ID K8XXS0_RHOOP Unreviewed; 692 AA.
AC K8XXS0;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=WSS_A14494 {ECO:0000313|EMBL:EKT81985.1};
OS Rhodococcus opacus M213.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1129896 {ECO:0000313|EMBL:EKT81985.1, ECO:0000313|Proteomes:UP000005951};
RN [1] {ECO:0000313|EMBL:EKT81985.1, ECO:0000313|Proteomes:UP000005951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M213 {ECO:0000313|EMBL:EKT81985.1,
RC ECO:0000313|Proteomes:UP000005951};
RX PubMed=23409266;
RA Pathak A., Green S.J., Ogram A., Chauhan A.;
RT "Draft Genome Sequence of Rhodococcus opacus Strain M213 Shows a Diverse
RT Catabolic Potential.";
RL Genome Announc. 1:E00144-12(2013).
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:EKT81985.1}.
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DR EMBL; AJYC02000044; EKT81985.1; -; Genomic_DNA.
DR RefSeq; WP_005256765.1; NZ_AJYC02000044.1.
DR AlphaFoldDB; K8XXS0; -.
DR Proteomes; UP000005951; 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 Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 24..403
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 414..614
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 623..678
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 160
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 326
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 692 AA; 76231 MW; 40EF80FC877D4A4B CRC64;
MHTASDSGGR HLRWPTRGIS FGGDYNPEQW PEEVWQRDVE LMREACVDFA TVGVFSWARL
QPTPDTWDFG WLDRVLDLLH DGGVRVDLAT ATASPPPWLT TAHPEVRPVD ERGYRYEIGS
RQTWSPSSPI YRDHSLVLVE KMATRYGGHP ALALWHVSNE LGCHNSRCYS PDSARAFRRW
LQRRYGDLTE LNRAWGTTFW SQHYSDWNEV VPPAASTTFG NPTHLLDWRR FCSDALLDQY
LAEREVLRRI TPDIPVTTNF MVGMGSPQSL AGDMNYAQWA PEQDLVSTDH YLVGPATGDG
AAHHRLSFSA DLTRGIAGSR PWLLMEHSTS AVNWQPVNRA KAPGEMLRNS LAHVARGADG
IAFFQFRASD AGAEKFHSAL VPHAGTDSAR WREVVQLGAV LRRLEPVAGS RVEAPVGVLF
DWESQWACEQ DGHPSRLMQP MAIAERAHHA FSGVTCDVIP ADADLSGYAV VVVPAVYLCS
DEDAARIEAA ARAGAQVLVT AFSGIADRDD HVRLGGYPGA FRDLLGVRTE EFFPLGADET
VALDDGTAAR IWTEYLTVSE DVEVLARHTE GHLQGVPALT RRPVGDGAAW YLATVPDTQS
WTRIAEAICA AAGLDLHAGQ HADVEIVRRR GENGSWLFVL NHTTEKVTVE VSGTDLVTER
VVDGPLTLEP GSCAVIREDS ADTGARTRKA DA
//
