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Database: UniProt
Entry: A0A226HX61_9FLAO
LinkDB: A0A226HX61_9FLAO
Original site: A0A226HX61_9FLAO 
ID   A0A226HX61_9FLAO        Unreviewed;       619 AA.
AC   A0A226HX61;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN   ORFNames=B0A75_15170 {ECO:0000313|EMBL:OXA98010.1};
OS   Flavobacterium oncorhynchi.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=728056 {ECO:0000313|EMBL:OXA98010.1, ECO:0000313|Proteomes:UP000198336};
RN   [1] {ECO:0000313|EMBL:OXA98010.1, ECO:0000313|Proteomes:UP000198336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 59446 {ECO:0000313|EMBL:OXA98010.1,
RC   ECO:0000313|Proteomes:UP000198336};
RA   Stine C., Li C., Tadesse D.;
RT   "Whole genomes of Flavobacteriaceae.";
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|RuleBase:RU000675};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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:OXA98010.1}.
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DR   EMBL; MUHA01000024; OXA98010.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A226HX61; -.
DR   Proteomes; UP000198336; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR026283; B-gal_1-like.
DR   InterPro; IPR048912; BetaGal1-like_ABD1.
DR   InterPro; IPR048913; BetaGal_gal-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF21317; BetaGal_ABD_1; 1.
DR   Pfam; PF21467; BetaGal_gal-bd; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PIRSF; PIRSF006336; B-gal; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..619
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013370830"
FT   DOMAIN          33..356
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          398..508
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          528..586
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        181
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        265
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ   SEQUENCE   619 AA;  70503 MW;  47B333F3D831E7FB CRC64;
     MKKVYYTLLF AFFTLLSASA QQKQTFAISG GDFLLNGKPI QIHSGEMHYS RIPQQYWRHR
     LKMMKAMGLN AVATYVFWNY HETAPGVWDF KTGNKNLAEY IKTAQEEGLF VILRPGPYVC
     AEWEFGGYPF FLQNVPNMVI RGNNKEYLAA TKAYFTQLYN QVKDLQITKG GPIIMVQGEN
     EFGSYVAQRK DVPLEEHKKY SAAVFQQLKD LGFEVPFFTS DGSWLFEGGA LPGALPTANG
     ESDIAKLKEV VNKFNNGQGP YMVAEFYPGW LDHWAEPFPT QKPEQTARQT KKYLDNKVSF
     NYYMVHGGTN FGFTSGANYD KEHDIQPDMT SYDYDAPISE AGWATPKYNM LRELLKTSET
     PAIPEKMPII EIPKIALTKT VDLADLKAKI SPVYEDTPQT FEQLNQGDGY VWYSKKFTQP
     ISGKLELKGL RDYAIVYVNG KKVAELNRYY KKYDCEIEVP FNATLDIVVE NMGRINYGSQ
     INENNKGIIS PVIINGQTIT GDWEMYKLPM SQEPDLTAYK NSGKVNRPTL YQGTFTLNKT
     GDTFLDMRDW GKGIVFVNGI NIGRYWSVGP QQTLYLPGCW LKKGKNNIVI FEQKNETLQK
     ELKSITTPIL EDLRPEKGQ
//
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