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 27-MAR-2024, entry version 122. DE RecName: Full=Beta-galactosidase; DE Short=Beta-gal; DE EC=3.2.1.23; GN Name=lacZ; Synonyms=lacA; OrderedLocusNames=Teth39_0611; OS Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium OS thermohydrosulfuricum). OC Bacteria; Bacillota; 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 -!- FUNCTION: Beta-galactosidase. {ECO:0000250|UniProtKB:P26257}. 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:0000250|UniProtKB:P26257}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P26257}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 KEGG; tpd:Teth39_0611; -. DR eggNOG; COG3250; Bacteria. DR HOGENOM; CLU_006501_5_1_9; -. DR Proteomes; UP000002156; Chromosome. DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1. DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1. 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; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1. DR SUPFAM; SSF49785; Galactose-binding domain-like; 1. DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 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 //