ID A5D9Q8_PICGU Unreviewed; 977 AA.
AC A5D9Q8;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN ORFNames=PGUG_00009 {ECO:0000313|EMBL:EDK35911.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK35911.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK35911.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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:0000256|ARBA:ARBA00001412};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR EMBL; CH408155; EDK35911.2; -; Genomic_DNA.
DR RefSeq; XP_001486632.1; XM_001486582.1.
DR AlphaFoldDB; A5D9Q8; -.
DR STRING; 294746.A5D9Q8; -.
DR GeneID; 5129417; -.
DR KEGG; pgu:PGUG_00009; -.
DR VEuPathDB; FungiDB:PGUG_00009; -.
DR eggNOG; KOG2024; Eukaryota.
DR HOGENOM; CLU_002346_0_2_1; -.
DR InParanoid; A5D9Q8; -.
DR OMA; EITDFCH; -.
DR OrthoDB; 276651at2759; -.
DR Proteomes; UP000001997; Unassembled WGS sequence.
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; 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.
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:UP000001997}.
FT DOMAIN 695..973
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 977 AA; 111544 MW; 6BD1BE99F6729654 CRC64;
MVNGTSIMSP LPNLLLLPSE DFTFEKKLVV PGHWQLQGYG SPQYTNVVYP FVVDVPNPPT
RNPTGTYHRQ FTVPKTWESH QCRIRFEGVD NSYHVFLNGK LIGYHEGSRN CAEFDLEPAI
KRDQVNHLWV RVYQWSSSTY IEDQDQWWLS GIFRDVWLLG FHKQGHIENF VVTTDLKNTD
GVCGLKVQVG GENHSFQKFE GLKLYVNLSG SENLAEVNSS VTNLGIKVPN VKPWTAETPT
LHKLTLELRD STGFVLSKVV QKVGFRKVEM SDGQIKVNGQ PILLRGVNRH DHHPQFGRAV
PLDFIKRDLQ LMKQHNINAV RTSHYPNTPQ LYELANEYGF WVFAEADLEC HGFFECVRRP
IDGSDDPEYK NGKLELFGRA KKFTSDNPEW KNTYVDRARG LVLRDINQPC IIVWSLGNEA
FFGQNHVAMA DFIRHADPTR LVHYEPDMDA TVTDMYSRMY PSFETMQEFI KKNDKPLVLC
EYAHAMGNGP GLLRQYQELF YTVPHFQGGF VWEWNNHGLE TEANGSKFYG YGGDFGEKVH
DGVFCMDGLV DSRHEPTPGL LEYKKVIEPV EVRFHDGEIE FKNMFDFSDL DAYYATFRLV
EYESVFSEEI LASRQLHFPS VPPHSSYSIL FPCEIPSSSN TVILDVDVKT LNSSEAVPKD
HTVAFGQKVF KASTKTEFNK TISNVNVEET NHRITVRSKA LEFQFNKITG CVEKYNQDKP
IIVAGLNNLT FWRPTTNNDD NFDGPYWKKF GLDMMEIQVR NVKVTPIANG ERSNLLATLE
VESFIGPPIL SWGFDCIQKY SIYADRLEIG TLLTAIGFNK CCVPSTLPRL GYEFAVPETV
NEISWLGRGS GESYADKKES QKIGLYKKKF GDSDYSYDYP QENGNHEDVT WLALKDGDGG
FVITMKNRNF GFKCSSEYDV QQALHPHEIK RGQKYVRVDY QQHGVGTAAC GPGVLEKFQF
KLEGPIEFTT TIRYVES
//
