ID A0A1M7AC65_9BACT Unreviewed; 1160 AA.
AC A0A1M7AC65;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230};
GN ORFNames=SAMN05720762_1068 {ECO:0000313|EMBL:SHL40270.1};
OS Fibrobacter sp. UWH4.
OC Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC Fibrobacter.
OX NCBI_TaxID=1896210 {ECO:0000313|EMBL:SHL40270.1, ECO:0000313|Proteomes:UP000184331};
RN [1] {ECO:0000313|EMBL:SHL40270.1, ECO:0000313|Proteomes:UP000184331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWH4 {ECO:0000313|EMBL:SHL40270.1,
RC ECO:0000313|Proteomes:UP000184331};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FRAY01000006; SHL40270.1; -; Genomic_DNA.
DR RefSeq; WP_072979605.1; NZ_FRAY01000006.1.
DR AlphaFoldDB; A0A1M7AC65; -.
DR STRING; 1896210.SAMN05720762_1068; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000184331; Unassembled WGS sequence.
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 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; 2.
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; IPR023232; Glyco_hydro_2_AS.
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 InterPro; IPR032312; LacZ_4.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 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 Pfam; PF16353; LacZ_4; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1160
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012252158"
FT DOMAIN 766..1036
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1160 AA; 131831 MW; 7ADB27FF9FE19789 CRC64;
MKNFLVSSAV SCAALFAVFA TSASAQPNDE WNGKPRVFAV NALTPHVTSM PYTTVKEALV
GDRHASEWYQ SLSGKWKFYH VDKPAQRNND FYKDNYDVSG WDDIPVPSSW QLLGYDHPIY
TNVIYPWSQN NRVSAPYAPT DFNPVGHYRR NFTVPEKWAG KRIRLHFEGV ESAYYVWVNG
NYVGYAEDSF TGHEFDINKY LRKGENNVSV QVFRWCDGSW LEDQDFIRLS GIMRDVYIYA
VPEVHIQDFQ IDATLTNNYT DGLLKTTAWI YNSTGSASGD YTVELSLYND KGAEVISPSA
QKVSGIGSKG EKSVHFELPI TKPDRWSAET PNLYTAVLTI KDGSGKIIQV ESNKIGFRKI
EIKKDNGAPR LFVNGMPVKF HGVNRHELDP DNGRAVTYER MEQDIILMKR FNINALRMSH
YPNNPVMYDL CDKYGIYVID EANVESHGAN SELPKNSDDW RAPVVDRLNT MVQRDKNHPC
IILWSLGNEA GNGNVFASER ERAHQIDSTR YVHYEGDNNN ADVTSQMYWG YDYIAGYKDA
NKPVMLCEYE HAMGNSVGDL QEYMDAFYGN PRAFGGFIWD FIDQGLHHKG TPYWEFGGMW
GDWQNDDNFC ANGLVFPDRK IQPEMWEIKY QYSQLRVKNV DAAKGKIEIE NRYLFKNLGD
FLDAYWQIRE DGKVINGGKL NGSQMNIGPN QKKEVTIEMP KIETKIGAEY FLDIDFRLKN
DELWAKAGHS VGHEQFGINL GQLWSTEVDI STVGTHRVIK GSGELTLEGK DFKIRFDENA
GTLASYVLDG DTIIKNGGIP NFWRAPTDND KGFNMEKGHG EWRKASQKRN VSSEVKEVSA
NETQVTFNFS FPDVGSSKMK LTYFVYGSGD IVVEYTFNPD GSKSYIPNVG TLFTVPQGYE
KVRWFGRGPD ENYMGRNRGS FMGIYSTLVD SMTVMYMEIG ETGQRTDVKW ATLTNNDGKG
LMIVGNPRLE FNAQHYTPEQ LTNVKLPWEL KRDKDITLRV DLHQMGLGGI NSWGAEPLNA
YRLNANREYS HKFRIAPIRK QLNDPTEYSL LGFRNFGWND LAPAAYPGDK IYENQPEKDV
AETANKDPNG TDAVKPLVFR TPDSYAPRSY NVFDMQGRLV AKFTTQGIED LQAKTSAAVN
RSGTYLVRSK SGKTFRINVR
//
