ID A0A1H1G694_9EURY Unreviewed; 676 AA.
AC A0A1H1G694;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=DWB78_16885 {ECO:0000313|EMBL:RDI69825.1}, SAMN05216278_3540
GN {ECO:0000313|EMBL:SDR08569.1};
OS Halopelagius longus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae.
OX NCBI_TaxID=1236180 {ECO:0000313|EMBL:SDR08569.1, ECO:0000313|Proteomes:UP000199289};
RN [1] {ECO:0000313|EMBL:SDR08569.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12397 {ECO:0000313|EMBL:SDR08569.1};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000199289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12397 {ECO:0000313|Proteomes:UP000199289};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RDI69825.1, ECO:0000313|Proteomes:UP000255421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC12-B1 {ECO:0000313|EMBL:RDI69825.1,
RC ECO:0000313|Proteomes:UP000255421};
RA Zhang X.;
RT "Genome sequence of extremly halophilic archaeon Halopelagius longus strain
RT BC12-B1.";
RL Submitted (JUL-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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC {ECO:0000256|ARBA:ARBA00005940}.
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DR EMBL; QQST01000003; RDI69825.1; -; Genomic_DNA.
DR EMBL; FNKQ01000005; SDR08569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1G694; -.
DR OrthoDB; 85141at2157; -.
DR Proteomes; UP000199289; Unassembled WGS sequence.
DR Proteomes; UP000255421; 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: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:SF2; BETA-GALACTOSIDASE YESZ; 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.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 6..387
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 405..610
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
SQ SEQUENCE 676 AA; 74842 MW; 18FD538B4850B65F CRC64;
MSIGVCYFPE HWPDERTEAD VERMADAGLE YVRMGEFAWS RMEPEPGAYD FEWLDRAVSR
IGDHGMQAVL CTPTAAPPKW LVDEYPGILQ EEADGTTRHY GGRRHYCYNS EEFRRESRRI
TEKLADRYAD DPTVAGWQTD NEYGCHGTLR CYCDDCASAF RDWLRETYGD IDSLNEAWGT
EFWSQTLNSF AQVDPPRHAA AGHHPSRLLD YYRFSSDSVA EYNRLQVDIL REANDEWFVT
HNFMSHDDLD AYDVAADLDF ASWDSYPTGH VQVQHEAVSD EELRAGDPDN VGLDHDLYRS
AADAPFWVME QQPGDINWPP YSPQPAEGAM RLWALYAVAR GADVVSYFRW RRCRMGQEQY
HSGLLAEDGT PDRGYGDAVA AASDLDELAS VAAGDADGSF ASPDADVALL HDYDNLWASE
IEPMTPDFDY WRHVETYYAA LRERSVHVDV VPPTAELAAY DAVVAPTLYL ATDELAETLT
AYVEGGGELL VTMRSGVKDA HNKLHDDAQP GPLRSLVGAR VEQHESVPES LESRLTYGGR
EFGCRVWNEW LSPTEEGAEV VGRYEGSMAD GSPAIVRNAV GDGSVTYVGT WPDSDLTGAV
VGDLLDRAGV ETTDAFPAQV RASRRGGLTW IANFGGDSLS VDAPDDAEWV LGGPTVGPAA
VAVTDANLSS LSPAEE
//
