ID R1FJG6_9PSEU Unreviewed; 945 AA.
AC R1FJG6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN ORFNames=H480_41460 {ECO:0000313|EMBL:EOD59702.1};
OS Amycolatopsis vancoresmycina DSM 44592.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1292037 {ECO:0000313|EMBL:EOD59702.1, ECO:0000313|Proteomes:UP000014139};
RN [1] {ECO:0000313|EMBL:EOD59702.1, ECO:0000313|Proteomes:UP000014139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44592 {ECO:0000313|EMBL:EOD59702.1,
RC ECO:0000313|Proteomes:UP000014139};
RA Kumar S., Kaur N., Kaur C., Raghava G.P.S., Mayilraj S.;
RT "Draft genome sequence of Amycolatopsis vancoresmycina strain DSM 44592T.";
RL Submitted (FEB-2013) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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:EOD59702.1}.
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DR EMBL; AOUO01000720; EOD59702.1; -; Genomic_DNA.
DR RefSeq; WP_004561777.1; NZ_AOUO01000720.1.
DR AlphaFoldDB; R1FJG6; -.
DR PATRIC; fig|1292037.4.peg.7765; -.
DR eggNOG; COG3250; Bacteria.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000014139; 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; 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; 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; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 676..940
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 945 AA; 103355 MW; 45889F33826EA3C1 CRC64;
MPYLEDPGPG RGSVPARAAF TSDAPALSLN GTWRFRLSPG LAAAPAGIEG DDFDDSAWDE
LPVPSLWQLH GHGRPAYTNV RYPFPVDPPH VPSDNPTGDH RLRFDLPADW PAGSALLRFD
GIDSCGRIWL NGTELGVTRG SRLPAEFEVG PLLRPHGNVL AVRVHQWSAG SYLEDQDMWW
LSGIFRGVTL LARPDGGIGD YWVRADYDHT TGLGTVQVET GPDVVLDIPE LEIAGHPAGE
PLALPVEPWT AETPRLYDGI LSTVAERVPV RIGFRTVSIE DGQLKVNGRR LLLRGVNRHE
HDPRTGRVVS PETALADVLL MKRHNVNAVR TSHYPPDPAF LELCDTHGLW VIDECDLETH
GFEPLGWAGN PSSDPIWADA YLDRMRRTVE RDKNRPSVIL WSLGNESHTG ENLARMADWV
RHRDPTRPIH YEGDHECAYV DVHSRMYATH EEVERIGRRE DDNARRRDLP FVLCEYGHAM
GNGPGGLLEY RELFERYPNC QGGFVWEWID HGLAADEHFA YGGDFGEPIH DGNFVIDGLL
FPDRTPSPSL AEFAKIIEPV RISAGASGIV VRNHHDFVTT AHLTFTWTLE DEGITVAQGV
LDVPSVPSGQ SVSVPLPVLP ATGGESWLTV SAALASATAW APAGHVVGWG QLPVSAAPAA
APLPPRGPVF RTGGRLVLGA GAFDPATGVL TSLGEHAVHG PRLDVWRATT DNDRGTFAGR
PDADQWREAG LHRMQHRVIA VDADGEELVV RTRVAPPALP SGLLADYTWT AFDDRLRLRV
AVTPDGEFPG TLPRLGLTMA VPGAFGAAEW FGGGPGEAYP DSRQAARIGR FSRSVDGLQT
PYVFPQENGN RTAVRWARLT APDGHGIQVD GDPVFDFTAR RWTAAELEAA RHTDDLVPGE
LVHLTLDVAQ HGLGSASCGP GVLPRYRLVP QKTEFTLWFR AVRSR
//
