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Database: UniProt
Entry: A0A1D7YGR6_9ACTN
LinkDB: A0A1D7YGR6_9ACTN
Original site: A0A1D7YGR6_9ACTN 
ID   A0A1D7YGR6_9ACTN        Unreviewed;       984 AA.
AC   A0A1D7YGR6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN   ORFNames=BFF78_28950 {ECO:0000313|EMBL:AOR34539.1};
OS   Streptomyces fodineus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1904616 {ECO:0000313|EMBL:AOR34539.1, ECO:0000313|Proteomes:UP000094960};
RN   [1] {ECO:0000313|Proteomes:UP000094960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW1S1 {ECO:0000313|Proteomes:UP000094960};
RA   Kim M.-K., Kim S.B.;
RT   "Streptomyces puniciscabiei strain:TW1S1 Genome sequencing and assembly.";
RL   Submitted (SEP-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 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR   EMBL; CP017248; AOR34539.1; -; Genomic_DNA.
DR   RefSeq; WP_069781088.1; NZ_CP017248.1.
DR   AlphaFoldDB; A0A1D7YGR6; -.
DR   KEGG; spun:BFF78_28950; -.
DR   Proteomes; UP000094960; Chromosome.
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          405..576
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000259|SMART:SM01029"
FT   REGION          30..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          670..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..686
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   984 AA;  106893 MW;  76C88A0F099FAB7E CRC64;
     MALSRRNFSA LAGSTALGLA LGGSDGPGAP SAYAARSVPT GPAPAPPSAD GERHTIGYDR
     YSLLVDGRRL VVWSGEMHPF RLPSPSLWRD VLQKMRAHGY NAVSIYVAWN YHSPAPGRYD
     FTGVRDLGLF LRMAAETGLY VILRPGPYIN AEVDGGGFPG WLTATKGTAR TDDPTYLGHV
     DEWLTQVNRI ARRHLFTQGT GTILLYQIEN EYDAHPGDAT GRAYMSHLYK KVRADGIDVP
     LFHNDKGRNG YWVPGSFGTG GERGGWLYGF DGYPSPSQTP PDWGKFGPGG AHGGAGASPS
     TPGFVPEFGG GWFDPWGGAW FDGKGYAESR RTTDAAYERR FYLTNLANGL TLHNVYMTFG
     GTSWGWLPAP VVYTSYDYGA AIDEARNVTE KITPMHELGH LLQRVPDFAK LDRAADVHAE
     GLKVYHLTNP DTGAHVYVTR NDGTQAVTAD LPTAEGRLRV TVPGKDAKLF TTGLSLGRRT
     LKYANVQPVM CLNAGRQDIA VFAGRPGEMA ELVLKCPVEP DVMRLDPEAA WVVDNDELHV
     NAPLGLGGLT RVLVQKGETG TPLLLLFADD GTAARLFPYD TPSGTLLVYG PALLRHVELR
     GSEVHLTGDV TQTTSVEVWG PRGIDTLVWN GRTLPTRVTM SGSLMTTGPL PAAPEVKLPE
     LGGWRMRTEN PEVGPSFDDS HWKTADKKTS FSTTPVPDGR PVLFADDYGF HYGDVWYRGT
     FTDTTGLEEV ALAYSTGTQG LLMAWLDGEP LGTHRMPVPD RNTTVRQGTW ADTAVFPIRA
     ALRSPGRHVL SVLVRRMQHD QDGKGLDTHK AARGLTAATF KGASPKVRWR IQGAAAPDPV
     RGPMNNGGLY GEREGWHLPG FRDHDWEKAT FPRAARYQGV TWYRTTFRLS VPADVDASIG
     LTLQDDPYRA YRAQIFLNGW NLGQYINGVG PQHTFVLPNG ILRTRGTNTL ALAVLSELTT
     LSGPGKVGLT LLGRASGGLP VTPV
//
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