ID F3PNC9_9BACE Unreviewed; 1104 AA.
AC F3PNC9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN ORFNames=HMPREF9446_00215 {ECO:0000313|EMBL:EGF59668.1};
OS Bacteroides fluxus YIT 12057.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=763034 {ECO:0000313|EMBL:EGF59668.1, ECO:0000313|Proteomes:UP000003416};
RN [1] {ECO:0000313|EMBL:EGF59668.1, ECO:0000313|Proteomes:UP000003416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12057 {ECO:0000313|EMBL:EGF59668.1,
RC ECO:0000313|Proteomes:UP000003416};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2011) 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|RuleBase:RU000675};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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:EGF59668.1}.
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DR EMBL; AFBN01000005; EGF59668.1; -; Genomic_DNA.
DR RefSeq; WP_009123581.1; NZ_GL882606.1.
DR AlphaFoldDB; F3PNC9; -.
DR STRING; 763034.HMPREF9446_00215; -.
DR eggNOG; COG1621; Bacteria.
DR eggNOG; COG1874; Bacteria.
DR HOGENOM; CLU_007853_0_0_10; -.
DR Proteomes; UP000003416; Unassembled WGS sequence.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd18825; GH43_CtGH43-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR048912; BetaGal1-like_ABD1.
DR InterPro; IPR048913; BetaGal_gal-bd.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR InterPro; IPR019801; Glyco_hydro_35_CS.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF21317; BetaGal_ABD_1; 1.
DR Pfam; PF21467; BetaGal_gal-bd; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW Reference proteome {ECO:0000313|Proteomes:UP000003416};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1104
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003304601"
FT DOMAIN 1003..1104
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
SQ SEQUENCE 1104 AA; 125159 MW; 8FF1BAF1E899D207 CRC64;
MKQKMIRSLA LLVGLFCLLS VKAQMANSSI VPGEVWKDTD GNPINAHGGG LLYHEGTYYW
YGEYKKGKTT LPEWATWECY RTDVTGVSCY SSKDLLNWKF EGIVLPAVKD DEKHDLHPSK
VLERPKVIYN EKTKQFVLWA HVESADYSKA CAGVAVSDSL TGTFTYVGSF RPNGAMSRDQ
TVFVDDNGKA YQFYSSENNA TLYISELTDD YLKPTGRYTR NFVKQSREAP AVFKYNGKYY
MLSSGCSGWD PNVAELAVAD SIMGQWSTIG NPCTGPDADK TFYAQSTYVQ QVYGKGNAYI
AMFDRWKKKD LEDSRYVWLP LEFGKDGKIT IPWHDSWNPR TQWEGQGDFS AGKGTFLLNG
KPFVVKAAEL HYPRIPKAYW DQRIKLCKAL GMNTICLYVF WNSHEPQPGV FDFTGQNDLA
EFCRLCRQND MYVILRPGPY VCAEWEMGGL PWWLLKKKDI RLRESDPYFI ERVGIFEKAV
AEQVADMTIQ NGGPIIMVQV ENEYGSYGED KGYVSQIRDI VRANYPGVTL FQCDWASNFT
KNGLHDLVWT MNFGTGANID QQFAPLKKLR PDSPLMCSEF WSGWFDKWGA NHETRPAADM
IAGIDEMLSK GISFSLYMTH GGTNWGHWAG ANSPGFAPDV TSYDYDAPIS ESGQTTPKYW
ELRKTLSKYM DGEKQAKVPA LIKPIRIPAF QFTEMAPLFD NLPAAKKDRN IRTMEEYNQG
FGSILYRTTL PEMKTSSLLT VNDAHDYAQI FLNGKYIGKL DRRNGEKQLA FPACPKGARL
DILVEAMGRI NFGRAIKDFK GITRSVELTV DIDGHPFTCD LKDWEVYNLE DTYDFYKNMK
FRPIGSLKDE SGQRIPGCYR ATFKVNKPSD TFLNFETWGK GLVYVNGHAM GRIWEIGPQQ
TLYIPGCWLK KGENEVMVFD IIGPKEAKSE GLSEPLLDQL LVTKPLTHRN EGESLDLSGD
HPVFSGSFNP GNGWQERKFN QPVTGRYICL EALNSQDGKD LACIAEMYLL DEHGERLSRE
PWIVNYADSE DVSHANCSAD KLFDLQESTY WSTTKGTPYP HAVVIDLGST RTLTGIQYLP
RMESEVPGGI KDFKVYVKTK NFKY
//
