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Database: UniProt
Entry: A0A074WUX3_9PEZI
LinkDB: A0A074WUX3_9PEZI
Original site: A0A074WUX3_9PEZI 
ID   A0A074WUX3_9PEZI        Unreviewed;      1009 AA.
AC   A0A074WUX3;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   16-JAN-2019, entry version 22.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=M436DRAFT_46798 {ECO:0000313|EMBL:KEQ73527.1};
OS   Aureobasidium namibiae CBS 147.97.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Dothideales; Saccotheciaceae;
OC   Aureobasidium.
OX   NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ73527.1, ECO:0000313|Proteomes:UP000027730};
RN   [1] {ECO:0000313|EMBL:KEQ73527.1, ECO:0000313|Proteomes:UP000027730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ73527.1,
RC   ECO:0000313|Proteomes:UP000027730};
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; KL584709; KEQ73527.1; -; Genomic_DNA.
DR   RefSeq; XP_013427573.1; XM_013572119.1.
DR   EnsemblFungi; KEQ73527; KEQ73527; M436DRAFT_46798.
DR   GeneID; 25410589; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000027730; 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:UP000027730};
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:UP000027730};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26   1009       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5001701748.
FT   DOMAIN      399    576       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1009 AA;  109248 MW;  ECCADA57437A174F CRC64;
     MVLGKTFMKA AALVAGLAIT SDALALRKPN LNELIKPYKR DVGLLQDLVT WDEHSLFVRG
     ERVMIYSGEF HPFRLPVPSL WLDVFQKIKA LGYNAVSFYV DWALVEGKQG DFTAEGIFAW
     EPFFEAAQEA GIYLIARPGP YINAEVSGGG FPGWLARNPG IPRTRDPRFL EATDNYSRAI
     GEIIAKAQIT NGGPIILYQP ENEYSQAVSS DPEFPDQVYM AAVEKKFRDA GIIVPSILND
     AYPHGYFAPG TGPGAVDIYG HDSYPLGFDC ANPTTWPNNS LPTYFGDLHA EQSPSTPYSI
     LEFQGGSFDP WGGSTFEKCG VLLNSEFQRV FYKNDFSYGL TIFNIYMTYG GTNWGNLGHP
     GGYTSYDYAA VIAEDRSVSR EKYSEAKLEA NFLQASPAYL TAIPQNNTHA NGSYTDNPDI
     AVTALFGNRT NFFVVRHAVF NSYESTQFKL TLPTSQGNIT IPQLNGSLVL NGRDSKFAVT
     DYDAAGTNLL YSSAEIFTQK SYGDKQILLV YAGFNENHEL ALTLSCSSEV LEGSGLNIVK
     KKGTTIIGFK SSSERRVVKI GELFVYILDR NDAYNYWVLD LPSSPTSAAV VKAGYLLRTV
     EVSGNSLHLT GDINATTEIE VIGGAPAKLT ELTFNGESIK FAQDSCSGVV TGSVAYNEPS
     FSLPDLSTVG WKVIDSLPEI ASSYDDSLWT NADLTYSNNT QRNLTTSVSL YGQDYGYNGG
     SLLFRGHFTA TGSEDSIYLQ TQGGSAFGMS AWLNGTFLGS ARGIDAASNA NSTFSLPNVA
     SGSSYVLTVL IDHMGLQENG QGGSSEMKTP RGILNYSLAG RNASALTWKL TGNLHGEDYE
     DRTRGPLNEG GLYAERQGYH LPGAPTSGWT NSTLGPMAGV TSPGVSFYAT TFDLDMPAGY
     DIPISISFSN ATSSSNGSAT VAYRSQIFVN GYQFGKYVSN IGPQDVFPVP EGIFNYHGPN
     YFAVSLWALD EGGAKISNLS LVAGPVIQSG YGPVSLSPMT GWSKREGAY
//
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