ID A0A1Q5Q029_9ACTO Unreviewed; 699 AA.
AC A0A1Q5Q029;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=BSZ39_10550 {ECO:0000313|EMBL:OKL53238.1};
OS Bowdeniella nasicola.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Bowdeniella.
OX NCBI_TaxID=208480 {ECO:0000313|EMBL:OKL53238.1, ECO:0000313|Proteomes:UP000185628};
RN [1] {ECO:0000313|Proteomes:UP000185628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19116 {ECO:0000313|Proteomes:UP000185628};
RA Meng X.;
RL Submitted (DEC-2016) 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:OKL53238.1}.
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DR EMBL; MQVR01000075; OKL53238.1; -; Genomic_DNA.
DR RefSeq; WP_073717295.1; NZ_MQVR01000075.1.
DR AlphaFoldDB; A0A1Q5Q029; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000185628; 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:0005975; P:carbohydrate 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; 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; 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:UP000185628};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 9..378
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 390..620
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT ACT_SITE 145
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 300
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 699 AA; 75504 MW; ECB3AAB02DFD8AD2 CRC64;
MAGIIYGADY NPEQWNAQVR ERDVELMKEA GLSLASVGVF SWARLEIADG EFDFGWLDEV
IENLAAAGIG IDLATATASP PAWLTTAHPE ILPVTEDGVR LAHGSRQDFC PSSPVFRRYA
ARLAGKLAER YGTHPALKLW HISNEYGCHS VHCYCETSAE AFRGWLLNKY GDLESLNEAW
GTDFWSQRYT DITQVDVPRA TPTLKNPGQV ADFLAFSSDE MLACYLAEKE AIRAHSDVPV
TTNFMGLFPH ANYRDWAPHI DVISDDSYPD PATVFAAHET ALVSDLMRSL KDGQPFYLLE
QTTSAVQWRE RNVRKRPGVF ALQSLARIAR GADAICQFQW RQSVRGAETF HSAMVPHAGR
ASRTFTEVCQ LGDTLKRLGP AVGARVKTTV ALLIDWASIF HRAAAIGPGP DRGLAAISAW
HRTAFERGYP VDFVFPDSDL SAYRVIIVPE LFAMSKATAD ALTAAAEGGA QIIVTAPSAV
VDETGKAYEG GYAAIISDLL GIVVLDHHLV AEDSDQLADP RVDRISSAIT PALDQVNLET
EPSSALFRVL DRMSHPRPAL AGGIWAEEIA ISDGVEALAT FAGGDLSGLP AITYRAASGG
GGTYVATDLE SVGRAAIFQL AELRARITGE RLEMPDGVEA IRRGDVVFVL NHGDSAAQIA
GLTGHDLVSD SVVTGHLVVP PRSAAAIDVS SRRESPDLS
//
