ID W7YCS7_9BACT Unreviewed; 817 AA.
AC W7YCS7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:GAF02256.1};
GN ORFNames=JCM21142_3885 {ECO:0000313|EMBL:GAF02256.1};
OS Saccharicrinis fermentans DSM 9555 = JCM 21142.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC Saccharicrinis.
OX NCBI_TaxID=869213 {ECO:0000313|EMBL:GAF02256.1, ECO:0000313|Proteomes:UP000019402};
RN [1] {ECO:0000313|EMBL:GAF02256.1, ECO:0000313|Proteomes:UP000019402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 21142 {ECO:0000313|EMBL:GAF02256.1,
RC ECO:0000313|Proteomes:UP000019402};
RA Starns D., Oshima K., Suda W., Iino T., Yuki M., Inoue J., Kitamura K.,
RA Iida T., Darby A., Hattori M., Ohkuma M.;
RT "Draft Genome Sequence of Cytophaga fermentans JCM 21142T, a Facultative
RT Anaerobe Isolated from Marine Mud.";
RL Genome Announc. 2:e00206-14(2014).
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:GAF02256.1}.
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DR EMBL; BAMD01000007; GAF02256.1; -; Genomic_DNA.
DR RefSeq; WP_027470706.1; NZ_KI912107.1.
DR AlphaFoldDB; W7YCS7; -.
DR STRING; 869213.GCA_000517085_00715; -.
DR eggNOG; COG3250; Bacteria.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000019402; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000019402};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..817
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004906528"
FT DOMAIN 26..170
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 184..287
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 293..445
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 622..697
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 711..812
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
SQ SEQUENCE 817 AA; 92849 MW; 0CDC4F2D49E25ECD CRC64;
MKQIVTGLIL FLLTIGNTLS AQDQNFNKSW LFFNDKAEGA EKVQFDDSSW RKLDLPHDWA
IEGPFDSKYN ARCGGLPFHG IGWYRKHFLI PESAKGKVVR IEFEGAMYDA YVWVNGKLVG
NHPYGYIGFE FDISQYLNYG QDNIIAVRLT PQDLSSRWYP GAGIYRNTWL KIDEAVHVAH
WGTYITTPTV TDQKATVQNE TTIENKNNQE ATITVIQEYF SPEGKSVGKT EETMTIPAHS
SKVSGTWCNI KEPKRWDLAT PHLYRAVTSI EQNGKILDSY QTRFGIRHIS YNKDGFYLNG
RKIRFNGVCL HHDNGALGAA VYRRADERKL QIMKDMGVNA IRTSHNPPSK ELLELCDEMG
LLVQDEAFDV WSMPKVPNGY NVFFNEWAER DIKDMVKRDR NHPSIVMWSI GNEILEQKDK
KYGWKTAKML NDYVKEMDKT RPTTAGFNHY SGPYDNNMAQ QVDIAGMNYK PTKYGEVRDN
YPNLPIYGSE TSSCTSSRGV YHLPIEKYKT HESLHVSSYD LIGPPWAYPP DIEFHFQEQY
PHSMGEFIWT GFDYLGEPTP YGGKDNSTNG YWNGDWPVHS SYFGAVDLCG FPKDRFFLYQ
SQWTSKPMIH LLPHWNWKGM EGQNIPVYCY TNCDEAELFL NGKSMGKKVK GKDLTELKVD
FLRYEPKTFM SKYRLSWDVP YAAGELKVVG YKNGQAVQEK IIHTAGKPAK ISLSVDRKNI
DASGTDLAYV TVRIEDKNGN LCPTADNQIF FKLRGAGSLI AVDNGNQASL ESFQANHRKA
FSGMALAIIK STETAGNIQL TATSKGLKSA KVVIISK
//
