ID W7YMR7_9BACT Unreviewed; 991 AA.
AC W7YMR7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=JCM21142_62373 {ECO:0000313|EMBL:GAF03694.1};
OS Saccharicrinis fermentans DSM 9555 = JCM 21142.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC Saccharicrinis.
OX NCBI_TaxID=869213 {ECO:0000313|EMBL:GAF03694.1, ECO:0000313|Proteomes:UP000019402};
RN [1] {ECO:0000313|EMBL:GAF03694.1, ECO:0000313|Proteomes:UP000019402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 21142 {ECO:0000313|EMBL:GAF03694.1,
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001412};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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:GAF03694.1}.
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DR EMBL; BAMD01000028; GAF03694.1; -; Genomic_DNA.
DR RefSeq; WP_052342985.1; NZ_KI912107.1.
DR AlphaFoldDB; W7YMR7; -.
DR STRING; 869213.GCA_000517085_00870; -.
DR eggNOG; COG3250; Bacteria.
DR Proteomes; UP000019402; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 2.70.98.10; -; 1.
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; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
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 PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 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; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000019402};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 107..240
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 263..342
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 348..564
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 991 AA; 113620 MW; 5A39368B5E10FE95 CRC64;
MRALDNFYLF NMISVYMSKV CTVMVFKLIF ICLNLFFNGY MALATVNDAL VSETNSKAWF
TSQFVVCSKG DQITTDTKVK YLSGTGNDDM VEWDFYCSEG MNSGKWTKIG VPSCWEQQGF
GAYNYGSDPM EDRASEYGLY KRKFMVPKEW RDKDIDIVFE GVMTDCEVKI NGKSAGSVHQ
GAFYEFKYPI SGLLAYGTEN VLEVKVNKVS ANESVNHAER EADFWIFGGI YRPVYLTISP
KENIDRVAIN AQMNGEIFAD VWVDAKEADR LELALYDLDG QKIQDLKINS FEKSKLKWSV
SAQANHILSW NPERPHLYVL QFVLLDKDGR PLHKVSQRIG FRTVEVLEGD GIYVNGRRVK
FKGVNRHSFH PVSGRTTSKS WSIEQATMIK DMNMNAVRMA HYPPDVHFLD VCDSLGLFVI
NEICTWHNPI LDTKIARKII KETVVRDVNH PCILLWANGN EQGWNCEVDD DFSKWDIQNR
EVIHPWGVFR KTNTIHYSQY HSLVNDAYTK DKILFPTEFL HGLYDGGHGA GLQDYWEMMW
DMPLSAGGFL WDFADEGIVR TDKNGEIDLQ GNKAPDGIVG PNGEKEASYF TIKEVWSPLY
IEDRFIREDF NGLFRIENRY SYTNLGECDM TAQWVELCGP DEMAGNRLLS ETKVQLPNLA
PMSKGEFKVT MPDNWHLADV LYLKARDPYG KEIFTWSYPV ASPKRMNRKY IDYSTIGGIK
TNTSQQVIKV ETDNVSYLFS KETGLLKEVR KGDRVIPLNN GPLILNQNDE IDSLVVTTHK
DSVVIKVVFE ASEWMPVWST IREKRSDVIK CTVHTNGLLD LKVQLKGFRN LKAYRGITFS
FPESEVAGMK WLGDGPYRVW RNRMKGTRFQ VWENDYNNTV TGESGFVYPE FKGFFSNIYW
SKIKGRENNG FTVYCRTPHT YLRMLTPQNP KGDHKGRVSP LFPQGDISFV MNIPAIGTKF
QNSNTMGPHG NLEYYFGNDD APMVMDLTFQ F
//
