ID A0A085Z0M5_9FLAO Unreviewed; 951 AA.
AC A0A085Z0M5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
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 ORFNames=IX39_16410 {ECO:0000313|EMBL:KFE97988.1};
OS Chryseobacterium formosense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=236814 {ECO:0000313|EMBL:KFE97988.1, ECO:0000313|Proteomes:UP000028713};
RN [1] {ECO:0000313|EMBL:KFE97988.1, ECO:0000313|Proteomes:UP000028713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24722 {ECO:0000313|EMBL:KFE97988.1,
RC ECO:0000313|Proteomes:UP000028713};
RA Pipes S.E., Stropko S.J., Newman J.D.;
RT "Genome of Chryseobacterium formosense LMG 24722.";
RL Submitted (JUL-2014) 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:KFE97988.1}.
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DR EMBL; JPRP01000003; KFE97988.1; -; Genomic_DNA.
DR RefSeq; WP_034678412.1; NZ_JPRP01000003.1.
DR AlphaFoldDB; A0A085Z0M5; -.
DR STRING; 236814.IX39_16410; -.
DR eggNOG; COG3250; Bacteria.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000028713; 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; 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 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.
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}.
FT DOMAIN 42..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 735..849
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|Pfam:PF02929"
SQ SEQUENCE 951 AA; 108385 MW; 9EA0EBD8B586FC2C CRC64;
MSFSSKIFAL LCVCSQLLFS QSKEIQFLTG KDAEHTKEWD FWINSGRKSG SWSKINVPSH
WEQQGFGSYN YGRDYVTYGK NFKFHDETGL YEHKFTVPNS WKGKTINIVF EGSMTDTEVK
INGKLAGEIH EGAFYEFKYD ISDKIQFGKE NILEVKVSKM SADKSVNNAE RLADYWILGG
IFRPVYLEAN SKEHISSTSI DAKADGTFRS DIHLKGINSV NSLKVEIFDV KNNLVGESQV
TIQKGDTLKQ IQFSVKNPKL WTAETPNLYK AKFTLNKNKK TISHTEEKFG FRTIEIRKGD
GIYINGTKIK MKGINRHVWW PETGRAVTEN VDLMDVQLIK EMNMNAVRCA HYPPNKSFLK
ICDSLGLYVL DELAGWQKKY STGVGKKLVK EMVARDANHP SIIFWSNGNE GGHNFDLDSE
YAKYDLSNRP VIHAHHKPGN AFNGIDCNHY EDYYSTKKIL EGENIYMPTE FLHAQDDGGG
GTSLADYWEL HWNSKKGAGG FLWAFVDEGL VRTDFNNQID VNAINAPDGV LGPHREKEGS
FYAIREIYSP VKIDLKTLPN NFNGNIPVEN RYHFTNLKEC QFEWKLIKFK TPFSSESGFD
IIKTGKAESP NIKPTEKGNV NLNLPTNWKE NEGLLLTATD SFGKEIYTWT WKLKSNDEIS
KRFSTSLIKT NQVSVVENDS LFILKSDEKE FAIGKKDGLL KSVIVDKKGK KMTFKNGPVF
VNGTMELSSI KSFAEEQNQL IEVNYKNGNK IIWKLNPNGI LELNYEYSLS GDYPFSGVSF
DYPENYVINS KWLGKGPYHV WKNRTQGQTY NVWQNLKNST RTGFSPWIYP EFKGYFDDVS
WLQLDTAEGK ITVGTKEEKM FVRLFDFYGI YGAEGYPKLP SGNISFLDAI PPLGTVLAFN
INDKTESLGL ESEPNHLNGT FKRTLYFYFG LPDLGDENKQ FTMPKENILT D
//
