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Database: UniProt
Entry: D6KDT7_9ACTN
LinkDB: D6KDT7_9ACTN
Original site: D6KDT7_9ACTN 
ID   D6KDT7_9ACTN            Unreviewed;       606 AA.
AC   D6KDT7;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=SSTG_05112 {ECO:0000313|EMBL:EFF89242.2};
OS   Streptomyces sp. e14.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=645465 {ECO:0000313|EMBL:EFF89242.2, ECO:0000313|Proteomes:UP000004704};
RN   [1] {ECO:0000313|EMBL:EFF89242.2, ECO:0000313|Proteomes:UP000004704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=e14 {ECO:0000313|Proteomes:UP000004704};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Streptomyces sp. strain e14.";
RL   Submitted (OCT-2009) 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|RuleBase:RU000675};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR   EMBL; GG753627; EFF89242.2; -; Genomic_DNA.
DR   RefSeq; WP_009192330.1; NZ_GG753627.1.
DR   AlphaFoldDB; D6KDT7; -.
DR   STRING; 645465.SSTG_05112; -.
DR   eggNOG; COG1874; Bacteria.
DR   OrthoDB; 9813184at2; -.
DR   Proteomes; UP000004704; 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; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR026283; B-gal_1-like.
DR   InterPro; IPR048912; BetaGal1-like_ABD1.
DR   InterPro; IPR048913; BetaGal_gal-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF21317; BetaGal_ABD_1; 1.
DR   Pfam; PF21467; BetaGal_gal-bd; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PIRSF; PIRSF006336; B-gal; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004704}.
FT   DOMAIN          24..336
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          384..492
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          517..573
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        171
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        247
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ   SEQUENCE   606 AA;  65982 MW;  620FF604F8141627 CRC64;
     MQTTADAARD RRPAATLTHA GGTLLRAGRP HRILSGSLHY FRVHPGQWAD RLARLAALGL
     NTVDTYVPWN FHERTPGDVR FDGWRDLDRF VRLAQETGLD VIVRPGPYIC AEWDNGGLPA
     WLTGTPGMRP RTSHPPFLAA VARWFDQLIP RIAALQAGRG GPVVAVQIEN EYGSYGDDGD
     YVRWVRDALT ARGVTELLYT ADGPTELMLD AGAVEGELAA ATFGSRPEQA ARLLRSRRPE
     EPFFCAEFWN GWFDHWGEQH HVRPARSAAD DVGRILGAGG SLSLYMAHGG TNFGLWAGAN
     HDGDRLQPTV TSYDSDAPVA EHGALTEKFF ALRDELTAAG QPVPDGPPPA DPPLLPPAEL
     PVIPGAALLD ALRTVAEPVC APAPLSFEEL GQASGLVLYE AEPLLPDGEF EVTVSGLHDR
     AQVFVDGVPV AVLDRETASC RVRGTGRRVR LELLVENQGR INYGPLLGQG KGILGGVRVD
     RRLVHGWRMH RLPLDEWSPD ELSRAVSLAP ADGRAGFATA RLTVTEPADT FVALPGFGKG
     FCWVNGHLLG RYWHIGPQTT LYLPAPFLHP GDNTLTVLEL ERLGDHIALC DRPGLGEPQE
     YIETFD
//
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