ID A0A0U3LA08_STRGL Unreviewed; 606 AA.
AC A0A0U3LA08;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN ORFNames=WQO_07800 {ECO:0000313|EMBL:ALU93260.1};
OS Streptomyces globisporus C-1027.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1172567 {ECO:0000313|EMBL:ALU93260.1, ECO:0000313|Proteomes:UP000064183};
RN [1] {ECO:0000313|EMBL:ALU93260.1, ECO:0000313|Proteomes:UP000064183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-1027 {ECO:0000313|EMBL:ALU93260.1,
RC ECO:0000313|Proteomes:UP000064183};
RX PubMed=22815456; DOI=10.1128/JB.00797-12;
RA Wang L., Wang S., He Q., Yu T., Li Q., Hong B.;
RT "Draft genome sequence of Streptomyces globisporus C-1027, which produces
RT an antitumor antibiotic consisting of a nine-membered enediyne with a
RT chromoprotein.";
RL J. Bacteriol. 194:4144-4144(2012).
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; CP013738; ALU93260.1; -; Genomic_DNA.
DR RefSeq; WP_010064479.1; NZ_CP013738.1.
DR AlphaFoldDB; A0A0U3LA08; -.
DR STRING; 1172567.WQO_07800; -.
DR KEGG; sgb:WQO_07800; -.
DR Proteomes; UP000064183; Chromosome.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; 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}.
FT DOMAIN 12..327
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 374..475
FT /note="Beta-galactosidase 1-like first all-beta"
FT /evidence="ECO:0000259|Pfam:PF21317"
FT DOMAIN 514..573
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
FT ACT_SITE 156
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT ACT_SITE 232
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ SEQUENCE 606 AA; 65724 MW; 2F0A7DE702A441A8 CRC64;
MTDFTVGDDG FRSDGKPVRL LSGALHYFRV HEEQWEHRLA MLAAMGLNCV ETYVPWNLHE
PREGEVRDVG ALGRFLDAVE RAGLWAIVRP GPYICAEWEN GGLPVWVTGR FGRRVRTRDA
EYRAVVERWF RELLPQVVQR QVVRGGPVIL VQAENEYGSF GSDAVYLEWL AGLLRECGVT
VPLFTSDGPE DHMLTGGSVP GLLATANFGS GAREGFEVLR RHQPKGPLMC MEFWCGWFDH
WGAEPVLRDA EEAAGALREI LECGASVNVY MAHGGTNFAG WAGANRGGPL QDGEFQPTVT
SYDYDAPVDE YGRATEKFHL FRKVLREYAE GPLPELPPEP KGLAVPVRAE LTGWTGLGDV
LEALGDPETE SGVPPAFEEL GVDRGLVRYR VAVPGPRQAY PLGASGLRDR AVVYVDGVRA
GVLTEESGTL PEPVAGPAEV ELWVESLGRV NYGPRLGEPK GITGGVLHER QYLHGVRARG
LRLEAFEAPG AVAALPFGPV EAAVGAGDAG RTGLFRGEFT VEGAAGLGHA GIELPGWTRG
FVWVNGFCLG RYWSAGPQRI LYVPGPVLRE GANEVWVLEL EDAGGPWVEL GPGVPVRAGT
PGVVQR
//
