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Database: UniProt
Entry: A0A1Q7VUX8_9ACTN
LinkDB: A0A1Q7VUX8_9ACTN
Original site: A0A1Q7VUX8_9ACTN 
ID   A0A1Q7VUX8_9ACTN        Unreviewed;      1008 AA.
AC   A0A1Q7VUX8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN   ORFNames=AUG49_19610 {ECO:0000313|EMBL:OLE22301.1};
OS   Catenulispora sp. 13_1_20CM_3_70_7.
OC   Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC   Catenulisporaceae; Catenulispora.
OX   NCBI_TaxID=1805055 {ECO:0000313|EMBL:OLE22301.1, ECO:0000313|Proteomes:UP000186605};
RN   [1] {ECO:0000313|EMBL:OLE22301.1, ECO:0000313|Proteomes:UP000186605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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:OLE22301.1}.
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DR   EMBL; MNJN01000305; OLE22301.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7VUX8; -.
DR   Proteomes; UP000186605; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.102.20.10; Beta-galactosidase, domain 2; 1.
DR   Gene3D; 2.60.390.10; Beta-galactosidase, domain 3; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR018954; Betagal_dom2.
DR   InterPro; IPR037110; Betagal_dom2_sf.
DR   InterPro; IPR025972; BetaGal_dom3.
DR   InterPro; IPR036833; BetaGal_dom3_sf.
DR   InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF13364; BetaGal_ABD2; 2.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF117100; Beta-galactosidase LacA, domain 3; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          402..585
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000259|SMART:SM01029"
SQ   SEQUENCE   1008 AA;  105631 MW;  D0AFA4EAC1BE50F3 CRC64;
     MPEISRRSFT TLSTGAAASL VVPLGGSGIT GPAAAAAPPI SPSALSTAAS HTVSFDKYSL
     IVDGRRLTLW SGEFHPFRLP SPSLWTDVLQ KMRANGYNAV SIYVSWNYHS AAPGLYDFTG
     VRDLDQVLTA AADVGLFVTV RPGPYINAEV DAGGFPGWMT TSSGTARTDD SAYLAHADEW
     LTAVNAIVAK HQYTNGGGTV LLYQLENEYS AHRTDGIGAS YMAHLYAKVR ADGITVPLFH
     NDKGRNGAWV PGSFGTGGET GRILYAFDGY PSPSSTPPDW GYFGTGGSTG GSTASPDTPG
     FEAEFGGGWF DCWGGAEFNG QGYAGARATR DAVYERRFYL TNLANGIKLQ NVYMTFGGTS
     WGWLPAPVVY TSYDYGAALD EARNQTSKLV PMKQIGLMLE SVPDLAQLDK AATVTASNTS
     VKTYHLTNPS TGAHFYFLRN DSSSTVSGVT LPVTTSAGTL TVPASGGGIR FTGKDMKVLA
     TGIGLGHRQL LYATAQPMYQ ATIGARDVAV FAGRNGDPAE VVLPAAQTPT VTVLAGSATS
     AYDPTNQLLR INATLSGLVS ILIAFHDGGL PLLLLLADDA ASAALWRPTA AAGPVLVRGP
     ALVRAASSCG SVVHLTGDTT TASDLEVWAP SGIAFVTWNG HAVRTSTSSS GSLLATAQLP
     GPAAVSLPAL TSWRYAAENP ESAPGFDDSG WPAADKITSG SVTPVPPGQP VLFADDYGFH
     YGDVWYRGHY SGTSEATAVS LSYSSGTQGL VMAWLDGTPL GTHRQPVPTS AQATVHTWTA
     TATFAIPAEL RGSGSHVLSV LVRPMAHSED GGGNDAHKTA RGLTAVTFSG ATPSLSWRIQ
     GGSTTADTVR GPLNTGGLYG ERNGWHLPTF SDWAWQPIQL PRADTFQGVR WYRTSFMFAP
     PPGVDASVGL TLTDTSTRAY RVQIFLNGWN LGQYINDVGP QRTFVLPNGI LHANAPNVLA
     LAVLADGTTP AGPGTVALTL LGTAAGGVPV RNLERSSGHR DRRGPHDL
//
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