ID I9EEF4_9BACE Unreviewed; 994 AA.
AC I9EEF4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=HMPREF1061_03272 {ECO:0000313|EMBL:EIY18359.1};
OS Bacteroides caccae CL03T12C61.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=997873 {ECO:0000313|EMBL:EIY18359.1, ECO:0000313|Proteomes:UP000002965};
RN [1] {ECO:0000313|EMBL:EIY18359.1, ECO:0000313|Proteomes:UP000002965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL03T12C61 {ECO:0000313|EMBL:EIY18359.1,
RC ECO:0000313|Proteomes:UP000002965};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Zitomersky N.L., Coyne M.J.,
RA Comstock L.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Bacteroides caccae CL03T12C61.";
RL Submitted (FEB-2012) 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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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:EIY18359.1}.
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DR EMBL; AGXF01000016; EIY18359.1; -; Genomic_DNA.
DR RefSeq; WP_005682027.1; NZ_JH724079.1.
DR AlphaFoldDB; I9EEF4; -.
DR GeneID; 75112073; -.
DR PATRIC; fig|997873.3.peg.3410; -.
DR HOGENOM; CLU_009998_0_0_10; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000002965; Unassembled WGS sequence.
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 GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 2.70.98.10; -; 1.
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; 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; 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 PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..994
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003720133"
FT DOMAIN 74..181
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 184..286
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 288..497
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 994 AA; 113460 MW; D69ED819B71436B8 CRC64;
MKTKKTLAMV GIFLFLAIRP SVASSFTERT YLLPTRLEGS CRPVLLLSGT WDFKYSPESR
WTSIQVPGEA AMQGFAIEHD KPFFYKKDFT IPADYAGKRL ILRFDGVYSH ARLSVNGKFV
REHHGGFTRW ETDITSFVRI GKKNEIQLAV VDRLDEISYA SGYAHHPIGG ILRDVTLFAL
PESHLYDIGV ETHLDSLYQD ADLRFFCKFS GQESTEMELR LKDKSGKYVP LSQSRFALSD
GQNIFSLPVK NPLKWDAEHP NLYELEIIVF QNGQETSRFS RNIGFREVKI IKDRMLVNGH
QVKLRGACRH DIHPTLGRTT TLELDSLDAV LFKQANMNFV RTSHYPSTER FLEFCDRYGI
YVESETAVCF VDTYRQKNYK PGRSQNDPAF AERYLGQCRE MVKSLRSHPS ILFWSIGNES
VYGSNFQLCW DWIKATDTTR PVIFSYPGSA VEKKAEIFDI LSMHYQNVYG NVGQWGMATR
NFQGHGIPAL FDEWAHPACY TYATLQTDPN IREFWGKSLD MMWSGLFNAP GGLGGAIWGY
VDETFSLPEP KFGTSFWKEF ARTAKPLDYQ GNCVGYGEWG IVDVWRRQKP EFWSTKKAYS
PVRLLVEDNL SFTTGQELML TIHNRFDHTN LNEIHATYTY RGVTKSLELQ PVAPHTKGMI
VIPAEQWENG ETLQVEFFTA ANELIDVYRF VLGTEKIIYP SLLAGQNLSV TDEGDKVIVH
GNGFEIPFDK ETGLIVNATV GGEVIIEKGP FLNLYVNLNH LTGAEVRKTA NHFATSDIDW
KKKSFDYSQQ KDGVCISLTG TYREVNVDFD IKVTSAGELS INYRTEGVPN GFLRETGLSF
YLPHSIHQLN WRRKGYWNYY PVGAFAGNEG EASLYESQQK GYGEKPVQSW QVDTHNYYYW
ADAGANCKEP LTQMAKGMKE NIYYYSLSTG AEGEHQLSVI SQDASVACRI NKCANEQLIL
YANNRWDYPE IAWGNYCKTL EVLPCYGRID IRVR
//
