ID M0BX48_9EURY Unreviewed; 996 AA.
AC M0BX48;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=C477_17505 {ECO:0000313|EMBL:ELZ15500.1};
OS Haloterrigena salina JCM 13891.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=1227488 {ECO:0000313|EMBL:ELZ15500.1, ECO:0000313|Proteomes:UP000011657};
RN [1] {ECO:0000313|EMBL:ELZ15500.1, ECO:0000313|Proteomes:UP000011657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13891 {ECO:0000313|EMBL:ELZ15500.1,
RC ECO:0000313|Proteomes:UP000011657};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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:ELZ15500.1}.
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DR EMBL; AOIS01000057; ELZ15500.1; -; Genomic_DNA.
DR AlphaFoldDB; M0BX48; -.
DR STRING; 1227488.C477_17505; -.
DR PATRIC; fig|1227488.3.peg.3510; -.
DR eggNOG; arCOG07337; Archaea.
DR eggNOG; arCOG07813; Archaea.
DR Proteomes; UP000011657; Unassembled WGS sequence.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032312; LacZ_4.
DR InterPro; IPR006558; LamG-like.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF16353; LacZ_4; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM00560; LamGL; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000011657};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 679..815
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
FT REGION 284..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 996 AA; 110928 MW; E7F11B3F97823A97 CRC64;
MLLASGGVAL LPGLAAGGRT DDPIPDRSPG DLDLEAYLEN PAMVAENQTE PHVPTIPYPS
VEAALAGDRR CASPSERRDR SPFVRSLEGE WEFVWSLTPD GSPDDFDAVN DWDQINVPSV
WQTEGYGHAM YRNVPVPMTP YEPPEVPDTI NPVGTYHRTV TVPGNWTNDR RTFLRFEGIK
SAAFVWVNGR YVGYDQGSMT PAEFDVTDAL EPGKNTVAVQ VYRWSDGTYL ENQDMWHFAG
IYRDAYLYST PQVHLRDYAV RTDVDESYED ATLTIDAEVA DLSTADADGD GRGGKKRGGE
NGKNHGRANG NGTPDSYALR AQLFDPGGDH VTTFEEDVDV PAGDSVGVTL ETDVSDPHKW
SAEHPHLYRL GLELVPSGSN RPLEAQLERV GFREYEIVDG QVRVNGTPVE FRGVNRHEHD
PVRGRTMTTE RIREDLELLK RSNVNAIRTS HYPNDPEFAA LADEYGFYVQ DEVNAETHQN
EELVNEHPEF DPSFMDRFRR MVQRDKNHPS IFTWSTGNEA GLGPAHVEMA DYATEVDDTR
FLYHQANNGG VAPFAPIIGP RYVSPDELEG FALDEDEDRP VIMGEYSHAM GNSLGLMEPF
WERIHEYDQL QGGFVWDWVD QTLYEDLTIT PDESGTGNDG ALHGNPSIVE TDRGSALALS
GLDDWVELYR DPSLDVTEPG LTVETVVKPR EPWTGADPYV TKGDTQYALQ MADEDTLEWF
VYDPDEEWVT VSAPVPDDWT GSWHHVAGVH TGAELQLYVD GELLETTEHD GEIGHARQPV
NVGRNATLHT DGYGDWLSNA VFDSVRIYDR ALSPAELASD RAADDAILDL AFEEFRDEGT
FRSYGVSPFC INGTIFADRT PQPELWELKK AHQPVGIDPI DPVAGVVEIH NRFHFTPLSA
LEATWELTDG ETVLQDGVLS LEVEPGTTRD ATVPFDEPDL EPGAEYWLTI RVTLAEDTKW
ADAGHEVAFE QFAVPFDVPE PPLKRIDSMP STSVSR
//
