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Database: UniProt
Entry: A0A1K1SEP7_9PSEU
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ID   A0A1K1SEP7_9PSEU        Unreviewed;       943 AA.
AC   A0A1K1SEP7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=SAMN04489730_5519 {ECO:0000313|EMBL:SFW82859.1};
OS   Amycolatopsis australiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=546364 {ECO:0000313|EMBL:SFW82859.1, ECO:0000313|Proteomes:UP000182740};
RN   [1] {ECO:0000313|EMBL:SFW82859.1, ECO:0000313|Proteomes:UP000182740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44671 {ECO:0000313|EMBL:SFW82859.1,
RC   ECO:0000313|Proteomes:UP000182740};
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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DR   EMBL; FPJG01000006; SFW82859.1; -; Genomic_DNA.
DR   RefSeq; WP_072478991.1; NZ_FPJG01000006.1.
DR   AlphaFoldDB; A0A1K1SEP7; -.
DR   STRING; 546364.SAMN04489730_5519; -.
DR   OrthoDB; 9762066at2; -.
DR   Proteomes; UP000182740; 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   943 AA;  103350 MW;  53B232C6A5FE0F94 CRC64;
     MSYVEDPGPG YGALPPRAAF TSDAPSLSLN GTWRFRLSPS VAAAPPGVEG DEFDDSAWDE
     LPVPSLWQLH GHGRPAYTNV HYPFPVDPPH VPSENPTGDH RLRFDLPADW PAGPAVLRFD
     GIDSCGRIWL NGVELGVTKG SRLPSEFEVG PLLRPRGNVL AVRVHQWSAG SYLEDQDMWW
     LSGIFRSVTL LARPAGGIGD HWIRADYDHE SGLGTVRVET GPDVVLDIPE LGVSGHPAGE
     PLALPVEPWS AETPRLYAGT LSTAAERVPV RIGFRTVTIE DGQLEVNGRR LLLRGVNRHE
     HDPRTGRVVS PETALADVLL MKRHHVNAVR TSHYPPDPAF LELCDEYGLW VIDECDLETH
     GFGPLGWDRN PSGEPMWAEA CLDRMRRTVE RDKNRPSVIL WSLGNESHTG ENLARMAAWV
     RHRDPTRPVH YEGDHDCSYV DVHSRMYATP SEVERIGQRD DANARRRELP FLLCEYGHAM
     GNGPGGLLEY RELFERYPNC QGGFVWEWID HGLVTADHFA YGGDFGEPIH DGNFVIDGLV
     FPDRTPSPGL AEYAKIIEPV RVGPDPAGIR VSNHYDFRST AHLAFTWVLE DEGTAVARGV
     LDVPVVHSGQ SVVVPRPDLP VTRGESWLTV SAVLADATAW APAGHVAGWG QLLVSPAPPR
     PSRPARGPVF RTAGRLILGD GEFDPATGAM TTFGGHAVRG PRLDVWRATT DNDRGASAGR
     PDASLWREAG LHRMQHRVIG VDADGDELVV RTRVAPPAQA FGFFADYTWT AFDDGLRLRV
     AVTPDGPVPE TIPRLGLTMA VPGTFGSAEW FGGGPGEAYP DSRQAARIGR FSSSVDGLQT
     PYVYPQENGN RIDVRWARLT DPDGRGIRID GDPRFAFTAR RWTAAELEAA RHTSDLVAGP
     WVHVTLDTAQ HGLGSASCGP GVLPPYRLVP QKTEFSLLFS TSR
//
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