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Database: UniProt
Entry: A0A367EBX4_9ACTN
LinkDB: A0A367EBX4_9ACTN
Original site: A0A367EBX4_9ACTN 
ID   A0A367EBX4_9ACTN        Unreviewed;       610 AA.
AC   A0A367EBX4;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=DTL70_29630 {ECO:0000313|EMBL:RCG15531.1};
OS   Streptomyces diacarni.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2800381 {ECO:0000313|EMBL:RCG15531.1, ECO:0000313|Proteomes:UP000252914};
RN   [1] {ECO:0000313|EMBL:RCG15531.1, ECO:0000313|Proteomes:UP000252914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LHW51701 {ECO:0000313|EMBL:RCG15531.1,
RC   ECO:0000313|Proteomes:UP000252914};
RA   Li L.;
RT   "Streptomyces reniochalinae sp. nov. and Streptomyces diacarnus sp. nov.
RT   from marine sponges.";
RL   Submitted (JUN-2018) 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}.
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:RCG15531.1}.
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DR   EMBL; QOIN01000066; RCG15531.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367EBX4; -.
DR   OrthoDB; 9813184at2; -.
DR   Proteomes; UP000252914; 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:UP000252914}.
FT   DOMAIN          27..339
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          388..496
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          522..577
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        174
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        250
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ   SEQUENCE   610 AA;  65992 MW;  FF2ADDE9DBDB582D CRC64;
     MTPPTTGPAA SSAGRAAATL THADGRFLRG GRPHRVLSGS LHYFRVHPDH WADRLDRLAA
     LGLNTVDTYV PWNFHERHPE DIRFDGWRDL PRFVQLAQRA GLDVIVRPGP YICAEWDNGG
     LPAWLTGTPG MRPRTSHPPF LDAVGRWFDA LIPKVAALQA ARGGPVVAVQ IENEYGSYGD
     DHRYLRWVRD ALVDRGITEL LYTADGPTPL MLDGGTLPGE LTAATFGSRP ADAAALLHTR
     RQGEPFFCAE FWNGWFDHWG EKHHVRSADS AAGTVRELLD ADGSISLYMA HGGSNFGLWA
     GANHDGETFQ PTVTSYDSDA PIAEHGALTP KFHALRATLA TALGAAAPQR PLPADPPLLA
     PRTLPVSRQA ALLEALRATT DPVHAPSPLS FEELGQSAGL VLYTAHPLVP PGRQEVTVTG
     LHDRAQIFLD GVPAAVLDRE TASFTVEGTG ERTRLELLVE NQGRINYGPL LGQGKGILGG
     VRVERRLVHG WSMHRLPLDA WTSQETAHAA SAAAPGGTAG FAHAHLELVE PADTFLALPG
     FAKGFVWVNG TLLGRYWEVG PQRTLYVPGP LLRAGANTLT VLELERFGGH LALVDRPELG
     PAEQYVETFE
//
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