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Database: UniProt
Entry: A9ECS4_9FLAO
LinkDB: A9ECS4_9FLAO
Original site: A9ECS4_9FLAO 
ID   A9ECS4_9FLAO            Unreviewed;       852 AA.
AC   A9ECS4;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:EDP94304.1};
GN   ORFNames=KAOT1_04105 {ECO:0000313|EMBL:EDP94304.1};
OS   Kordia algicida OT-1.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Kordia.
OX   NCBI_TaxID=391587 {ECO:0000313|EMBL:EDP94304.1, ECO:0000313|Proteomes:UP000002945};
RN   [1] {ECO:0000313|EMBL:EDP94304.1, ECO:0000313|Proteomes:UP000002945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT-1 {ECO:0000313|EMBL:EDP94304.1,
RC   ECO:0000313|Proteomes:UP000002945};
RX   PubMed=21622754; DOI=10.1128/JB.05241-11;
RA   Lee H.S., Kang S.G., Kwon K.K., Lee J.H., Kim S.J.;
RT   "Genome sequence of the algicidal bacterium Kordia algicida OT-1.";
RL   J. Bacteriol. 193:4031-4032(2011).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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:EDP94304.1}.
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DR   EMBL; ABIB01000020; EDP94304.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9ECS4; -.
DR   STRING; 391587.KAOT1_04105; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_006501_5_0_10; -.
DR   Proteomes; UP000002945; Unassembled WGS sequence.
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; 2.60.120.430; Galactose-binding lectin; 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; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006101; Glyco_hydro_2.
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   InterPro; IPR021720; Malectin_dom.
DR   PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF1; 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   Pfam; PF11721; Malectin; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
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:UP000002945}.
FT   DOMAIN          12..153
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          168..272
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          280..581
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          680..815
FT                   /note="Malectin"
FT                   /evidence="ECO:0000259|Pfam:PF11721"
SQ   SEQUENCE   852 AA;  98834 MW;  42D6AB12C5D9782E CRC64;
     MCVAFFFLSH GQSKTINSGW QYSEDKTNWQ TVNIPHTWNV KDAFDDVAGY RRGLGFYQKQ
     LFVSSKEKDQ IFYLKFNAVN QEATVFVNGK KVTNHKGGYT AFTTEITSHI NFDSYNIIEV
     EVDNSHNENI PPLDADFTFY GGIYRDVELI KVPKQHFSLK DFASDGFYVN YDNVSNEKAG
     VNVTVLIDNF DEKTNTNVDL TIVDAENNLI TEKHQKAKLN AKESKTIKVT FPEIKNPKLW
     SPDDPYLYKL QLTLRDTNGI ILDQKYANIG FRWTTIDSEN GFFLNGKPLK LIGINRHQDY
     KNYGNAVPIE LQKQDIHLIK NMGANVIRFA HYPHARELYK LCDELGILVW TEIPIVNKVT
     DSEAFFEVST TMQKEHIKQY YNYPSVVMFG YMNEIFLRLA FDRKSTKEEK EALKKTTLKL
     ANQLEELTRK LAPNHITVMA GHLNEVYNET GIADVPMLLG WNLYFGWYDA QIEDLGTFLD
     DQHQRYPNRS LLLSEYGPGA DVRIFTKTPK KFDFSTNYQA KLHQSYYKQI TNRPFMTGMT
     AWNFADFGSE FRGDAIPHVN QKGLVQYDRT PKDIYYWYKS VLDTKEPFIH IATDNLKKLT
     LLEDETFPIQ IYSNQPSISV FLNGEKYREY SLENGFVSVD LPLQNGQNRI EVMTHEVYEE
     KYVHINRIKT FDFENFKRFG INIGSHLYFY DEEQNITFVP DQVYKKGWFG YKNGTAYGIT
     KDKNQGLPHN IKNTDAEPLF QTLLEGCNEY KMDVPEGNYK VILYFVEPQI KPTENIYNLS
     KNTATIDKKQ RIFDVYINEK LIEKQLNLAQ AYPEKYGVTL QTKIQTKKGL TLKLNAIEGL
     PVISGILIEK LD
//
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