ID BGAL_KLULA Reviewed; 1025 AA. AC P00723; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 2. DT 27-MAR-2024, entry version 153. DE RecName: Full=Beta-galactosidase; DE Short=Beta-gal; DE EC=3.2.1.23; DE AltName: Full=Lactase; GN Name=LAC4; OrderedLocusNames=KLLA0B14883g; OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces. OX NCBI_TaxID=284590; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1511885; DOI=10.1016/0378-1119(92)90248-n; RA Poch O., L'Hote H., Dallery V., Debeaux F., Fleer R., Sodoyer R.; RT "Sequence of the Kluyveromyces lactis beta-galactosidase: comparison with RT prokaryotic enzymes and secondary structure analysis."; RL Gene 118:55-63(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / RC WM37; RX PubMed=15229592; DOI=10.1038/nature02579; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., RA Weissenbach J., Wincker P., Souciet J.-L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-119. RX PubMed=6324114; DOI=10.1093/nar/12.5.2327; RA Breunig K.D., Dahlems U., Das S., Hollenberg C.P.; RT "Analysis of a eukaryotic beta-galactosidase gene: the N-terminal end of RT the yeast Kluyveromyces lactis protein shows homology to the Escherichia RT coli lacZ gene product."; RL Nucleic Acids Res. 12:2327-2341(1984). 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}. 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; M84410; AAA35265.1; -; Genomic_DNA. DR EMBL; CR382122; CAH02587.1; -; Genomic_DNA. DR EMBL; X00430; CAA25128.1; -; Genomic_DNA. DR PIR; JC1266; JC1266. DR RefSeq; XP_452194.1; XM_452194.1. DR PDB; 3OB8; X-ray; 2.80 A; A/B/C/D=2-1025. DR PDB; 3OBA; X-ray; 2.75 A; A/B/C/D=2-1025. DR PDBsum; 3OB8; -. DR PDBsum; 3OBA; -. DR AlphaFoldDB; P00723; -. DR SMR; P00723; -. DR STRING; 284590.P00723; -. DR ChEMBL; CHEMBL3309040; -. DR CAZy; GH2; Glycoside Hydrolase Family 2. DR PaxDb; 284590-P00723; -. DR GeneID; 2897170; -. DR KEGG; kla:KLLA0_B14883g; -. DR eggNOG; KOG2024; Eukaryota. DR HOGENOM; CLU_002346_0_0_1; -. DR InParanoid; P00723; -. DR OMA; HYEADIY; -. DR BRENDA; 3.2.1.23; 2825. DR SABIO-RK; P00723; -. DR EvolutionaryTrace; P00723; -. DR Proteomes; UP000000598; Chromosome B. 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; 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 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. DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Glycosidase; Hydrolase; Reference proteome. FT CHAIN 1..1025 FT /note="Beta-galactosidase" FT /id="PRO_0000057663" FT ACT_SITE 482 FT /note="Proton donor" FT /evidence="ECO:0000250" FT ACT_SITE 551 FT /note="Nucleophile" FT /evidence="ECO:0000250" FT HELIX 7..9 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 16..18 FT /evidence="ECO:0007829|PDB:3OBA" FT TURN 29..31 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 37..46 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 47..49 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 53..55 FT /evidence="ECO:0007829|PDB:3OB8" FT HELIX 58..61 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 66..70 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 77..79 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 85..90 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 106..115 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 117..122 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 123..130 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 132..140 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 143..149 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 155..158 FT /evidence="ECO:0007829|PDB:3OBA" FT TURN 160..162 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 165..176 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 179..183 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 187..190 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 198..220 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 225..237 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 241..247 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 258..262 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 275..280 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 287..295 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 301..304 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 306..314 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 320..328 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 333..336 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 339..342 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 349..353 FT /evidence="ECO:0007829|PDB:3OBA" FT TURN 359..361 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 367..379 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 384..386 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 396..403 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 