ID F4LWN5_TEPAE Unreviewed; 1825 AA.
AC F4LWN5;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00013303, ECO:0000256|RuleBase:RU361154};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230, ECO:0000256|RuleBase:RU361154};
GN OrderedLocusNames=TEPIRE1_0812 {ECO:0000313|EMBL:CDI40488.1};
OS Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1).
OC Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC Tepidanaerobacteraceae; Tepidanaerobacter.
OX NCBI_TaxID=1209989 {ECO:0000313|EMBL:CDI40488.1, ECO:0000313|Proteomes:UP000010802};
RN [1] {ECO:0000313|Proteomes:UP000010802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Re1 {ECO:0000313|Proteomes:UP000010802};
RX PubMed=23469343; DOI=10.1128/genomeA.00213-12;
RA Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.;
RT "First genome sequence of a syntrophic acetate-oxidizing bacterium,
RT Tepidanaerobacter acetatoxydans strain Re1.";
RL Genome Announc. 1:E00213-E00213(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|RuleBase:RU361154};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR EMBL; HF563609; CDI40488.1; -; Genomic_DNA.
DR RefSeq; WP_013777860.1; NC_019954.2.
DR STRING; 1209989.TepRe1_0750; -.
DR KEGG; tae:TepiRe1_0812; -.
DR KEGG; tep:TepRe1_0750; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_2_0_9; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000010802; Chromosome.
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:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR CDD; cd08547; Type_II_cohesin; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.680; -; 1.
DR Gene3D; 2.70.98.10; -; 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 Gene3D; 2.60.120.1060; NPCBM/NEW2 domain; 1.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011081; Big_4.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR002102; Cohesin_dom.
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; IPR013222; Glyco_hyd_98_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR023230; Glyco_hydro_2_CS.
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; IPR038637; NPCBM_sf.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 1.
DR Pfam; PF07532; Big_4; 1.
DR Pfam; PF00963; Cohesin; 1.
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; 1.
DR Pfam; PF08305; NPCBM; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SMART; SM00560; LamGL; 1.
DR SMART; SM00776; NPCBM; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW Reference proteome {ECO:0000313|Proteomes:UP000010802};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 639..780
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
FT DOMAIN 980..1251
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
FT DOMAIN 1351..1495
FT /note="Glycosyl hydrolase family 98 putative carbohydrate-
FT binding module"
FT /evidence="ECO:0000259|SMART:SM00776"
SQ SEQUENCE 1825 AA; 206006 MW; 19BA77C0D6CC6F92 CRC64;
MSKKLITSFV LLVFILTNLG IAAFAMPSDG IQEWNDNPTL FQVKREPAHA TFIPFADVET
ALMRDRDNSP YFKLLNGQWK FHWSKNPASR PVDFYKEDFD VSQWDEIPVP SCWQLQGYDY
PIYTNVTYPW TGYENPKPPK APTVYNPVGS YRHTFTIPED WDGREVFISF QGVESAFYLW
VNGQEVGYSE DSFTPAEFNI TEYLEQGENT IAVEVYRWSD GSWLEDQDFI RLSGIFRDVY
LYSVPKVHIR DFKVETDLDD QYKDATLNLR VDLRNLGIEN PDNYKVEAML YDADESPVLL
EPFYTTASFG EEENEVSVEL EQFIENPLKW SAEDPNLYTL VLSLKDSTDN ILETTSCRVG
FREFEIEDKQ MKINGKPIMF KGTNRHEIDP DTGRVISKER MIQDILLMKQ FNINAVRTSH
YPNDPMWYDL CDEYGLYLID EANVESHGAN GTLPKSDPNW LDACLDRMKS MVERDKNHPS
VLIWSLGNEA GSGTTFKHMA EWARQADPTR IIHYEGDNQW ADVQSNMYAR VGTVENYGKT
GTKPYILCEY AHAMGNSVGN LFKYWDVIEK YPNLQGGFIW DWVDQALRWP TPVKRIISDK
SNNKFKSEMF GELEVGRSGN ALRGYTILPD VPELNITGQG LTLEAWVKPE ASASSDNVII
AKGDSQFAIK HTANYLQQNR SVIEFYIYDA DIPGQWTQWV AAAADTPSDW FGEWHHVAGT
YDGTKLTIYI DGELKAEKET TAKITANAYP VGIGRDVERN RGFNGLIDDA RIYNRALTID
EINNHERQPD ESTVLWVDFE DVEEDGYRDS EFFAYGGDWG DNPNDGNFCA NGLIFPDRTV
QPELYEVKKV YQNIGIKAVD LENGQIEIQN KYLFTNLEEF NMSWELLEDD EIIDSGNIVI
DLAPLSSKVI TVPFETPQIK PGAEYWLNIN FTLKEDTPWA DAGHEIAKEQ FSMPFSKEPL
SLSISDMPEL ELEENDEEIL INGDKFTIVF DKSKGTMSSY VYDDKEVIKE GPIPNFWRAP
IDNDKGNGMP SRTATWRYAG ENRQISNVTV TRLADQVIQI DVDATLPTKV ESEYKATYVF
YGSGDVVVNN TLISDSSLPE IPEIGTILTL PEEFENIKWY GRGPQENYWD RNTGALVGVY
NSTVDEEFIP YLEPSETGNK TDVRWVTLTN DEGFGLLAIG MPLIEVNALH YTPEDLSTAS
HPYKLVRRDD ITLRLNYKQM GLGGDDSWGA KPHSEFTLYP GKPYSYSYRL KPITLSTQSP
MELNKEVISL DALKGINIDG KPLPSFNSQI PDYEIQILEG SRTIPPVVEP IPTSDKVQLE
VTQAETLPGT ATITATSELG VTTIYSIKFI TVPEIYLSDI DWINATCGWQ TIQRDKSVEG
NPLRLLGPSN QVITFEKGIG THADSEIIYD IEGKGYGIFE SYIGVDREIS NGSIIFEVWL
DGEKVFESDV MTARTPAQFI SIDVRGKNEL KLVAHDAGDG NAEDHADWAD AKFKKSDEEP
IAEPKITLTS PNSVQSGIEF TTKIGLSNVT EAVYAADITI NYDTNLFELI TCQTADDNTV
ISKVYEDELG SVKVSIDFKE PVTAEAIELF DIVFKAKEIT ETKSGIIGIS KALIKTTEVE
ELQVQPIEKT IEVIAEDIPE KVISSIKPVE ITTKVGEPPI LPDKVIVIYS DNSTAEVNVI
WNEINPEQYA NIGKFTVKGT VEGTDIKAVA NITVEAISEE KSFTIISGTK LDRTTGIKAK
VKVKHKTESN THPGNEVVLF QLMKGTTPIS IIALEKDIVT EEVFTAHFNV KDYESLAYKV
KVFVFDRFDS DITAPLNLAE PTELD
//
