ID A0A0D2AE20_9EURO Unreviewed; 1010 AA.
AC A0A0D2AE20;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
GN ORFNames=PV06_09377 {ECO:0000313|EMBL:KIW38411.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW38411.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW38411.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW38411.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|RuleBase:RU000675};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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; KN847341; KIW38411.1; -; Genomic_DNA.
DR RefSeq; XP_016258627.1; XM_016410820.1.
DR AlphaFoldDB; A0A0D2AE20; -.
DR STRING; 215243.A0A0D2AE20; -.
DR GeneID; 27361451; -.
DR VEuPathDB; FungiDB:PV06_09377; -.
DR HOGENOM; CLU_005732_2_0_1; -.
DR OrthoDB; 1032627at2759; -.
DR Proteomes; UP000053342; Unassembled WGS sequence.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.102.20.10; Beta-galactosidase, domain 2; 1.
DR Gene3D; 2.60.390.10; Beta-galactosidase, domain 3; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR018954; Betagal_dom2.
DR InterPro; IPR037110; Betagal_dom2_sf.
DR InterPro; IPR025972; BetaGal_dom3.
DR InterPro; IPR036833; BetaGal_dom3_sf.
DR InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR InterPro; IPR019801; Glyco_hydro_35_CS.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421:SF122; BETA-GALACTOSIDASE A-RELATED; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF13364; BetaGal_ABD2; 2.
DR Pfam; PF10435; BetaGal_dom2; 1.
DR Pfam; PF13363; BetaGal_dom3; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SMART; SM01029; BetaGal_dom2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF117100; Beta-galactosidase LacA, domain 3; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW Reference proteome {ECO:0000313|Proteomes:UP000053342};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1010
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002238338"
FT DOMAIN 395..574
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 1010 AA; 110623 MW; C22E72F0BB65AAF0 CRC64;
MKLVFASIVG LLATQLSALA VPSNTFGRYK ITDHPDPEKR ALLQNLVTWD ETSLFVRGER
MMIWSGEFHP FRLPVPSLWL DVFQKIKALG FNCASFYVDW ALVEGKHGNY TADGVFALEP
FFNAASSAGI YLLARPGPYI NAESSGGGFP GWLQRIKGRL RTTDPSFIEA TQNYVIHVAG
TIAKAQITNG GPIILYQPEN EYSGFCCGID GPDGNYMQIV EDQAREAGVV VPLLSNDAGV
NGYNAPGTGN GSVDIYGHDS YPLGFDCANP TVWPAGKLPT DYWQRHLRQS PTTPYSITEF
QAGSFDPWGG PGFEKCGVLV GSDFERVFYK NDLSFGVKFL NLYMIFGGTN WGNLGHPGGY
TSYDYAAPIA EGRQVDRDKY SQLKLIGNFV KVSPAYFDAV PLHNSTALYT DNEDLLVTPV
KGNSSATTFY VVRHTNYTSQ ASTSYKLMLQ TSAGNLTVPQ AGGVLTLNGR DSKIHVTDYD
VNGTKILYST AEVFTWKDFG QKKVLLVYGG EGEHHEISIS STSTPSLVEG PQVGITMKNG
SQAVVAWETT TQRRIVEVDN LQIFILDRNS AYNYWVPELS GNAQTVGFSS QETTASSIIV
KAGYLIRAAY LEGSNLHLVA DFNATTPIEV IGAPSIANAL FINGQASQYS TSSIGSWTTN
VTWADPKLTL PTLSNLEWKY IDTLPEVQPG FDDSLWPVAD LTTTNNTWRK LTTPTSLYAS
DYGFHSGSLL YRGHFVSQGN ESTLYVNTRG GTAYGHSIWL NQTFIGSWAG VSTQNNTNVT
YDLPPNLQSG KAYVFTVLID HMGYDESGTV GSDEMKTPRG VFDYALAGRD KADVGWKLTG
NLGGEDYRDR VRGPLNEGGM YAERQGWHLP NPPTQNWDSR SPFDGISQAG VGFFSTQFDL
NIPSGWDVPL SFTFGNSTLP PAEYRVLMYV NGFQYGKYVN HIGPQTSFPV PQGVLNYQGT
NWLALTLWAH QSTGAKLENF QIESDTPVMS ALGEVDFVGG SGYSQREGAY
//
