ID D7K8T8_9BACE Unreviewed; 539 AA.
AC D7K8T8;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Exo-poly-alpha-D-galacturonosidase {ECO:0000313|EMBL:EFI37174.1};
GN ORFNames=HMPREF9010_02805 {ECO:0000313|EMBL:EFI37174.1};
OS Bacteroides sp. 3_1_23.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=457390 {ECO:0000313|EMBL:EFI37174.1, ECO:0000313|Proteomes:UP000003808};
RN [1] {ECO:0000313|EMBL:EFI37174.1, ECO:0000313|Proteomes:UP000003808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3_1_23 {ECO:0000313|EMBL:EFI37174.1,
RC ECO:0000313|Proteomes:UP000003808};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D.,
RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Strauss J., Daigneault M., McDonald J., Ambrose C.E.,
RA Allen-Vercoe E., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacteroides sp. strain 3_1_23.";
RL Submitted (MAR-2010) 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; GG774955; EFI37174.1; -; Genomic_DNA.
DR RefSeq; WP_008650832.1; NZ_GG774955.1.
DR AlphaFoldDB; D7K8T8; -.
DR HOGENOM; CLU_016031_8_3_10; -.
DR Proteomes; UP000003808; 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.
DR PROSITE; PS00502; POLYGALACTURONASE; 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}.
SQ SEQUENCE 539 AA; 59199 MW; F98587963348F3FC CRC64;
MNTLTKRLFW MALCCLPFIS SGCKQSETTV KESSISDALY QNLPFEMPKV QQPVFPAYEV
NIEKFGAKGD GLFLNTKAIN DAIKDVNQRG GGKVIIPEGV WLTGPIELLS NVNLYTEQNA
LVLFTGDFEA YPIIATSFEG LETRRCQSPI SARNAENIAI TGHGTFDGNG DCWRPVKKGK
LTASQWKKLV NSGGVLDEKQ EIWYPTAGSL RGAMACKDFN VPEGINTDEE WAEIRPWLRP
VLLSIVKSKK VLLEGVTFKN SPSWCLHPLS CEDFTVNNIM VINPWYSQNG DAIDLESCKN
ALIINSVFDA GDDAICIKSG KDEDGRRRGE PCQNVIVKNN TVLHGHGGFV VGSEMSGGVK
NIYVEDCTFM GTDVGLRFKS TRGRGGVVEN IYINNINMIN IPNEPLLFDL FYGGKGAGEE
SEEDLLSRMK TAIPPVTEET PAFRNIHISN IVCRGSGRAM FFNGLPEMPI SNITVKNVVM
TEAADGVVIS QVDGVTLENI YVESSKGNNI LNVKNAKNLT IDGKVYEELG AKEEILSLK
//
