ID A0A1A7KFT8_9FLAO Unreviewed; 951 AA.
AC A0A1A7KFT8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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|RuleBase:RU361154};
GN Name=lacZ {ECO:0000313|EMBL:OBW40743.1};
GN ORFNames=AB670_02907 {ECO:0000313|EMBL:OBW40743.1};
OS Chryseobacterium sp. MOF25P.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1664318 {ECO:0000313|EMBL:OBW40743.1, ECO:0000313|Proteomes:UP000092708};
RN [1] {ECO:0000313|EMBL:OBW40743.1, ECO:0000313|Proteomes:UP000092708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MOF25P {ECO:0000313|EMBL:OBW40743.1,
RC ECO:0000313|Proteomes:UP000092708};
RA David V.-J., Thomas B., Ramon P.Y., Thao N., David R., Richard E.,
RA Roderick C., Nikki M., Timothy W.J., Alexander A.E., Kimberley T.;
RT "A floR containing integrative conjugative element found in multidrug
RT resistant Chryseobacterium spp. isolates: exception to the general rule?";
RL Submitted (JUN-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:OBW40743.1}.
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DR EMBL; LFEG01000098; OBW40743.1; -; Genomic_DNA.
DR RefSeq; WP_066679712.1; NZ_LFEG01000098.1.
DR AlphaFoldDB; A0A1A7KFT8; -.
DR PATRIC; fig|1664318.4.peg.2976; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000092708; Unassembled WGS sequence.
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; 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; 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; 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.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 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:UP000092708}.
FT DOMAIN 52..188
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 204..292
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 295..515
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 568..630
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|Pfam:PF16353"
SQ SEQUENCE 951 AA; 108584 MW; 00D6B6E6579FFADB CRC64;
MSCFSKIFVL LCLCSQLLHS QSKEIQFLSG KDSEHTKEWD FWINGGRKSG NWDKIQVPSQ
WEQQGFGSYN YGRDYVTYGK NFKFNDEVGL YKHQFLVPNS WKGKTINIVF EGSMTDTEVK
INGRSAGAIH QGAFYEFKYD ISDKLIFGKE NILEVKVSKI SADKSVNNAE RLADYWILGG
IFRPVYLEAT SKEHISWTAI DAKADGTFRS NIHLKGINSA NNLQVEIFDI KNNLVGESQI
QIKKDDTLKQ IQFSVKNLKL WTAETPNLYK AKFTLNKNRK TIFQSEEKFG FRTIEIKKGD
GIYINGTKIK MKGINRHVWW PETGRAVNEN IDLMDVQLIK EMNMNAVRCS HYPPNKSFLK
ICDSLGLYVL DELAGWQKKY STEVGEKLVK EMVVRDANHP SIIFWSNGNE GGHNFDLDAE
FAKYDLSNRP VIHAHHKPGN AFNGIDCNHY EDYYSTQKIL EGENIYMPTE FLHAQDDGGG
GTSLADYWEL HWNSKKGAGG FLWAFADEGL VRTDFNNQID VNAINAPDGV MGPHREKEGS
FYAIREIYSP VKIDLKTLPN DFNGIIPIEN RYHFTNLNEC KFEWKIVKFK TPFSSESGSD
VIKTGKAESP NIKPTEKGNI NLNLPSNWKE SEGLLLTAID KFGKEIYTWT WKIASNDGIS
KQFSKSLLKE FPISVIENDS LFILKSDEKE FAIGKKDGLL KSVIVDKKGK KMTFKNGPVF
VNGTMELSSI KSFAEGQNQL IEVNYKNRNK IIWKLNPNGI LELNYEYSLS GDYQFSGVSF
DYPENYVINA KWLGKGPYHV WKNRTQGQTF NVWQSLKNST RTGQSPWIYP EFKGYFDEVS
WLQLDTAEGK ITVGTKEEKM FVRLFDFYGI YGAEGYPKLP TGNISFLDAI PPLGTVLAFN
INDKTETLGP ESEPNHLKGT FKRTLYFYFG LPDLGDENKQ FTMPKENILT D
//
