ID A0A1M4UA11_9BACT Unreviewed; 1088 AA.
AC A0A1M4UA11;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN05444274_101617 {ECO:0000313|EMBL:SHE53403.1};
OS Mariniphaga anaerophila.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Mariniphaga.
OX NCBI_TaxID=1484053 {ECO:0000313|EMBL:SHE53403.1, ECO:0000313|Proteomes:UP000184164};
RN [1] {ECO:0000313|EMBL:SHE53403.1, ECO:0000313|Proteomes:UP000184164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26910 {ECO:0000313|EMBL:SHE53403.1,
RC ECO:0000313|Proteomes:UP000184164};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQUM01000001; SHE53403.1; -; Genomic_DNA.
DR RefSeq; WP_072998753.1; NZ_FQUM01000001.1.
DR AlphaFoldDB; A0A1M4UA11; -.
DR STRING; 1484053.SAMN05444274_101617; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000184164; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000184164}.
FT DOMAIN 763..1052
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1088 AA; 124057 MW; CAE74CFD0B1AD85C CRC64;
MKTYTLLLAL IAIIALSSCK QYKKYKDVPF TEPNPKPWED PTVFAINKEA PHAHFIPFTS
AEQARAGNKW QSPLLKSLNG TWQFHLSQNP SERPFWFFQD DFDTRDWDEI AVPANWEVVG
FDYPIYTNVK YPHAKTPPLI QEHYNPVGSY KRTFEVPQEW NGSDVILHFG AVSSSMNLWV
NEQFVGYSED SKTPAEFNIT KYLVEGSNTL AVEVFRWSDA SYLEDQDFWR LSGITRDVYL
QARGKQALKD FQVGSNLDES YKNGLFSLDV EVVNQGSLTV EAVLSDNGKV TKKYSKTSND
KTLSFDAEIP NVKQWSAEVP NLYELIITLK NGNEILEVIK QDVGFRRIEI IDATLRVNGK
YVYVKGVNLH EHHDVNGHVM DRETMMKDIK TMKEHNINAV RTSHYPQPAE WYELCNKYGL
YLVDEANIES HGFGAVHQGD FDKSKHVAYL PEWADAHLYR INNVLQRDKN QPSIIAWSMG
NECGNGKVFF DGYKMLKEKD PSRLVQFEQA ESAENSDIKC PMYWRIPQMI KFAEETPVQP
LIQCEYAHAM GNSVGNFQDY WDVIEKYDIM QGGFIWDWVD QGLLTTNEAG EEFWAYGGDF
GPDTVPSDGN FCNNGLVNPD RAVKPHLLEV KKVYQHIGFK AVDLSKGLIS IKNKYAFLNT
SVFNFIWEVT GDGKTIDKGQ LKKTDLAPGE TKNFDIDFSY QPEAGVEYFL TLKAVLKEDL
NLVEAGWTLA EEQFRLPFKA AKTKRSKANL PEIKLSENDK TIAILGEGFS LAFNKKSGEM
SSFKKGETEM LISGPVPNFW RAPIDNDFGN DLHNRSRVWR KAGENRKVST VSVQKINKGT
AKITLLFDLV DAEGTKIADY KSTYTIYGSG DVLVENGFKM TGDKLPEIVR MGMNLVMPRK
FDQMTWFGRG PHESYNDRKT SAFVGLYSGS VAGQYWAYLR PQENGNKTDV RWLTITDKEG
NGLFFSGMPL SEVSAHHNIM EDFESLERTD GRQVPGIDVI NRHTTDVKPR ELTTVNIDYM
QMGVGGDDSW GGVTHDKYRL TEKEYKYSYR IKAISSADDV LDIYKNGHLF LQDHDSEVHI
KNLKIKEL
//
