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Database: UniProt
Entry: L0FYN9_ECHVK
LinkDB: L0FYN9_ECHVK
Original site: L0FYN9_ECHVK 
ID   L0FYN9_ECHVK            Unreviewed;       610 AA.
AC   L0FYN9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Beta-galactosidase/beta-glucuronidase {ECO:0000313|EMBL:AGA79009.1};
GN   OrderedLocusNames=Echvi_2770 {ECO:0000313|EMBL:AGA79009.1};
OS   Echinicola vietnamensis (strain DSM 17526 / LMG 23754 / KMM 6221).
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Echinicola.
OX   NCBI_TaxID=926556 {ECO:0000313|EMBL:AGA79009.1, ECO:0000313|Proteomes:UP000010796};
RN   [1] {ECO:0000313|Proteomes:UP000010796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17526 / LMG 23754 / KMM 6221
RC   {ECO:0000313|Proteomes:UP000010796};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Echinicola vietnamensis DSM 17526.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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DR   EMBL; CP003346; AGA79009.1; -; Genomic_DNA.
DR   RefSeq; WP_015266561.1; NC_019904.1.
DR   AlphaFoldDB; L0FYN9; -.
DR   STRING; 926556.Echvi_2770; -.
DR   KEGG; evi:Echvi_2770; -.
DR   PATRIC; fig|926556.3.peg.2924; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_009935_3_1_10; -.
DR   OrthoDB; 9801077at2; -.
DR   Proteomes; UP000010796; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 1.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF2; BETA-MANNOSIDASE; 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   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010796};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..610
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003942802"
FT   DOMAIN          106..179
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          217..310
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          352..478
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
SQ   SEQUENCE   610 AA;  69202 MW;  E336885E3D4E173F CRC64;
     MKKSLLLGAG LLLAQSFVWA QDGNWKPAEG KIMTSWAEEV DPANVHQEYP RPQLVREDNW
     QNLNGLWQYK IQAKGEEAPS SFDGEILVPF AVESALSGVG ERVGAEKELW YKTTFDAKKS
     SRERVLLHFG AVDWEAEVFV NGQSVGIHKG GYAPFSFDIT DALEGRKDNE LVVRVWDPSN
     DGPQPRGKQI KNPHGIWYTP VTGIWQTVWT ENVPTSYIAN TKNTPDVDAG TLTVETEIEN
     AESGQMVQVK AFADGQVVAE EKVEAGQPAV LHIDNPQLWE PGNPFLYDLE VSLVKGNRVV
     DATESYAAMR KVSMELDENG VQRMLVNDKF IFQYGPLDQG WWPDGLYTAP NEEALLFDIV
     KTQEMGFNMI RKHVKVEPAR WYYHCDRLGM LVWQDMPSGD MGNQWNPRPG IVGVGTERDR
     TPESEQIFRN EWKEIMDDFH NFPSIIVWVP FNEAWGQFKT EEIVKWTMDY DPSRLVNGAS
     GGNFFPVGQI MDLHNYPEPA MPNPKFFGKD MVITLGEFGG LGLPVEGHTW QEKDNWGYQS
     FKSVEDLENR YAEMMSSLAK LIPRGLSAAV YTQTTDVEVE TNGLMTYDRK VIKLTPEFLK
     KVHEQLYDAR
//
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