ID W0JS02_9EURY Unreviewed; 646 AA.
AC W0JS02;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=HALLA_03005 {ECO:0000313|EMBL:AHG01369.1};
OS Halostagnicola larsenii XH-48.
OG Plasmid unnamed {ECO:0000313|EMBL:AHG01369.1}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halostagnicola.
OX NCBI_TaxID=797299 {ECO:0000313|EMBL:AHG01369.1, ECO:0000313|Proteomes:UP000019024};
RN [1] {ECO:0000313|EMBL:AHG01369.1, ECO:0000313|Proteomes:UP000019024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XH-48 {ECO:0000313|EMBL:AHG01369.1,
RC ECO:0000313|Proteomes:UP000019024};
RC PLASMID=1 {ECO:0000313|Proteomes:UP000019024};
RG DOE Joint Genome Institute;
RA Anderson I., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (JAN-2014) 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; CP007056; AHG01369.1; -; Genomic_DNA.
DR AlphaFoldDB; W0JS02; -.
DR KEGG; hlr:HALLA_03005; -.
DR PATRIC; fig|797299.3.peg.3115; -.
DR eggNOG; arCOG04085; Archaea.
DR HOGENOM; CLU_012430_1_0_2; -.
DR Proteomes; UP000019024; Plasmid 1.
DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
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:SF2; BETA-GALACTOSIDASE YESZ; 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.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Plasmid {ECO:0000313|EMBL:AHG01369.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019024}.
FT DOMAIN 1..364
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 371..578
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 587..631
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
SQ SEQUENCE 646 AA; 72386 MW; D654B84354635314 CRC64;
MADAGIEYVR MAEFSWRVLE PERGEFDFEW LDEIIGLIGE YGMEVVLCTP TAAPPRWLVA
ERPEILQRDR DGTVRSVGSR RHYCFNSEAY REESERVVRV LAERYADDPR VVGWQTDNEY
GCHGTTRCYC DDCASAFRSW VRQEYDSVAD LNDAWGTTFW SQQYDDFEQV DIPRPTPAQD
HPSLALDFAR FSSDSVVEYN RLQADILRGA NDDWFVTHNF MNLFESVDAY DVGEDLDLIS
WDSYPTGHVQ QAVDEASTDE LRAGNPDLLS FNHDLYRSVL DRPFWVMEQQ PGDVNWPPHS
TQPAPGAMRL WAHHATAHGA DAVVYFRWRR CLEGQEQYHA GLRKQDGSAD RGYHDATQAA
EELFDVDDVD APVALLHDYE NAWALGEQPH APDFDYWQLL QAFYGGIRSH GVQVDIVHPD
TSLESYDAVV APTVHLATAQ LADRLTAFVE SGGELLLGPR TGHKDEYGKL ASSVQPGPLT
DLVGATVDQH ESVPPQLEAT VSRTDDTQTW YAFRTWAEWL EADGAQPILE YDGDAVEDGR
TAAVRNRIGE GSVVYCGVWP EPDLAVDLVG SVLERAGVRR SAVLPGGVRV AHRGGYTWVM
NFGSDPITVD LTGEASWRLG DETIDPFDLS IADGDVVDGL SVRILE
//
