ID A8F5P7_PSELT Unreviewed; 1090 AA.
AC A8F5P7;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, 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=Tlet_0915 {ECO:0000313|EMBL:ABV33481.1};
OS Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS TMO) (Thermotoga lettingae).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Pseudothermotoga.
OX NCBI_TaxID=416591 {ECO:0000313|EMBL:ABV33481.1, ECO:0000313|Proteomes:UP000002016};
RN [1] {ECO:0000313|EMBL:ABV33481.1, ECO:0000313|Proteomes:UP000002016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO
RC {ECO:0000313|Proteomes:UP000002016};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga lettingae TMO.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABV33481.1, ECO:0000313|Proteomes:UP000002016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO
RC {ECO:0000313|Proteomes:UP000002016};
RX PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA Noll K.M.;
RT "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT the Thermotogales.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
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; CP000812; ABV33481.1; -; Genomic_DNA.
DR RefSeq; WP_012002962.1; NZ_BSDV01000001.1.
DR AlphaFoldDB; A8F5P7; -.
DR STRING; 416591.Tlet_0915; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR KEGG; tle:Tlet_0915; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_0_2_0; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000002016; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
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 InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR036156; Beta-gal/glucu_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; 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 NCBIfam; NF041100; betagal_LacZ_Ttogales; 1.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 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 PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 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:UP000002016}.
FT DOMAIN 718..983
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1090 AA; 127330 MW; 6E92D508EA151569 CRC64;
MEWQDPEAVN ENIEKPHATF IPYFNPFTAC WEYPKQFIPL SGKWKFFFSN NPFDLPCNFY
DENFDDSSWD EIDVPSNWEM FGYDKPIYTN TTYPFGKNPP EISKNYNPTG IYRKTVIIPD
SWFDREIFLH FEGVRSFFYL WINGKRVGYS KDSCTPAEFR VNDYLKPGSN TLTVEVLKWC
DGSYLEDQDM WWLAGIYRDV YLYTTPRIYL RDIFVRTDLD EEFKNGKLFV DMEIKNSLAN
KIESTISISI VDPDGKESIL KEERIILSHQ LETLSYTFVL GKVFKWSVET PYLYVLKVKV
GEDEKKINTG FRKIQINHGR LLLNGKLLYI KGVNRHEFDP RRGHAVGVET MFKDIELMKQ
NNINTVRTSH YPNQTKWYDL CDYYGLYVID EANIESHGVG WDPEETLANK PEWKKAHFDR
IQRMVERDKN HISVIFWSLG NEAGDGENFE YPALWIKSRD NTRMVHYAPY GAMKPGDAFY
LDVVSVMYPP IEKLLEYASK EQSRPLIMCE YAHAMGNSVG NLRDYWQVVE NQPYLHGGCI
WDWVDQGFEK KDEAGGTFWA YGGDFGDEPN DGNFCCNGLV LPDRTPSPAL SEVKKIYQYV
KVSRINRNLF EIENRYSCTN LSAFDIFWEL KKDGKIVMSQ KIDVELPAGE RKTISINFPQ
LDNGEYFIIF LFLLKKDTVW AKKGHIVAWE QFQVKEPCYE RISIKGNINL RENSNQYIVL
SKNVAVAFSK KTGFLEYIKL GEETILCKLA PNFYRAPTDN DLGNKMPERL FVWKEATYHQ
SLQKINFQIE KNYISIASLN RLPGDSLLHL TYTVFPNNEI LIDYVLDARE SRVEIPRVGT
SFTMPKSFTK VKWYGRGPHE TYEDRKDSGI FSIHEKNVSE MIHKYIRPQE TGNRTDVRWF
SISDERSSLF VYGVPVINFS VWPFSMESLE KAQHTNELIE QDLITVNVDY KQMGVGGDDS
WGALPHPEYI LIPGIYHYEF RLLATNNTDS SEFYRRLPAF EEDYEISMSL SKQKLKVNEE
LVISVFIQNK SISTYEDDLL LFADEKLIDC QRVAVPPYET HRKDFSVKFV EKGTHLISIN
TKNKKPVYVF
//
