BGAL_THEP3
ID BGAL_THEP3 Reviewed; 743 AA.
AC P77989; B0K7M6;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Beta-galactosidase;
DE Short=Beta-gal;
DE EC=3.2.1.23;
DE AltName: Full=Lactase;
GN Name=lacZ; Synonyms=lacA; OrderedLocusNames=Teth39_0611;
OS Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium
OS thermohydrosulfuricum).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=340099;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Zverlov V.;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33223 / DSM 2355 / 39E;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J.,
RA Richardson P.;
RT "Complete sequence of Thermoanaerobacter pseudethanolicus 39E.";
RL Submitted (JAN-2008) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR EMBL; Y08557; CAA69850.1; -; Genomic_DNA.
DR EMBL; CP000924; ABY94275.1; -; Genomic_DNA.
DR RefSeq; WP_012269093.1; NC_010321.1.
DR AlphaFoldDB; P77989; -.
DR SMR; P77989; -.
DR STRING; 340099.Teth39_0611; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR EnsemblBacteria; ABY94275; ABY94275; Teth39_0611.
DR KEGG; tpd:Teth39_0611; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_006501_5_1_9; -.
DR OMA; YPYVGYA; -.
DR Proteomes; UP000002156; Chromosome.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProt.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR032311; DUF4982.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR040605; Glyco_hydro2_dom5.
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; IPR008964; Invasin/intimin_cell_adhesion.
DR Pfam; PF16355; DUF4982; 1.
DR Pfam; PF18565; Glyco_hydro2_C5; 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 PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF49303; SSF49303; 1.
DR SUPFAM; SSF49373; SSF49373; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..743
FT /note="Beta-galactosidase"
FT /id="PRO_0000057677"
FT ACT_SITE 388
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 453
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CONFLICT 54
FT /note="Y -> H (in Ref. 1; CAA69850)"
FT /evidence="ECO:0000305"
FT CONFLICT 84..87
FT /note="TVAK -> LLR (in Ref. 1; CAA69850)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="R -> KG (in Ref. 1; CAA69850)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="L -> M (in Ref. 1; CAA69850)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="S -> R (in Ref. 1; CAA69850)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="N -> S (in Ref. 1; CAA69850)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="A -> S (in Ref. 1; CAA69850)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="I -> V (in Ref. 1; CAA69850)"
FT /evidence="ECO:0000305"
FT CONFLICT 648..649
FT /note="SC -> TA (in Ref. 1; CAA69850)"
FT /evidence="ECO:0000305"
FT CONFLICT 652
FT /note="N -> V (in Ref. 1; CAA69850)"
FT /evidence="ECO:0000305"
FT CONFLICT 659
FT /note="A -> S (in Ref. 1; CAA69850)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 743 AA; 85765 MW; A803F29C65B73A5A CRC64;
MGRDVLNFNV DWLYIPEDLN DAYKFDFDES NFEVVSLPHA NKTFPHHYFK EEDYRFVSWY
RKHFKVDERY KGKKVYIHFE GVITVAKVYV NGEFVGEHKG GYTPFEFDIT EYIKYGNFEN
LIAVQVDSRE HKDIPPEGHL VDYMLFGGIY RNVWLKILND THIKDVYFVV DKLQDSVAEI
SITTTIAGKE ISNGKILTEV INKEGVVCSS VVTDIKEMQK EIVQQIKMDN PLTWHPDHPY
LYNVSVKLIA ENEILDNYTF KTGIRTVEFR DDGKFYINGE PLKLRGLNRH QTFPYVGGAM
PDRVQRKDAD ILKYELGLNY VRTSHYPQAV SFLDRCDEIG LLVFEEIPGW QHIGDENWKN
IAKENLKEMI LRDRNHPCIF MWGVRINESL DDHDFYKEMN EIAHKLDRSR PTGGVRYLRD
SEKLEDVFTY NDFIYNLEGK IQLPNHKKYM VTEYMGHMYP TKSYDNLNRL ITHARLHALI
QDKQYGIPNM AGASGWCAFD YNTTSAFGSG DNICYHGVCD IFRLPKFAAH FYRSQADPHL
YGPYVFIASY LIPSFEEENG DKLLVFSNCE EVELYINDKF VKRQMPNRVD FPSLPHPPFE
FSMKECGINY MEVRVNNASI TAIGLIDGKE VARHTLRPYG KPHKLILSCD DNEIMADGAD
CTRVVVSVVD ENGSILPYAN IPVSFEIEGE GKLIGENPLT LEAGRGAVYV KSTRKPGEII
LKAKSHYVAE ESNVSIKTKS IGY
