ID A0A1I0QW98_9EURY Unreviewed; 1588 AA.
AC A0A1I0QW98;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN ORFNames=SAMN05216285_4019 {ECO:0000313|EMBL:SEW31585.1};
OS Natrinema salifodinae.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1202768 {ECO:0000313|EMBL:SEW31585.1, ECO:0000313|Proteomes:UP000183275};
RN [1] {ECO:0000313|Proteomes:UP000183275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12284 {ECO:0000313|Proteomes:UP000183275};
RA Varghese N.;
RL Submitted (OCT-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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; FOIS01000005; SEW31585.1; -; Genomic_DNA.
DR STRING; 1202768.SAMN05216285_4019; -.
DR eggNOG; arCOG07337; Archaea.
DR eggNOG; arCOG07813; Archaea.
DR OrthoDB; 38162at2157; -.
DR Proteomes; UP000183275; 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:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.70.98.10; -; 2.
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; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
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 InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 2.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 2.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF16353; LacZ_4; 1.
DR Pfam; PF13385; Laminin_G_3; 2.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SMART; SM00560; LamGL; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000183275};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 738..864
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
FT DOMAIN 1080..1568
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT DOMAIN 1227..1358
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
FT REGION 337..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1588 AA; 173335 MW; 0FF5D5B57D2E6931 CRC64;
MTQKRGGEAG RAVSTSLAPS RREFLAATGL AALVPAVAGK SVGAPDTGDG SSPGRIRNLS
AYLEDPSVFA ENGEPTHVTT AIPYESVGTA RRADEPFTEL ESRFEHSPYF RSLNGEWDFR
FYERPSDVPE SYDGVTDWDS ISVPSVWQTE GYDQRLYMNT AITWDHYDPS QEGDLVPDED
GLVDVPGVGD DGANPVGTYR RTFTVPSEWD GREVFLHFEG AKQAYFVWID GEYVGFQQGA
MTPGEFDVTD HVSPGEESRV TVQVYRWSDG EALETIDMFR YSGIHRSVYL YSTPQVHLRD
FDVRTALDEN YEDAALSVDV ELANYTDDER GEYTVTGHLF SPDWADPRRG PPGDRGEPTR
DDPPHGRKVA TVSASETVGG DGAVLALEAD VENPAKWSAE HPVLYTLVLE LAADGETTEV
MLEKVGFREY ETTRGDQGAV ITVNGEPVNV KGVNRHETDP DAGRTVPIET LREDLETMKR
FNVNAIRTSH YPNDPSLYRL ADEYGIYVQD EVYVESHWWE GLVANTEAYH DQAVERFRRM
ILRDRNHASV FSWSTGNEAG TGAEHINMAA LAMDDDEYLP PDTADVSGVE SVESYSGPVE
GLAPDRLMYH QPNGGGWNVE YSDMLGPRYP SVGTLLRTAD GSHIGDGLRS VVMGEYNHAM
GNSLGLVNEM WSGHIMPPVR RATNRADDDG HGALVGSPDV VPGPDAAPGG STDGAVVLDG
SGDYLDVRNA PAHDGTSPGF TVDLTVRDLD ASEHSPLVTG GERYALRVAD GSIAFAIDGD
GETVTAPVPD GLNDDEWHTI VAVCGADELR LSVDGEELAS ETHATDEIAG GDTRVTIGAD
AESNAYASVT IDSVGIYDRA VDADEAAAAD GSSGEGAVLR YDFADLLRDE SLQGGFVWDW
VNQDLNDVTA DGEAYQFYHN DGPDGAFSLN GLLWSDRRPQ PELWQLKHSH QPVGVADADV
ADGQIYVTNQ YDFTSLDALD GSWELVADDE TVQSGDLDLA LPPGESRCVS VPLDEPDDVE
PGTEYRLNLS FTLPEGTEYA DAGHEVAVEQ LDVPFDAPDP EPVDPDEMPP LTVSEGDDVV
VSGEGFEYTF DTDLGTLSSM RYDGTEVLER GPLFNAWRAP IMNEVQQWGS APAYSWYDAG
LDDLTHSVES IDVRQSDDST VRVDVESFVE GTVTDEQLTP DATEFGNDGY LRNEPSIVEG
VSGTAVEFGG DSSLAFERSE SLDITEAGLT LECWVRPGEP QDGGDAQTYI SKGGRQYLLK
RRRADRDGYL EFVFNADGGW QVADAPVPDD WTEGWHHLAG VWDGTEMRLY IDGEQQGSSA
AFDGSLTHVD VPTEVAPGVA DGTAMDNVRI YDRALSPDEL ETLADEPIDG AVAWLNLDEF
EDAGQEGPGF ETSYRYRVYG SGDVALEVET DPNGELRSTV EGWLPKVSVQ LELPERFDEF
EWYGRGAIET YPDRKWGVPV GRYAGSVDEQ YVPYLPPTDN GNKADTRWAT LSDGDVGLLG
VAGDTTMNVS LEQWANLDEA DHQYELEDRG SVGFNLDHAV TGVGGTPTDP IQRYQVEAEP
ATFRFVLRPF ATGKMDSMDL AAREFPDE
//
