BGAL_KLULA
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 03-AUG-2022, entry version 146.
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 / 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}.
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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; 28985.XP_452194.1; -.
DR ChEMBL; CHEMBL3309040; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR EnsemblFungi; CAH02587; CAH02587; KLLA0_B14883g.
DR GeneID; 2897170; -.
DR KEGG; kla:KLLA0_B14883g; -.
DR eggNOG; KOG2024; Eukaryota.
DR HOGENOM; CLU_002346_0_0_1; -.
DR InParanoid; P00723; -.
DR OMA; WCDHGIL; -.
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; 2.60.40.10; -; 2.
DR Gene3D; 2.70.98.10; -; 1.
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 Pfam; PF02929; Bgal_small_N; 1.
DR Pfam; PF16353; DUF4981; 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 SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF49303; SSF49303; 2.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 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