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Database: UniProt
Entry: A0A074XW29_AURPU
LinkDB: A0A074XW29_AURPU
Original site: A0A074XW29_AURPU 
ID   A0A074XW29_AURPU        Unreviewed;      1017 AA.
AC   A0A074XW29;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   16-JAN-2019, entry version 20.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=M438DRAFT_372164 {ECO:0000313|EMBL:KEQ87839.1};
OS   Aureobasidium pullulans EXF-150.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Dothideales; Saccotheciaceae;
OC   Aureobasidium.
OX   NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ87839.1, ECO:0000313|Proteomes:UP000030706};
RN   [1] {ECO:0000313|EMBL:KEQ87839.1, ECO:0000313|Proteomes:UP000030706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ87839.1,
RC   ECO:0000313|Proteomes:UP000030706};
RX   PubMed=24984952;
RA   Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J.,
RA   Zalar P., Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y.,
RA   Lipzen A., Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT   "Genome sequencing of four Aureobasidium pullulans varieties:
RT   biotechnological potential, stress tolerance, and description of new
RT   species.";
RL   BMC Genomics 15:549-549(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000256|RuleBase:RU000675,
CC         ECO:0000256|SAAS:SAAS01116863};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
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DR   EMBL; KL584976; KEQ87839.1; -; Genomic_DNA.
DR   EnsemblFungi; KEQ87839; KEQ87839; M438DRAFT_372164.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000030706; 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; -; 1.
DR   Gene3D; 2.60.120.260; -; 2.
DR   Gene3D; 2.60.390.10; -; 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; PTHR23421; 1.
DR   Pfam; PF10435; BetaGal_dom2; 1.
DR   Pfam; PF13363; BetaGal_dom3; 1.
DR   Pfam; PF13364; BetaGal_dom4_5; 2.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SMART; SM01029; BetaGal_dom2; 1.
DR   SUPFAM; SSF117100; SSF117100; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000030706};
KW   Glycosidase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108888};
KW   Hydrolase {ECO:0000256|RuleBase:RU000675,
KW   ECO:0000256|SAAS:SAAS00108869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030706};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25   1017       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5001702657.
FT   DOMAIN      396    573       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1017 AA;  110322 MW;  0F3EC94516AA0CFE CRC64;
     MLGKTLIKAA ALVASLAITS DALALKKQNL NDLIKPYKRE LLQDLVTWDE HSLFVRGERI
     MLYSGEFHPF RLPVPSLWLD VFQKIKALGY NGVSFYVDWA LIEGKQGDFS AEGIFAWEPF
     FEAATKAGIY LIARPGPYIN AEVSGGGFPG WLARNPGIPR TRDPRFLNAT DNYSRQIGEI
     IAKAQITEGG PVILYQPENE YSQAVSSDPE FPDQVYMAAV EKRFRDAGIV VPSILNDAYP
     HGYFAPGSGE GAVDIYGHDG YPLGFDCANP TTWPDNALPT YYGDLHAEQS PSTPYSILEF
     QGGSFDPWGG LGFEQCSELL NSEFQRVFYK NDFSFGMTIF NIYMTYGGTN WGNQGHPGGY
     TSYDYGAVIT EQRLVSREKY SEAKLEANFL QASPAYLTAI PQNNTHANGS YSNNPEIAVT
     ALFGNRTNFF VIRHAAYNSL ASTEFKLTLP TSQGNITIPQ LNGSLVLNGR DSKWAVTDYD
     AAGTNLLYSS AEIFTQKAYG DKQVLVVYSG ANENHELAFT LSCSSEVIEG SGINIVKKKG
     TTIIGFKSSS ERRIVKIGEL YVYILDRNDA YNYWVLDLPS SPVSGNYTNG TIDTSAAIVK
     AGYLLRTVEA SGTILSLTGD LNATTEIEII GGAPAKLTEL KFNGETIKFA QDSCSGVVTA
     SATYSEPSFS VPDLSTVDWK VTNSLPEIVA GYDDSLWTNA DLTYSNNTQR NLTTPVSLYA
     QDYGYNIGNL LYRGHFTATG GENSIYLQTQ GGSAFGMSAW LNGTFLGSAR GIDAASNANS
     TFSLPNVASG SSYVLTVLID HMGLQENGQG GSSEMKTPRG ILNYSLNGRN ASAISWKLTG
     NLGGEDYQDR TRGPLNEGGL YAERQGYHLP GAPTSSWSNS THGPMIGITA PGVAFYSTTF
     DLDMPAGYDI PIAISFSNAT SSTNGSASVA YRSQIYVNGY QFGKYVSNIG PQDVFPVPQG
     IFDYNGSNYL AVSLWALDEG GAKISNLSLV AGPVIQSGYG PVELSPLTCW SKREEAY
//
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