ID   A0A1V1ZHP6_9FLAO        Unreviewed;       847 AA.
AC   A0A1V1ZHP6;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Beta-galactosidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BKM32_06790 {ECO:0000313|EMBL:OMP31612.1};
OS   Mangrovimonas sp. DI 80.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Mangrovimonas.
OX   NCBI_TaxID=1779330 {ECO:0000313|EMBL:OMP31612.1, ECO:0000313|Proteomes:UP000188854};
RN   [1] {ECO:0000313|EMBL:OMP31612.1, ECO:0000313|Proteomes:UP000188854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DI 80 {ECO:0000313|EMBL:OMP31612.1,
RC   ECO:0000313|Proteomes:UP000188854};
RA   Krishnamurthi S., Pal Y., Verma A., Sundharam S.;
RT   "Taxonomic characterization of strain DI 80 closely related to
RT   Mangrovimonas sp.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:OMP31612.1}.
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DR   EMBL; MSDT01000003; OMP31612.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V1ZHP6; -.
DR   Proteomes; UP000188854; 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; 1.
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:UP000188854}.
FT   DOMAIN          6..145
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          164..265
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          272..574
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          673..821
FT                   /note="Malectin"
FT                   /evidence="ECO:0000259|Pfam:PF11721"
SQ   SEQUENCE   847 AA;  97065 MW;  3A54B4906931BCFF CRC64;
     MLGQTKTINS GWQYSEDKVE WQSVNIPHTW NLEDAFDDQP GYRRGLGCYK KQVFIASEEK
     EKIHYLKFNA VNQEATVYVN GKIVGNHKGG YTAFSFNITS LINFDAYNLI EVVVDNSHNE
     NIPPLDADFT FYGGIYRDVE LITLPKQHFS VTDFASDGFY VNYYDVSKEK GGIEVTAILE
     NLATAKTQIQ LKLELLDSEG ANVKSRIESL KLHSGTSNEF KIKLPEIYNP KLWSPETPYL
     YRLKLTLLDE QENVLDYKWT NVGFRWVSVD SEKGFFLNGK PIKLIGVNRH QDYKGYGNAV
     PIELQKKDIE LIKNMGANVI RFAHYPHSRE LYDMCDKLGI LVWTEIPIVN KVTDSKAFFE
     TSITMQKEHI KQYYNFPSVV MFGYMNEIFL RLAFDGKSSE EEKNQLKKVT LDLAQQLENL
     TRDMAPNHLT VMACHLNEVY NETGIADLPM ILGWNLYFGW YDAEIEGLGT FLDDQQRRFP
     KRSMLLSEYG PGADVRIYTR TPKKFDFSTD YQLKLNQSYV QQIKERPFMT GMTAWNFADF
     GSEFRGDAIP HVNQKGLVQY DRTPKDIYYW YKSVLDDAEP FLHIAASNLS GLTLIGENTY
     PVKIFGNQSS ATVYLNDRKL KDIVFMDGVA EVEMPFVNGT NCIMVVSGNR EEVECIEVVK
     ASSLNFEGFD RFGINLGAHF FFTDEAQQIT FVPDQEYVNG EYGYVDGKAY GMTKDKNQGM
     PHNIRNTTSE PLFQTMLEGC SSYKVDLPNG NYRVKLFFVE PQIKPSENIY NLSQSRKETQ
     KQQRVFDVYL NGQLIEKRVN MAQAYPEKYG ITMTSTLEIN NNQGLTVSLK PVEGTPVISG
     LLIEKLN
//