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Database: UniProt
Entry: E2N753_9BACE
LinkDB: E2N753_9BACE
Original site: E2N753_9BACE 
ID   E2N753_9BACE            Unreviewed;      1229 AA.
AC   E2N753;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN   ORFNames=BACCELL_00095 {ECO:0000313|EMBL:EEF92273.1};
OS   Bacteroides cellulosilyticus DSM 14838.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=537012 {ECO:0000313|EMBL:EEF92273.1, ECO:0000313|Proteomes:UP000003711};
RN   [1] {ECO:0000313|EMBL:EEF92273.1, ECO:0000313|Proteomes:UP000003711}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14838 {ECO:0000313|EMBL:EEF92273.1,
RC   ECO:0000313|Proteomes:UP000003711};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEF92273.1, ECO:0000313|Proteomes:UP000003711}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14838 {ECO:0000313|EMBL:EEF92273.1,
RC   ECO:0000313|Proteomes:UP000003711};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Bacteroides cellulosilyticus (DSM 14838).";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC         in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000256|ARBA:ARBA00001412};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEF92273.1}.
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DR   EMBL; ACCH01000006; EEF92273.1; -; Genomic_DNA.
DR   RefSeq; WP_007209492.1; NZ_JANSWE010000051.1.
DR   AlphaFoldDB; E2N753; -.
DR   HOGENOM; CLU_270292_0_0_10; -.
DR   Proteomes; UP000003711; 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; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
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   PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 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   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EEF92273.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..1229
FT                   /note="beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003161312"
FT   DOMAIN          246..410
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          466..573
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          576..807
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
SQ   SEQUENCE   1229 AA;  140252 MW;  9F1081A6AF645B86 CRC64;
     MRKLYATFLI SACALVSLPS NAQAEWKNDF SNQGEILKTV GKGVCGVTDG VFRSVDAYSC
     FGNPEWKNYT MSFKARAPKD ADQVQIWAGF RAYNRFDRYV LGLKGGLQDD IYLMRLGYMG
     TDEFLGVRPL GFHPVPGEWY NIKVEVCGNR IRVFLNNEKE PRIDVTDKNG NLAPSGQVTL
     GGGWIETEFD DLVVTPMRED ALKDVKVVEY RKMITPQEKE NKRQQERANY RTVKVNELVD
     SRTDISLDGT WLFMPEYQLD DKDKAISVAT DDKNWHVMSV PNFWNPIRIW LHGETMPSPA
     GPQPKGVSDT YYQQETERCE GYTFDYRKTK AAWYRQWVEL PANVEGKNMT LTFDAVSKVA
     EIYINGELAG SHIGMFGEIQ VDGSKLLKSG KNLVVVKVIS KTDGSSSESG SAAIDFFYSS
     VRESEKEDGK VSAKSNLLKD IAHGFYGDEP AGIWQPVKLT ITSPLKVENV FIKPSLDGAT
     FDLTVKNHGT KKNQFNLYTD IVDKETGSVL YSKLSLQKLV LNADEEKMFT YNINGLKPRL
     WTPQHPNLYD FRFRLVAAKG HELDCLTETS GFRTFEVKEG LFFLNGNRYW LRGGNHIPFA
     LAPNDLNLAN TFMQLMKAGN IDVTRTHTTP WNKLWMGAAD KNGIGVSFEG TWPWLMIHST
     PLPDAKLIEM WKEEFLSLLK KYRNHPSLLF WTVNNEMKFY DNDNDLERAK EKYRVISDVV
     KEMRRIDPTR PICFDSNYQA KGKKEKYGAD FMNTIDDGDI DDMHAYYNWY DYSLFRFFNG
     EFQKRFKMVD RPLISQEMST GYPNNETGHP TRSYQLIHQN PQSLIGYECY DFSNPQSFLN
     VQAFITGELA EALRRSNDQA SGIMHFALLT WFRQVYDYQK IEPYPTYYAL KRALQPILVS
     AELWGRNLYG GEKLPTRIYV VNDREDGTDL KPTLLRWEIQ DETGKKLVWG DEELPAVKHY
     GRYYIEPNIQ LPAKLPSNKV NAKLVLKLTE NGLPVSENEY NLLLADKKWN IGQVAENKKI
     VLLDNDGTKA IFDFLRINYQ TVSSVREAVN SKQKADLCVI SGLTNCTEEE KEFLRGYQAK
     GGKLLLLNSK EAAKIIYPEH ITGWIMPTEG DIVNMERNDA PVFDGIGVLE LRYFNNNKRE
     IPTACNATLH VNRNENLTEL AGQMKIHAYI DGGAPEDRIN RINSMRGFTL IQIKDGRGIA
     TVSTMCTEKA ETDPIAGKLL VNMINDLMK
//
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