria.
DR HOGENOM; CLU_016031_8_3_10; -.
DR OrthoDB; 9795222at2; -.
DR Proteomes; UP000010321; 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; PS51257; PROKAR_LIPOPROTEIN; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..452
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030169096"
SQ SEQUENCE 452 AA; 50220 MW; D26DC560FF7690AB CRC64;
MKKQSALWCL LLLLTIVACT ATSPRKETGE WAKVPGILKN IVPPAFADTI YDVTEYGAKD
DTAFDSRPAI LKAINQCNTD GGGTVLIPAG NYFIKGAITL KSNINLHIAE GARLEFSTEA
ADYLPMVLTK WEGTECFNYS PFIYAYQCTN VAVTGKGTID GNGSVTFNDW HAIQGPAVDR
LRQMGIDSVP VYERVFGEGH YLRPCMIQFY GCKNVLVEDL KIYDSPFWII HPVFCDNVTV
RNVYIDSNNY NNDGCDPESS TNVLIEGMDF NVGDDGIAIK SGRDQDGWRI GQATENVIIR
NCHFARWAIT IGSEMSGGVR NIYIEDCKID SCRNGIYFKS NLDRGGYFEN LNMRRIEADV
CLWGVINFRT NYHGYRGGNH PTLFRNICIE DVTCNRVDSV ALMANGLPEA KLYDITLRNI
TVKKAPKAIQ MENVVNLTLD NVTVNGKAVT AP
//