406..410 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 416..419 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 420..425 FT /evidence="ECO:0007829|PDB:3OBA" FT TURN 433..436 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 437..440 FT /evidence="ECO:0007829|PDB:3OBA" FT TURN 441..443 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 444..446 FT /evidence="ECO:0007829|PDB:3OBA" FT TURN 447..449 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 451..453 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 454..468 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 474..478 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 487..499 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 503..506 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 517..523 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 526..536 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 543..545 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 547..553 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 563..572 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 576..582 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 589..594 FT /evidence="ECO:0007829|PDB:3OBA" FT TURN 596..598 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 599..606 FT /evidence="ECO:0007829|PDB:3OBA" FT TURN 608..611 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 618..621 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 634..642 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 645..651 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 654..659 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 669..673 FT /evidence="ECO:0007829|PDB:3OBA" FT TURN 674..676 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 690..694 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 698..706 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 716..721 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 741..744 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 746..753 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 756..761 FT /evidence="ECO:0007829|PDB:3OBA" FT TURN 762..765 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 766..772 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 775..779 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 785..787 FT /evidence="ECO:0007829|PDB:3OBA" FT TURN 794..799 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 800..806 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 809..811 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 812..823 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 829..840 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 846..855 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 857..872 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 878..886 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 890..898 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 913..917 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 918..920 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 935..945 FT /evidence="ECO:0007829|PDB:3OBA" FT TURN 946..948 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 949..958 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 960..968 FT /evidence="ECO:0007829|PDB:3OBA" FT TURN 970..972 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 976..978 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 980..993 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 999..1001 FT /evidence="ECO:0007829|PDB:3OBA" FT HELIX 1007..1009 FT /evidence="ECO:0007829|PDB:3OBA" FT STRAND 1016..1024 FT /evidence="ECO:0007829|PDB:3OBA" SQ SEQUENCE 1025 AA; 117619 MW; AF3136235DB5A464 CRC64; MSCLIPENLR NPKKVHENRL PTRAYYYDQD IFESLNGPWA FALFDAPLDA PDAKNLDWET AKKWSTISVP SHWELQEDWK YGKPIYTNVQ YPIPIDIPNP PTVNPTGVYA RTFELDSKSI ESFEHRLRFE GVDNCYELYV NGQYVGFNKG SRNGAEFDIQ KYVSEGENLV VVKVFKWSDS TYIEDQDQWW LSGIYRDVSL LKLPKKAHIE DVRVTTTFVD SQYQDAELSV KVDVQGSSYD HINFTLYEPE DGSKVYDASS LLNEENGNTT FSTKEFISFS TKKNEETAFK INVKAPEHWT AENPTLYKYQ LDLIGSDGSV IQSIKHHVGF RQVELKDGNI TVNGKDILFR GVNRHDHHPR FGRAVPLDFV VRDLILMKKF NINAVRNSHY PNHPKVYDLF DKLGFWVIDE ADLETHGVQE PFNRHTNLEA EYPDTKNKLY DVNAHYLSDN PEYEVAYLDR ASQLVLRDVN HPSIIIWSLG NEACYGRNHK AMYKLIKQLD PTRLVHYEGD LNALSADIFS FMYPTFEIME RWRKNHTDEN GKFEKPLILC EYGHAMGNGP GSLKEYQELF YKEKFYQGGF IWEWANHGIE FEDVSTADGK LHKAYAYGGD FKEEVHDGVF IMDGLCNSEH NPTPGLVEYK KVIEPVHIKI AHGSVTITNK HDFITTDHLL FIDKDTGKTI DVPSLKPEES VTIPSDTTYV VAVLKDDAGV LKAGHEIAWG QAELPLKVPD FVTETAEKAA KINDGKRYVS VESSGLHFIL DKLLGKIESL KVKGKEISSK FEGSSITFWR PPTNNDEPRD FKNWKKYNID LMKQNIHGVS VEKGSNGSLA VVTVNSRISP VVFYYGFETV QKYTIFANKI NLNTSMKLTG EYQPPDFPRV GYEFWLGDSY ESFEWLGRGP GESYPDKKES QRFGLYDSKD VEEFVYDYPQ ENGNHTDTHF LNIKFEGAGK LSIFQKEKPF NFKISDEYGV DEAAHACDVK RYGRHYLRLD HAIHGVGSEA CGPAVLDQYR LKAQDFNFEF DLAFE //