ID E5WVA5_9BACE Unreviewed; 503 AA.
AC E5WVA5;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Pectate lyase superfamily protein domain-containing protein {ECO:0000259|Pfam:PF12708};
GN ORFNames=HMPREF1016_00607 {ECO:0000313|EMBL:EFV30715.1};
OS Bacteroides eggerthii 1_2_48FAA.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=665953 {ECO:0000313|EMBL:EFV30715.1, ECO:0000313|Proteomes:UP000003246};
RN [1] {ECO:0000313|EMBL:EFV30715.1, ECO:0000313|Proteomes:UP000003246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_2_48FAA {ECO:0000313|EMBL:EFV30715.1,
RC ECO:0000313|Proteomes:UP000003246};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C.,
RA Allen-Vercoe E., Ambrose C., Strauss J., Daigneault M., Haas B.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacteroides eggerthii strain 1_2_48FAA.";
RL Submitted (OCT-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}.
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:EFV30715.1}.
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DR EMBL; ACWG01000008; EFV30715.1; -; Genomic_DNA.
DR RefSeq; WP_004293061.1; NZ_GL622539.1.
DR AlphaFoldDB; E5WVA5; -.
DR HOGENOM; CLU_011370_1_1_10; -.
DR Proteomes; UP000003246; 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; IPR024535; Pectate_lyase_SF_prot.
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; PF12708; Pectate_lyase_3; 1.
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}.
FT DOMAIN 146..189
FT /note="Pectate lyase superfamily protein"
FT /evidence="ECO:0000259|Pfam:PF12708"
SQ SEQUENCE 503 AA; 56513 MW; 91584BCCFFFC0994 CRC64;
MNKYVKTLFS IIIAGFLFIA CEPVNEPRLL PALGDEPLSK EFCVSVNGVK AAVEKMAKLD
IPIHYTQVVC NGKASMKIVV TVQEDIQSYR ISPLRKGIQG EVVGNELTFT VDGPGFFVVK
INNMEDLYLL INPFIDYQAE LKNQTFVNIK DYDIDSTGNT LCTEKIQQAI DETAKKGGVL
YFPKGIYRTG QLNMRSNLSL FLADDALLMG SVNPNDYQEK CLIRIDSVDH FRILGYGTID
GAGWSGLRKN GAREFYLVYA SNCKDIVFDG VVLRDPTFWN TRVYRSEQVH FRNLKVLNNR
PVRNWTNTDG IDFDSSKDCS LINAVIHAGD DNVVVKGLDN ERVWTTENIL FDRILTMSNS
AAAKIGTETC VKKFSNITFS NIDVMKCKRA MVINAFDSTH IEKVRFENFY IESFEFPGNE
APRLIDFEIT NKSWRECTGN STIDGVEVKN IHILSDMDGV ESQILGKDAQ YCVRNVNITG
CTVQGKPISV EGGMNLKINE FVK
//
