ID G2X4D3_VERDV Unreviewed; 1046 AA.
AC G2X4D3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN ORFNames=VDAG_05015 {ECO:0000313|EMBL:EGY23577.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY23577.1, ECO:0000313|Proteomes:UP000001611};
RN [1] {ECO:0000313|Proteomes:UP000001611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC {ECO:0000313|Proteomes:UP000001611};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR EMBL; DS572703; EGY23577.1; -; Genomic_DNA.
DR RefSeq; XP_009653046.1; XM_009654751.1.
DR AlphaFoldDB; G2X4D3; -.
DR STRING; 498257.G2X4D3; -.
DR EnsemblFungi; EGY23577; EGY23577; VDAG_05015.
DR GeneID; 20706478; -.
DR KEGG; vda:VDAG_05015; -.
DR eggNOG; KOG2024; Eukaryota.
DR HOGENOM; CLU_002346_0_0_1; -.
DR InParanoid; G2X4D3; -.
DR OMA; EITDFCH; -.
DR OrthoDB; 276651at2759; -.
DR Proteomes; UP000001611; Chromosome 4.
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:SF1; LACTASE; 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 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:UP000001611}.
FT DOMAIN 754..1042
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1046 AA; 117056 MW; 5CD269343D74F6EC CRC64;
MSPKSIPPQE IEGTPDWQHQ AVFRRNTLPA RSYHIPETSL LLNGQWEFSY TSCPEESPQP
GDEDVPEDNW GTIEVPGHWQ LQGHGRPHYT NTVFPIPVCP PFAPTDNPTG VYRRTFNVPS
TWDASAQLRL RFDGVDSAYH IYVNGALVGY AEGSRNASEF DVTDFVKHDA PNDLFVKVYQ
WSSATYIEDQ DQWWLSGIFR DVHLLAFPKT DRIDDWFLRT DLDAKYENAT LQATVDVTAS
KSDSLKITLK ELVKNGGAVI TTKDAPVKSG DTKIDLDLAV SNPKKWTAET PYLYQVEITL
GAHTIQQNIG FRKVELKGGL IRVNGVPIRI YGVNRHEHHP KFGRAVPLDF IKRDLLLMKT
HNINSLRCSH YPPHPKLFDM CDELGLWVMD EADLETHGFY DCIARPLDIP EEWDYEERKK
QTFPPAGKYT SQNPDWKEAY VDRMVQLVQR DKNHSSIIMW SLGNEAFYGD NHKAMYEYGK
AFDPTRPIHY EGDVDAVTAD MFSYMYPPID RLLHLMKTAG VKEDGSWDKP IVLCEYAHAM
GNGPGALDDY VETFEANERL QGGYIWEWAN HGIWKEDPDG KKYYAYGGDF DDFPNDGTFV
MDGLLHSTHE PTLGLVQLKK SYQPLLLSVE GGKLVIKNKY DFVGVQHLSA TYKVEELGES
TSHIAAGSLE IPAVAAGETV SVDLPASLSN IKSTKDVYLT VSFRLKESTN WAEPSHEIAW
IQHQLSSAEA PASAAALNTL TSKLTVEKTR ARATISGLDF SFVFDTARGL LVSWTAGDKT
LLEKDPATGA ALIPNFWRPP TDNDVPVACV YWKRFGVHEL TSQLRSIDIV ESADKVEIST
KTFLSPPVLA WGFETTSKYT ISATGKLTVD VDLTPTGRMP TTIPRAGFNL HLPKALSQVK
YLGLGPDESY PDKQTSQRVG VYSATVPELQ THYEVPQENG NRMATRYVTL TEGGHGRGFR
ATPSDASAWT DESWRNFSFR ASHYSADTLH FAKHPCDLVE ADATLLRLDA RVAGVGSAAC
GPGPREDLLV KTKPLKFGFV LERVGF
//