ID W7YBJ5_9BACT Unreviewed; 1035 AA.
AC W7YBJ5;
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, ECO:0000256|RuleBase:RU361154};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230, ECO:0000256|RuleBase:RU361154};
GN ORFNames=JCM21142_93741 {ECO:0000313|EMBL:GAF05018.1};
OS Saccharicrinis fermentans DSM 9555 = JCM 21142.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC Saccharicrinis.
OX NCBI_TaxID=869213 {ECO:0000313|EMBL:GAF05018.1, ECO:0000313|Proteomes:UP000019402};
RN [1] {ECO:0000313|EMBL:GAF05018.1, ECO:0000313|Proteomes:UP000019402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 21142 {ECO:0000313|EMBL:GAF05018.1,
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 ECO:0000256|RuleBase:RU361154};
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, ECO:0000256|RuleBase:RU361154}.
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:GAF05018.1}.
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DR EMBL; BAMD01000064; GAF05018.1; -; Genomic_DNA.
DR RefSeq; WP_027470807.1; NZ_KI912107.1.
DR AlphaFoldDB; W7YBJ5; -.
DR STRING; 869213.GCA_000517085_00844; -.
DR eggNOG; COG3250; Bacteria.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000019402; Unassembled WGS sequence.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
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; 2.
DR InterPro; IPR004199; B-gal_small/dom_5.
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; IPR023230; Glyco_hydro_2_CS.
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; IPR032312; LacZ_4.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 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 Pfam; PF16353; LacZ_4; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW Reference proteome {ECO:0000313|Proteomes:UP000019402};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1035
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004904104"
FT DOMAIN 750..1026
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1035 AA; 118975 MW; AC330644E4D089AB CRC64;
MIKKIFMGAL IILSPGLFAQ KWQDPNVNAF NRAAMHSSFF AYESLEAANN SSQQSSSNYL
SLNGTWKFNW VENAWQRPTD FYKVGYNDMD WGKMPVPGIW ELNGYGDPQY VNIGYAWRSQ
YKNNPPIVPE ENNHVGTYRQ EIILPASWKG KDIVAHFGSV TSNISLYVNG KYVGYSEDSK
LEAEFNLTKY LKPGKNLIAF QVFRWCDGSY LEDQDFWRFS GVGRDCYLYA RNKTHLEDIK
VIADLDRDYK NGLLKVKLDV KGKANVNLIL SDAQGKTVVE KNVTGSGMIT TDMEVANPLK
WTAETPNLYK LTAVVKQGSK ILEVIPLKVG FRKVEKINNQ LCVNGQPILI KGVNRHELDP
DGGYVVSRER MVQDILMMKK FNVNAVRTCH YPNNNLWYDL CDEYGIYVVA EANIESHGMG
YGDATLAKNS QFAKAHMERN QRNVYRNFNH PAVIIWSMGN EAGFGGNFEA CYKWIKNYDS
SRLVQYEQAG QNDYTDIFCP MYYDYKRSEE YGQATDKTKP LIQCEYAHAM GNSEGGFKEY
WELVRKYPMY QGGFIWDFVD QSIHWKDKSG NLIYGYGGDF NPYDASDNNF LDNGLISPDR
KPNPHFYEVG YYYQSIWTKI IDVENGMIEI FNEYFFRDLS DFYLQWELVG DGKVLKTGIV
NELNVAPQQK NSIRLDLGLT DKINAKEVFI NVAYKLKSEE QGLDAGATLA RQQLVVKEYQ
FEALQIANNK YVNQKLTSPE LVENDVNYLL VLGESFQMDF NRHSGFLSRY IVDGKEVLKE
GATLKPNFWR APTDNDFGAR LQYKYAVWKN PKMDLKSLDG KLNKDGLAEI TAMYDMPEVS
AQLVLNYLIN NDGELMVKQQ LLADDNASVS DMFRFGMKLE MPGSYDFISY YGRGPGENYV
DRKDSEFVGL YQQQVHEQAY SYIRPQETGT KSDIRWWKQV DVSGFGICVN SNSTFSMSAL
NYTIDDLDDG KEKDQRHMPQ VVKSDFVTIC IDQKQMGLGC ITSWGALPRP EYRIPYQDYE
FEFVIKPVDH EFKIY
//
