ID A0A1C2GTN6_9SPHI Unreviewed; 801 AA.
AC A0A1C2GTN6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:OCX54752.1};
GN ORFNames=BEL04_01610 {ECO:0000313|EMBL:OCX54752.1};
OS Mucilaginibacter sp. PPCGB 2223.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1886027 {ECO:0000313|EMBL:OCX54752.1, ECO:0000313|Proteomes:UP000095113};
RN [1] {ECO:0000313|EMBL:OCX54752.1, ECO:0000313|Proteomes:UP000095113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PPCGB 2223 {ECO:0000313|EMBL:OCX54752.1,
RC ECO:0000313|Proteomes:UP000095113};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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:OCX54752.1}.
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DR EMBL; MDJS01000001; OCX54752.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C2GTN6; -.
DR STRING; 1886027.BEL04_01610; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000095113; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR032311; DUF4982.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR048229; GalB-like.
DR InterPro; IPR040605; Glyco_hydro2_dom5.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR NCBIfam; NF041463; GalB; 1.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF16355; DUF4982; 1.
DR Pfam; PF18565; Glyco_hydro2_C5; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OCX54752.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095113};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..801
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008662425"
FT DOMAIN 24..175
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 186..289
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 297..564
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 622..680
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 694..795
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
SQ SEQUENCE 801 AA; 90845 MW; D769D11269C30FD2 CRC64;
MGISCLLILL TSSVTFAQHS PSQNFNQNWK FNLGDDSLAK HQAYDDSRWR KLDLPQDWSI
EGKFDEKAPG TTNEAALPTG IGWYRKTFTI PATDKGKNIY IDFDGVYRNS TVWLNGHLLG
NRPNGYISFR YDLTPYLNFG ARPNVVAVKV DNSAQPNSRW YSGSGIYRNV WLLKENPHGF
DQWDTFVTTP SINDQNATVR IVTKVNFGSL GKKLHLKITI NNESGKTVAA VKSVIPYVGL
FKAYSFREEL KVFKPILWSV KHPYLYKAVC QVLDGDKVLN AETTSFGIRF FNFDEHKGFF
LNGRSLKING VCLHHDAGAL GAVVNKHAIE RQLKILKDMG CNAIRTSHNP PAPELLDLCD
KMGFLVMDEA FDMWKKKKTQ NDYHLDWDKW HKQDLIDQIK RDRNHASVFM WSIGNEIREQ
FDTSGIRIAK ELAGIVKEYD PTRPVTSALT ETDPKKNFIY QSGALDVLGF NYHHELYPDF
PKNYPGQKFL ATETVSALET RGHYDMPSDS IRRWPHNGKD PLKDGNADLT VSAYDNISAY
WGSTHEETWK VIKKYNFLSG MFIWTGFDYL GEPTPYPWPA RSSYFGIVDL AGFPKDIYYM
YQSEWTNKPV LHIFPHWNWQ PGKVVDVWAY YSRADEVELF LNGKSLGVRH KQVDDLHVQW
RVRYEAGALK AVSRLNGKVV LTREIHTAGK PARIELITDK TKLKADGTDL SYITVRVTDA
QGNLVPDAGN QIQFEVNGPG FIAGVDNGLQ TSLEPFNSSS CKVFNGLCLA IIQSKNYKGK
VMVTASSAGL QPVTIFIDCN K
//
