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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//