ID A0A170Z171_9BACT Unreviewed; 958 AA.
AC A0A170Z171;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=PJIAN_1843 {ECO:0000313|EMBL:GAT62250.1};
OS Paludibacter jiangxiensis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae;
OC Paludibacter.
OX NCBI_TaxID=681398 {ECO:0000313|EMBL:GAT62250.1, ECO:0000313|Proteomes:UP000076586};
RN [1] {ECO:0000313|Proteomes:UP000076586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM7 {ECO:0000313|Proteomes:UP000076586};
RA Qiu Y., Matsuura N., Ohashi A., Tourlousse M.D., Sekiguchi Y.;
RT "Draft genome sequence of Paludibacter jiangxiensis strain NM7.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000076586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM7 {ECO:0000313|Proteomes:UP000076586};
RA Qiu Y.-L., Tourlousse D.M., Matsuura N., Ohashi A., Sekiguchi Y.;
RT "Draft genome sequence of Paludibacter jiangxiensis NM7(T), a propionate-
RT producing fermentative bacterium.";
RL Genome Announc. 0:0-0(2017).
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:GAT62250.1}.
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DR EMBL; BDCR01000001; GAT62250.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A170Z171; -.
DR STRING; 681398.PJIAN_1843; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000076586; 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; 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 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.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000076586};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..958
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007904951"
FT DOMAIN 67..203
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 216..309
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 317..433
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 579..640
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|Pfam:PF16353"
FT DOMAIN 695..882
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|Pfam:PF02929"
SQ SEQUENCE 958 AA; 107614 MW; C38662E29AAFA178 CRC64;
MKQLKLKMGL LLVAAFVSVL SIQAQKKSPA VAASTETAIQ YLSGHGSDDA VDWDFFCTDG
RNSGKWSKIK VPSCWELQGF GTYQYGMPFY GKADPPGIAK EQGKYKYKFK LPKEWAGREV
RIVFDGVMTD CEAQINGRKC VGLHQGSFYR FKADVSDRIF FGDKENLLEV TVSKESSNPS
VNLAERRADF WNFGGIIRPV FVEALPAQNI DRTAIDAKAD GSFAADVYLG SGQGSDFKVV
AQLTDKEGKN VGKAIEVPVR GGSDRVKVEG AFSGIKTWSP ETPNLYNVTF SLIQGNIVRH
TVKERFGFRT IEVRPSDGLY INGQKVLVKG VNRHSFRPET GRTLSKKDNY DDVKLIKEMN
MNAVRLSHYP SDPEFLDACD ELGLYVMVEL LGWHGKYDTT VGKKLVNEMV TRDLNHPSVT
WWSNGNEGGF NFDLDGEFAP LDPQKRPVLH PQANFGGFET MHYRSYGESQ EYMRKPEIFM
PTEFLHGLYD GGHGAGLYDY WEMMRKHPRS AGGFLWSFAD EGVVRTDQNG KIDNAGSYAP
DGIVGPHHEK EGSFFTVKQV WAPVQVNVAS LSENFNGVLS VENRYDFINL KNCKFVWKLA
KLPYLKEKQI VASGEIGSPD VAAHASGELK LNLPSDWRKA DVLYLTATDP FGKEIWTWDW
TWKKPTDFFS FAGQKGSVSA REEGDNLIVK TASDELTFSK KSGELVNVLH DGKAVSFGKG
PRFTAARRGD RSMDVFYNHD DKDAKSKERI YNDISGNDRL TAFTFKTTAD SVTVDATYFG
NLQKTHWAIS ADGNIRVDYQ YDYEGEVELM GVKFDYPEDK VVSKQWLGNG PYRVWQNRLH
GTLLDNWQRD YNDPIPGESF EYPEFKGYFA NWKWVNFTTK EGNFALGNDD PDSYLGVFTP
RDGRDAQLFT LPQTGISVLK VIPAMRNKVN STDLIGPSSQ AKWVSGVQKG SIYLKFGK
//
