ID A0A1J5MS85_9GAMM Unreviewed; 867 AA.
AC A0A1J5MS85;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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};
DE Flags: Fragment;
GN ORFNames=BM565_12330 {ECO:0000313|EMBL:OIQ46195.1};
OS Gammaproteobacteria bacterium MedPE.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1860093 {ECO:0000313|EMBL:OIQ46195.1, ECO:0000313|Proteomes:UP000182920};
RN [1] {ECO:0000313|EMBL:OIQ46195.1, ECO:0000313|Proteomes:UP000182920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MedPE {ECO:0000313|EMBL:OIQ46195.1};
RX PubMed=27446036; DOI=10.3389/fmicb.2016.00996;
RA Lopez-Perez M., Kimes N.E., Haro-Moreno J.M., Rodriguez-Valera F.;
RT "Not All Particles Are Equal: The Selective Enrichment of Particle-
RT Associated Bacteria from the Mediterranean Sea.";
RL Front. Microbiol. 7:996-996(2016).
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 -!- 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:OIQ46195.1}.
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; MPDF01000109; OIQ46195.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5MS85; -.
DR STRING; 1860093.BM565_12330; -.
DR Proteomes; UP000182920; 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; IPR023232; Glyco_hydro_2_AS.
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 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; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154}.
FT DOMAIN 68..234
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 237..350
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 352..636
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 647..740
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|Pfam:PF16353"
FT DOMAIN 768..863
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|Pfam:PF02929"
FT NON_TER 867
FT /evidence="ECO:0000313|EMBL:OIQ46195.1"
SQ SEQUENCE 867 AA; 99172 MW; E0AF172A5318313D CRC64;
MKIASLLFAS TVALSSQGVA KNQERQPWED HRVFAINKLP PRATSFGFEN KYAALHLTKE
QATSFMLLNG QWPFHWRKSP SDKPEGFHLP TYDASKWAQI NVPGNWEVEG FGHPIYLDER
FPFTTTWPNV PKEYNPIGSY RKHFDIPDTW KNKQIFLHVG AAKSSLDVWL NGQKVGFSQG
AKTPAEFDIT KYINKRNNLL ALQLRRWSDA SYLESQDMLR ISGIERDVYL YATPKQRIYD
IGVTTQLSDN YSKAHLSLDV SVNNYASDSA NKLVVEFELL DPSRQLQQIM TGRKTISVGK
KSQKKISLSK GFGQPRLWNA EQPNLYTLLV TLKDTDGDVL ETHRQDIGFR EVTIEDAQLK
VNGQAITIRG VDRHETSPKT GHVVSKISME QDIKLMKQFN INAVRSSHYP NNPYWYELTD
QYGMYVIDEA NIESHPLAIN AKTQIGNELS WLPAHLDRTK RMVERDKNHP SIIIWSLGNE
AGEGKVFEAT YQWIKQRDPS RPVQYEPAGE DHYTDIFAPM YPSVQRLEKY AKSKPYRPGI
MIEYAHAMGN SVGNLKDYWE VIDRYPVLQG GFIWDWVDQS LEYTDENGVK FWAYGRDFHP
TLPTDGNFLN NGLVNPNRVP HPHAFEVKKV YQPVRFTEFN AVRGTIIINN RYNFKDLSEQ
ALKWVIEADG EQIHSAVQPM PLINAQGSKE FTLNLPQLLE SDAKEYFLTI GAVTKQAQRR
GDDTILPAGH EVAVEQFKLP VTFRADKLSG ITHHVMQRND NDEIELTTGN ISYVFNRKTG
WLTQISIASE KLLTSPLKPN FWRAPTDNDL GNKMNRWGSV WQGMSKSLRL EKIDVDERAG
GVKLTMSYQS EKLAGYFSVE YFVANTG
//
