(data stored in SCRATCH zone)

SWISSPROT: D6XX98_BACIE

ID   D6XX98_BACIE            Unreviewed;      1027 AA.
AC   D6XX98;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU361154, ECO:0000256|SAAS:SAAS01166384};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU361154, ECO:0000256|SAAS:SAAS01166384};
DE   AltName: Full=Lactase {ECO:0000256|RuleBase:RU361154};
GN   OrderedLocusNames=Bsel_0416 {ECO:0000313|EMBL:ADH97955.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97955.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97955.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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:RU361154,
CC         ECO:0000256|SAAS:SAAS01166382};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|RuleBase:RU361154, ECO:0000256|SAAS:SAAS00568376}.
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DR   EMBL; CP001791; ADH97955.1; -; Genomic_DNA.
DR   STRING; 439292.Bsel_0416; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   EnsemblBacteria; ADH97955; ADH97955; Bsel_0416.
DR   KEGG; bse:Bsel_0416; -.
DR   eggNOG; ENOG4105CNT; Bacteria.
DR   eggNOG; COG3250; LUCA.
DR   HOGENOM; HOG000252444; -.
DR   KO; K01190; -.
DR   OMA; DQDMFRL; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; -; 1.
DR   Gene3D; 2.60.40.10; -; 2.
DR   Gene3D; 2.70.98.10; -; 1.
DR   InterPro; IPR004199; B-gal_small/dom_5.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR023933; Glyco_hydro_2_beta_Galsidase.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR023230; Glyco_hydro_2_CS.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR032312; LacZ_4.
DR   PANTHER; PTHR46323; PTHR46323; 1.
DR   Pfam; PF02929; Bgal_small_N; 1.
DR   Pfam; PF16353; DUF4981; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SMART; SM01038; Bgal_small_N; 1.
DR   SUPFAM; SSF49303; SSF49303; 2.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
DR   PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XX98.
DR   SWISS-2DPAGE; D6XX98.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Glycosidase {ECO:0000256|RuleBase:RU361154,
KW   ECO:0000256|SAAS:SAAS00456829};
KW   Hydrolase {ECO:0000256|RuleBase:RU361154,
KW   ECO:0000256|SAAS:SAAS00456838, ECO:0000313|EMBL:ADH97955.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT   DOMAIN      755   1025       Bgal_small_N. {ECO:0000259|SMART:
FT                                SM01038}.
SQ   SEQUENCE   1027 AA;  116507 MW;  F006B4A28E3CC7F3 CRC64;
     MAMHEQTARR TYHPPENGYP EWNNNPELFQ INREAPHADP RLYDTKEKAV AGDPDQVAWR
     RSLNGTWSFL YADTPKERVE DFYTWDAGDE RFTTVQVPGH LQLQGFDYPH YTNTRYPWEE
     REDIKPPFAP VNYNPVGQYM RTFTMTGEPG DRPVYLRFEG VEAAFYLWIN GTFAGYSEDS
     FTPSEFEISD LVHAGENTVA VEVYHWCDSS WLEDQDFWRF SGIFRDVWLY ETPAEQIRDY
     TVKTSFHGTD GLLDLDVLIR RFKTKEVREL TVKADVYTYP DQKPVAEGAV TGSGDRMTLQ
     ITVPDVLRWS AETPNLYIVV LTLQDEAGEA ILYVHQKTGF QEFGLKDGLM TLNGAPLLFR
     GVNRHEFMPD KGRAGITREE MEADLILMKQ HNINAVRTSH YPNHPAFYEL CDIYGLYVID
     EVNMETHGTW VYGQEGIGET IPGNRPEWTE NVLDRCRSLY ERDKNATSVI IWSLGNESFG
     GSNLKEMYDY FKEKDETRLV HYEGIFHYRE YDASDMESTM YIPPHKVEDY AKEAEGNPDA
     KPYILCEYSH AMGNSLGNFH KYTDLFLKYP ILQGGFIWDW RDQALWSTRP DGTAFLAYGG
     DFGDTPTDGN FSGNGLIFAD GTATPKLLEA KKGYEPARIR FEGNHIHVTN DYAFLDLDGF
     RCQWELLSDG KTVREGTLSL KGAPGSTHSY AVDLPETEGE RILEVRLVLG EDTLWAEAGH
     EMTFEQFILN DNGAPRSETP RGQANVSHDD GEWLSVAAGG VTYTFARDTG DLTEVTKDGK
     QHLTAPVAPN FHRAMTDNDR GSGLPKRSAV WRKAGKNRRL NAFGVEESGE SVHVTVDYAF
     PDAGSSSMRV MYTLNGSGKA AVSFRFTPDN AMPEIPEVGL MMQLAPSLTE LQWYGRGPHE
     TYQDRFRSAR IGIHESTVNE RLTPYLKPQE CGNMTGVRWL TLTNPDGSGI RITGSGDLEA
     NALPYSPEEL ELATHQDRLP QPRHTVLRLN AAQMGVGGDD SWGQKTHDEY TLFTDRTFEA
     SFDLTLI
//

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