ID E4MA37_9BACT Unreviewed; 375 AA.
AC E4MA37;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=HMPREF9720_2199 {ECO:0000313|EMBL:EFR58198.1};
OS Alistipes sp. HGB5.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Alistipes.
OX NCBI_TaxID=908612 {ECO:0000313|EMBL:EFR58198.1, ECO:0000313|Proteomes:UP000002960};
RN [1] {ECO:0000313|EMBL:EFR58198.1, ECO:0000313|Proteomes:UP000002960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGB5 {ECO:0000313|EMBL:EFR58198.1,
RC ECO:0000313|Proteomes:UP000002960};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (NOV-2010) 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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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:EFR58198.1}.
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DR EMBL; AENZ01000029; EFR58198.1; -; Genomic_DNA.
DR AlphaFoldDB; E4MA37; -.
DR PATRIC; fig|908612.3.peg.1003; -.
DR eggNOG; COG3250; Bacteria.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000002960; 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 Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
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; IPR014718; GH-type_carb-bd.
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; PF16353; LacZ_4; 1.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 90..355
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 375 AA; 40778 MW; 6A4B3C1096FFE5BD CRC64;
MGATLGSGTF EVPRTEAGAC TECRVGYKAP RPESGVDYWL DIVYRLKEDK PYALRGFEAG
RYQFALPAAA PVRAAAARSA VVSRTERSVT LTAGSVTATV DAATGYLSGY AVRGCELMRS
PLVPNFWRAS TDNDRRGWRT RERMGAWRTM PERLKLESLN AADGAVTAVV CGGGVRLALR
YRLAADGELA VSYDLRIADT LPEPLRIGLQ ALWSGELDRY VYCGRGPGEN YADRKEGSLF
GVYSGSTADF SPAYIYPQEC GNRCDVHYLQ LGGKGGGVVF AGRQPLCVSV WPCTQEALDA
AEHTHEIVRL DDAWLVNVDC AQAGVGGTDS WSVKSRPSEA YRLLEKHYGY EFVIAPAGTP
ADAARTSRRV AYKNE
//
