ID A0A1M7L5R8_9SPHI Unreviewed; 818 AA.
AC A0A1M7L5R8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:SHM73464.1};
GN ORFNames=SAMN05216524_103208 {ECO:0000313|EMBL:SHM73464.1};
OS Mucilaginibacter sp. OK098.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1855297 {ECO:0000313|EMBL:SHM73464.1, ECO:0000313|Proteomes:UP000184158};
RN [1] {ECO:0000313|EMBL:SHM73464.1, ECO:0000313|Proteomes:UP000184158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK098 {ECO:0000313|EMBL:SHM73464.1,
RC ECO:0000313|Proteomes:UP000184158};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; FRCM01000003; SHM73464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M7L5R8; -.
DR STRING; 1855297.SAMN05216524_103208; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000184158; 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; IPR048230; GalA-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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 NCBIfam; NF041462; GalA; 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 PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..818
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012861971"
FT DOMAIN 97..224
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 229..339
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 341..487
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 642..698
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 713..813
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
SQ SEQUENCE 818 AA; 91479 MW; 4A295077170FBDFC CRC64;
MFKRLIRYCG ICFFLLLCAI KGIAQNAQQT SLSKRSKECF DFNWQFHKGD IAIKRAVKAA
GYGGLTDINV KVETNKEAVI AYTDVDKAAI FKPEDWKEVN LPHDWCVEGT FVNDKSIGSS
PAVSGYLPGG IGFYRKEFEI PETDKGKKIS VEFDGIFRNS TVWVNGQLIG NHQSGYTPSN
YDLTDVLRYG NEGKNVILVK VDATEYEGWW YEGCGIYRHV WLDKTNPVHV DRFGTYVTTS
PVSPDEAAVN IKTNIKNEYG VVKNVTLTSK IVDNKGVVLN IKTSSQAIEP FSTTEFSQKG
DIQKPLLWSP ETPNLYKVLT EVSENGIVID NYETIFGVRI IEINRNGVFL NGKLYPVKGT
CNHQDFAGIG VALPDKINEY KLKLLKEMGS NAYRCSHNPP TPELLDMCDR MGLLVLDENR
MLSSSEEGKK DLTTMLYRDR NHPSIFMWSM ENEEGIQGTV TGARILKTLV DITHKIDPTR
PVTAAMNHGR NEGGYSDVLD VVGYNYGDKG LAYVRDHEKY PRRIEFCTEA TSFISTRGEY
QNDWGKGYVS NLGLWQPNWG PLPGEDWADI VKYPYLGGLF VWTGFDYRGE PTPYQWPCLT
SHFGFMDICG FPKDGYYAYK AAWTNKPVVH IFPHWDWPGK EGDSIQVHCY TNCDEVELLL
NGKKVGTQKA VPYTKLIWKL VYKPGKLEAR GYKGGRLVTT DIVKTTTAPA QVTLSCDTSV
LKADGCDVAV IRVAIKDSKG RVNPTAANLI TFSIEGPGRI IGTGNGNPSS HEPDKASQRM
AFNGYCLVLV QSNKQAGEIR LKASSEKLKG DEVVIKVQ
//
