ID A0A0X7BE54_9FLAO Unreviewed; 1038 AA.
AC A0A0X7BE54;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230, ECO:0000256|RuleBase:RU361154};
GN Name=lacZ_3 {ECO:0000313|EMBL:KVV15733.1};
GN ORFNames=AP058_00765 {ECO:0000313|EMBL:KVV15733.1};
OS Flavobacterium sp. TAB 87.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1729581 {ECO:0000313|EMBL:KVV15733.1, ECO:0000313|Proteomes:UP000059935};
RN [1] {ECO:0000313|EMBL:KVV15733.1, ECO:0000313|Proteomes:UP000059935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAB87 {ECO:0000313|EMBL:KVV15733.1,
RC ECO:0000313|Proteomes:UP000059935};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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 ECO:0000256|RuleBase:RU361154};
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, ECO:0000256|RuleBase:RU361154}.
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:KVV15733.1}.
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DR EMBL; LLWK01000031; KVV15733.1; -; Genomic_DNA.
DR RefSeq; WP_066307039.1; NZ_LLWK01000031.1.
DR AlphaFoldDB; A0A0X7BE54; -.
DR STRING; 1729581.AP058_00765; -.
DR PATRIC; fig|1729581.3.peg.800; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000059935; 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; IPR023230; Glyco_hydro_2_CS.
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; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW Reference proteome {ECO:0000313|Proteomes:UP000059935}.
FT DOMAIN 760..1034
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1038 AA; 118130 MW; 345C694970E7A737 CRC64;
MKQTSHLLHV FLLWFIGVNV VQAQTLDPVI ENPAVVGINK LDARATFFPY NSLELAKEDN
VAKAENYLLL NGIWQFSYVD SPELRPVDFF KDTYDTSKWS TIKVPANWEV EGFGIPIYVN
ASYPFQKGEL NPPDIPDGNN PVGSYKRTFD VPKDWNGKDL FIHFGAVKSA FYVWINGEKV
GYSQDSKLPA EFNVTKFVKP GKNTIALEVY RWSDGSYLEC QDFWRISGIE RDVYLYARPK
VQLADYFAKA GLENNYMDGV FDLAVDLKSV DSKKQKGSIS VELTRDNQSI YSTTSAYELN
ANAAGKFNFK QKIPQVKTWS AEIPNLYQLD IVVKDHKGNV VEAISKKVGF RTSEVKNGQY
LVNGRPILFK GVNRHEHDPN TGHVISREDM LKDVKIFKEY NINAVRTAHY PNDPYFYELC
DEYGIYVVDE ANIESHGMGY ALDRTLANNP AWLDAHLQRV DRMVQRDKNH PSIVIWSMGN
EAGNGYNFYQ TYLSAKKIDD TRPIQHERAV HEWNTDLFVP MYDTPEQIEA YAKDKHRTKP
LVLCEYAHAM GNSMGGFKEY WDLFEKYDKL QGGFIWDFVD QGLKVTKNGR EIYAYGGDFG
PKGTPSDNNF LLNGLVQADR TPNPHIHEVA HIQQDVKFYA KDLKKGIVDI KNWYFFRDLS
NYKLNWEVIA NGEVVESGTI DALDIAPQTI KAVRIPFTTQ FKTGVEYFLN VSTILKSDEP
LLKAGYRVAY EQFELQKGLV QVPEKATEAV NFKTKGDVIT VTGKDFQLAF NQKEGTLTDF
NFKNESLLNK GPEVNFWRAP TDNDYGAGTQ KSYKAWKDAG TSGAVTANVK QLSKTEVQIM
FVRTLFNGDA TLTETFVVDG NGAVKVTNDL KALKGKHTDF YKFGNKLVLP ETYKNITFYG
KGPFEAYTDR QHAAKVGLYK QTIAEQYFGY LRPQENGNKL ETRWVALTKE NGSGLKFISE
TPFSASALNF KEEDLHSGDD RAQEHAGEID PRKEVFVNID GFQQGLGSIN SWGTLPLPEY
RLNYKDYSYS YWMVPIVK
//
