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Entry: A0A3R7HK64_9ACTN
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ID   A0A3R7HK64_9ACTN        Unreviewed;       683 AA.
AC   A0A3R7HK64;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
DE            Short=Beta-gal {ECO:0000256|PIRNR:PIRNR001084};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
GN   ORFNames=DC095_013265 {ECO:0000313|EMBL:RNC73838.1}, SFRA_008875
GN   {ECO:0000313|EMBL:RKM97326.1};
OS   Streptomyces xinghaiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1038928 {ECO:0000313|EMBL:RKM97326.1, ECO:0000313|Proteomes:UP000028058};
RN   [1] {ECO:0000313|EMBL:RKM97326.1, ECO:0000313|Proteomes:UP000028058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19609 {ECO:0000313|EMBL:RKM97326.1,
RC   ECO:0000313|Proteomes:UP000028058};
RX   PubMed=25477406;
RA   Bekker O.B., Klimina K.M., Vatlin A.A., Zakharevich N.V., Kasianov A.S.,
RA   Danilenko V.N.;
RT   "Draft Genome Sequence of Streptomyces fradiae ATCC 19609, a Strain Highly
RT   Sensitive to Antibiotics.";
RL   Genome Announc. 2:0-0(2014).
RN   [2] {ECO:0000313|EMBL:RKM97326.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 19609 {ECO:0000313|EMBL:RKM97326.1};
RA   Danilenko V.N., Bekker O.B., Vatlin A.;
RT   "Genome sequencing of Streptomyces fradiae ATCC 19609.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:RNC73838.1, ECO:0000313|Proteomes:UP000245280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OlgR {ECO:0000313|EMBL:RNC73838.1,
RC   ECO:0000313|Proteomes:UP000245280};
RA   Danilenko V.N., Bekker O.B., Vatlin A.;
RT   "Genome sequencing of Streptomyces xinghaiensis (fradiae) OlgR.";
RL   Submitted (OCT-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|ARBA:ARBA00001412,
CC         ECO:0000256|PIRNR:PIRNR001084};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC       {ECO:0000256|ARBA:ARBA00005940, ECO:0000256|PIRNR:PIRNR001084}.
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:RKM97326.1}.
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DR   EMBL; JNAD02000003; RKM97326.1; -; Genomic_DNA.
DR   EMBL; QFBD02000005; RNC73838.1; -; Genomic_DNA.
DR   RefSeq; WP_043461664.1; NZ_QFBD02000005.1.
DR   AlphaFoldDB; A0A3R7HK64; -.
DR   OrthoDB; 9800974at2; -.
DR   Proteomes; UP000028058; Unassembled WGS sequence.
DR   Proteomes; UP000245280; Unassembled WGS sequence.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
DR   CDD; cd03143; A4_beta-galactosidase_middle_domain; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR013739; Beta_galactosidase_C.
DR   InterPro; IPR013738; Beta_galactosidase_Trimer.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR003476; Glyco_hydro_42.
DR   InterPro; IPR013529; Glyco_hydro_42_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1.
DR   PANTHER; PTHR36447:SF1; BETA-GALACTOSIDASE GANA; 1.
DR   Pfam; PF02449; Glyco_hydro_42; 1.
DR   Pfam; PF08533; Glyco_hydro_42C; 1.
DR   Pfam; PF08532; Glyco_hydro_42M; 1.
DR   PIRSF; PIRSF001084; B-galactosidase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR001084};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001084};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028058};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT   DOMAIN          22..392
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          403..609
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   DOMAIN          618..673
FT                   /note="Beta-galactosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08533"
FT   ACT_SITE        158
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        315
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         123
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         166
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         323
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   683 AA;  74286 MW;  D66A9D4A2852ED15 CRC64;
     MSGDALRRLS GRLGGGIAYG GDYNPEQWPR EVWDEDVRLM REAGVNLVTV GVFSWAFLEP
     RPGQYEFGLL DEIMDLLHAG GVAVDLATAT ASPPPWFSLR HPEALPVTAD GTRLWHGSRQ
     TFCPSSPAYA EAAGRLVERL AERYRDHPAL ALWHVHNEWG NHNAHCFCDT SAQAFRDWLR
     ARYGDLDGLN ETWGTAFWSQ RYGDWAEVLP PRATAAVANP TQQLDHWRFS SDALLALHRR
     EAAILRRLSP GVPLTTNLLL TLEKKVDGFS FARECDIVAV DQYLTAADPE SHIGLSLDAD
     LARGLGGGAP WLLMEHSTSA VNWQPRNIAK TPGQMRRNSL AHAARGADGI LYFQWRQSKA
     GAEKWHSAML PHGGTDTKTW REVTALGRDL AALAEVRGSR VAADVALLFD WNAWWALESD
     ATPSRDVRYL DLVRAWYEAL WSLGITCDLV HPGSDPSRYR LVLVPALCLT TDADAASLAA
     FVREGGHAAV GFFSGVVDEN DHVRLGGYPG AYRELLGVRT DEFFPLREAE SVRLSDGSAA
     TVWTELVEPR GAETVLSFAA DPASGGPVAG HPAVTRHAFG DGVSWYVATR PEADGLRELL
     GRVCREAGVT AAAEVPAGVE AVRRQGPDAT YLFLINHTAR DASVPAAGVD LLSGAAVDGR
     AEVRAGDAMV IREHRPTGTA AAE
//
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