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Database: UniProt
Entry: G4TGK5_SERID
LinkDB: G4TGK5_SERID
Original site: G4TGK5_SERID 
ID   G4TGK5_SERID            Unreviewed;      1032 AA.
AC   G4TGK5;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   16-JAN-2019, entry version 41.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=PIIN_04392 {ECO:0000313|EMBL:CCA70454.1};
OS   Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS   (Piriformospora indica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Sebacinales; Serendipitaceae; Serendipita.
OX   NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA70454.1, ECO:0000313|Proteomes:UP000007148};
RN   [1] {ECO:0000313|EMBL:CCA70454.1, ECO:0000313|Proteomes:UP000007148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA70454.1,
RC   ECO:0000313|Proteomes:UP000007148};
RX   PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA   Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S.,
RA   Biedenkopf D., Wong P., Samans B., Grimm C., Basiewicz M., Murat C.,
RA   Martin F., Kogel K.H.;
RT   "Endophytic Life Strategies Decoded by Genome and Transcriptome
RT   Analyses of the Mutualistic Root Symbiont Piriformospora indica.";
RL   PLoS Pathog. 7:e1002290-e1002290(2011).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:CCA70454.1}.
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DR   EMBL; CAFZ01000083; CCA70454.1; -; Genomic_DNA.
DR   ProteinModelPortal; G4TGK5; -.
DR   EnsemblFungi; CCA70454; CCA70454; PIIN_04392.
DR   InParanoid; G4TGK5; -.
DR   OMA; WMMGKRV; -.
DR   OrthoDB; 179316at2759; -.
DR   Proteomes; UP000007148; 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:UP000007148};
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:UP000007148};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     16       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        17   1032       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5003468735.
FT   DOMAIN      401    586       BetaGal_dom2. {ECO:0000259|SMART:
FT                                SM01029}.
SQ   SEQUENCE   1032 AA;  116023 MW;  1A2B8EF6DA5B4662 CRC64;
     MLMLLGATVT IWLIQSARNP LAWNIFDLIG PRGRTKVHLS PATVLLRDNG LTKDVQWDEY
     SLFIKGRRVL LWSGEIHPWR IPVRSQWLDV LQKIKASGMN AISVYSHWGL HNPSPGVFDF
     TGWQDWQVFL DIAKQVGLWV VFRPGPYINA ETTGGGIPGW VLAQTPDDLR SNNTAYFEAW
     SPYIRHISEI IARNQITEGG PIIAVQAENE FTSNPEEGPS HKRQMMAQLR DAFTKSNVVV
     PLTHNDAGMN GYFVDGKGSP DIYGFDDYPQ GFDCANPLVW KNLTKAYHDY HMKTFPKSPL
     YIPEAQAGAF DPWGPSAPTY DNCRILTGPS FQNNLYNHML ASNAKMINLY MMYGGTSWGN
     IPFPGVYTSY DYGSPIRETR ALSDKYDHLK LLGLFLRSMP DMYHTDVLEN ESLLRTGSTS
     ELTVVHLKNP ITNAGFYYIR HVNVSTQDSF DYSLKLNTIH QELSLPLFSS LFTLRGRTTD
     LIMTDISFGD SLITYTSASI FFAGKMADRD VLILYGDMEQ AHEAIIHLRG KPRRLTTSPS
     VSMVRNQYHG IGTAISFLPG IRQVVEVWDT DQQLVLYCDT ETAFKLHAPM LQRRNTSDPF
     ATFWNIGSND TIVVGGPYIV RNATLDDGHL ALFGDLEGDT MLQLVGLPQG LNRITWNGID
     VGTDFELQEV LSVLTVPLGM VRKSTLLTLP TLENWRYRDS LPEITDSFNY DAWTVAENIV
     TNSSYKPLFG DGPVLYACDY GFCEGTVIWS GEFVATNEDR AVRMVINGGE AFAASVWLNG
     HFLKTTYGNS TRNTNIICET DEIFEFPEES LRKGERNVLV ILQDNMGMDE TGPHYDANQS
     KSPRGIRGYS LHSGGNFTSW KVQGRLGGYD RFVDRYRGLL NNGGLHGERL GWHLPGFPDE
     KWESRSLEMG LVDDRAGVGF FRTTFALDLP RDCDISISLE FEDDFPSPYR AFVFVNGWNM
     GKRIGNLGPQ TKFVVHEGIL NHHGPNTLAV ALWAMERGQG IKPRLRLVLN HKFEGGVGAD
     YEPGPGWADL YH
//
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