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Database: UniProt
Entry: F6XNT9_XENTR
LinkDB: F6XNT9_XENTR
Original site: F6XNT9_XENTR 
ID   F6XNT9_XENTR            Unreviewed;       648 AA.
AC   F6XNT9;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   13-FEB-2019, entry version 51.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   Name=glb1l {ECO:0000313|Ensembl:ENSXETP00000034051,
GN   ECO:0000313|Xenbase:XB-GENE-964696};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Silurana.
OX   NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000034051, ECO:0000313|Proteomes:UP000008143};
RN   [1] {ECO:0000313|Ensembl:ENSXETP00000034051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000034051};
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L.,
RA   Blitz I.L., Blumberg B., Dichmann D.S., Dubchak I., Amaya E.,
RA   Detter J.C., Fletcher R., Gerhard D.S., Goodstein D., Graves T.,
RA   Grigoriev I.V., Grimwood J., Kawashima T., Lindquist E., Lucas S.M.,
RA   Mead P.E., Mitros T., Ogino H., Ohta Y., Poliakov A.V., Pollet N.,
RA   Robert J., Salamov A., Sater A.K., Schmutz J., Terry A., Vize P.D.,
RA   Warren W.C., Wells D., Wills A., Wilson R.K., Zimmerman L.B.,
RA   Zorn A.M., Grainger R., Grammer T., Khokha M.K., Richardson P.M.,
RA   Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
RN   [2] {ECO:0000313|Ensembl:ENSXETP00000034051}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUN-2011) to UniProtKB.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|RuleBase:RU003679, ECO:0000256|SAAS:SAAS00534244}.
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DR   EMBL; AAMC01022692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01022693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01022694; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012820114.1; XM_012964660.2.
DR   UniGene; Str.27574; -.
DR   ProteinModelPortal; F6XNT9; -.
DR   Ensembl; ENSXETT00000034051; ENSXETP00000034051; ENSXETG00000015609.
DR   GeneID; 548712; -.
DR   CTD; 79411; -.
DR   Xenbase; XB-GENE-964696; glb1l.
DR   eggNOG; KOG0496; Eukaryota.
DR   eggNOG; COG1874; LUCA.
DR   GeneTree; ENSGT00390000006586; -.
DR   Reactome; R-XTR-1660662; Glycosphingolipid metabolism.
DR   Reactome; R-XTR-4085001; Sialic acid metabolism.
DR   Reactome; R-XTR-6798695; Neutrophil degranulation.
DR   Proteomes; UP000008143; Unassembled WGS sequence.
DR   Bgee; ENSXETG00000015609; Expressed in 13 organ(s), highest expression level in mesonephros.
DR   GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR   GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; -; 2.
DR   InterPro; IPR026283; B-gal_1-like.
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; PF13364; BetaGal_dom4_5; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PIRSF; PIRSF006336; B-gal; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008143};
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:UP000008143};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    648       Beta-galactosidase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5003345360.
FT   DOMAIN       39    354       Glyco_hydro_35. {ECO:0000259|Pfam:
FT                                PF01301}.
FT   DOMAIN      567    607       BetaGal_dom4_5. {ECO:0000259|Pfam:
FT                                PF13364}.
FT   ACT_SITE    186    186       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006336-1}.
FT   ACT_SITE    266    266       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006336-1}.
SQ   SEQUENCE   648 AA;  73085 MW;  1FB7C7222A555AFF CRC64;
     MMWLRTFLHI FLLMVPYGSV SVSTTSSRTF EIDFEHNCFR KDGQPFRYIS GSIHYSRVPQ
     YYWKDRLLKM KMAGLDAIYT YVPWNFHETK PGVYNFSGDH DIESFLKLAN EIGLLVILRA
     GPYICAEWDM GGLPAWLLAK ESIVLRSSDP DYLQAVDNWM GVFLPKMKPL LYHNGGPIIS
     VQVENEYGSY FTCDYNYLRH LLQLFRHHLG DEVVLFTTDG SGLQYVRCGT IQGLYTTVDF
     GPGSNVTETF SVQRYCEPKG PLVNSEFYTG WLDHWGEPHS VVATEMVTKS LDEILAHGAN
     VNMYMFIGGT NFGYWNGANT PYAPQPTSYD YDAPLSEAGD LTDKYFAVRE VIKKYKQIPE
     GPIPPTTPKY AYGEIKMEKV KTVTEALDIL ASHGAIQGTY PLTFDQMKQY FGFVLYRTTL
     PINCSNPTTL TTLSNGVRDR AYVTVNGVPQ GVLERDKQTA INVTGVAGAE LDLLVESMGR
     VNFGRYNNDF KGLLTNVTLN GELLVNWTMY PLDIDSAVNG GLLSTIHIPY ASAFSAPMFY
     KGSLIIPTGI PDLPQDTFIQ FPGWTKGQIW INGFNLGRYW PVRGPQVTLY VPRSILTTTL
     VNNITVLELE NSPCNSGKCV VEFVDKPVLN KVKQIVDEHK FSKEKFLK
//
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