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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//