ID A0A291GUN6_9MICO Unreviewed; 1001 AA.
AC A0A291GUN6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=CFK41_03230 {ECO:0000313|EMBL:ATG53897.1};
OS Brachybacterium ginsengisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=1331682 {ECO:0000313|EMBL:ATG53897.1, ECO:0000313|Proteomes:UP000217889};
RN [1] {ECO:0000313|EMBL:ATG53897.1, ECO:0000313|Proteomes:UP000217889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCY80 {ECO:0000313|EMBL:ATG53897.1,
RC ECO:0000313|Proteomes:UP000217889};
RX PubMed=24944333; DOI=10.1099/ijs.0.058388-0;
RA Hoang V.A., Kim Y.J., Nguyen N.L., Yang D.C.;
RT "Brachybacterium ginsengisoli sp. nov., isolated from soil of a ginseng
RT field.";
RL Int. J. Syst. Evol. Microbiol. 64:3063-3068(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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR EMBL; CP023564; ATG53897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291GUN6; -.
DR KEGG; bgg:CFK41_03230; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000217889; Chromosome.
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 Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154}.
FT DOMAIN 734..997
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1001 AA; 108230 MW; E01415FA38AF6EF5 CRC64;
MSTPQQSADS RSAGIKDPTD RWWEELPAGR NRLAGRAHLR SDAPALNLDG TWDFRYGTRA
DGSDLGDAGE ITVPGLWQFQ GHGAPQYTNV IYPIPREIPH VPDENPTGHY SRTLATPAEW
AEQLAAGARV LLRFQGVDSA AKVWIDGAEV GVTAGSRLTQ EFDVTDALTT AGEHLLEVRV
VQWSVNTYVE DQDMWWASGI FRSVDLLLRP VGGIHDLVTV ADFDPATGTG SLRATAFAAD
GTELAATVEI PALGHSAATG AEAVDLGEVR PWSAEDPHLY DATISTGAET VTLRLGFRRV
EVDGEIFRVN GERIVFRGVN RHEADPLVGR TQHEGNQDLD VALMKQHNLN AVRTSHYPPH
QRFLDVCDEA GLYVICEGDF ETHGFHADET WGEDGTGAAE GPAQNPLFEA SLVERSERFV
RRDRHHASII MWSIGNEAAS GPVTEAMVAR VRETDPTRPV IYEQDYAAEY VDVFSLMYPT
VDESAQIGRR DLSPEYQDKL TRMLRSFALD VPDGHFADPP ALTKPFLWIE YAHAMGNGAG
SLKEYMALTE QHPALHGGFI WEWIDHGLET TDAEGNRIYG YGGDFGERLH DGNFVADGLV
LPDRTPSPAL LDAKHHYSPV GLEVSAGGAR ITNRYAFSDL THLRAEVSLD AQATWQEIEL
PAIAPGESGE VALPVHDGAA TTVRLTTREV QGPVPAGHLV VAADHVDAER LRAAQTPSAD
GAVAPVRAED GTWSLGPARF DDLGRLVGLG ELEIEHAGAD LYRAPVDNER ARTRAPLEAR
WKRIGLDHAR RRLAEITADG DALVVRSRLG LDGSALGADV TERWSGTADG VGVEVTVTPS
AFWPADLPLP RIGWTFALPS APDQVEYEGY GPHESYPDTG GGTTFGLWTS TLAELQVPYV
FPQENGNRAG VVSAHLRGAG GAGLEVRAPE GLGLAARPWS TAELDARAHD GALRADGRTW
VTLSSALHGV GSAACGPEPL PEYVLSAREE TFAFHLSPGT V
//
