ID A0A1K1PXG0_9FLAO Unreviewed; 948 AA.
AC A0A1K1PXG0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN02927921_02110 {ECO:0000313|EMBL:SFW52169.1};
OS Sinomicrobium oceani.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Sinomicrobium.
OX NCBI_TaxID=1150368 {ECO:0000313|EMBL:SFW52169.1, ECO:0000313|Proteomes:UP000182248};
RN [1] {ECO:0000313|EMBL:SFW52169.1, ECO:0000313|Proteomes:UP000182248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12145 {ECO:0000313|EMBL:SFW52169.1,
RC ECO:0000313|Proteomes:UP000182248};
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 -!- 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}.
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DR EMBL; FPJE01000010; SFW52169.1; -; Genomic_DNA.
DR RefSeq; WP_072317328.1; NZ_FPJE01000010.1.
DR AlphaFoldDB; A0A1K1PXG0; -.
DR STRING; 1150368.SAMN02927921_02110; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000182248; 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 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 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:UP000182248};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..948
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012227763"
FT DOMAIN 56..195
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 199..296
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 302..516
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 683..869
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|Pfam:PF02929"
SQ SEQUENCE 948 AA; 108142 MW; 4E5A42489D8BE68D CRC64;
MRRLFLLHLV FCIAIQFPLY AQQEKTTQRL YLSGKGYQDT ETWEFKISDG RNGGTWSTIE
VPSVWEQQGF GKYQYGIKFY GKPHPEGIAD EVGEYKYKFT VPKGWENQRV KIVFDGSMTD
TEVRINGRKA GDKHQGAFYR FQYDISGLLK YGKENLLEVT VSKESENGSV NLAERRADYW
NFGGIFRPVF LEARPAYHID RTAVKAEADG SFEADVFLGE GATGLRAEAV VTDVAGKKKG
VLKGEAVPGS DRIRLSGTFE DIALWTAETP NLYHVDFLLY RGDELLHKVS DRFGFRTIEI
HKGDGIYVNG QRVLMKGVNR HSFWPESGRT LNKELNYADV RLIKEMNMNA VRLSHYPPDP
EFLDACDELG LYVMDELGGW HGHYDDAVGK KLVREMVTRD LNHPCIIFWS NGNEGGWNTN
LDNQFEIWDL QKRPVLHPQQ ELSGVETMHY RSYGETLEYF RGEEIFMPTE FLHGLYDGGH
GAGLFDYWEV MRKHPRSGGG YLWVYADEGI ARTDQGGRID NQGNYAADGI VGPHHEKEGS
FYTIKEVWSP VVVLQDEKLP EDFDGVFTLE NRYDFTNTNQ CTIAWELAAF PAPGDKSAGH
KTITGKTIKG PDIAPHAAGE LQLKLPSDWK KADVLYLKAQ DPEGKELWTW SYTWDKVKKP
VMTEQKKEAA VTETAAYYEV SASGTQIRID RKTGKLLQVW QSGKKIAFGN GPRFIAARRG
DRTLDGTVDK EAAKGEDRIY KEIAYEEKLR HIAVEEKNGE VTVTAGYFGP LQQVRWTVKK
DGTVQLDYDY EYHGIVELVG VSFDYPEDHM EQIRWLGKGP YRVWQNRLHG TTLDVWENEY
NDPVPGESFV YPEFKGYFDQ WRWAVFRTSE GEIRLRNGNP GSYLGVYTPR DGRDALLYTL
PQTGIAVFDV IPAVRNKVNA TDLVGPSSQP QWIEGRKKHT LYLEFKTD
//
