ID   A0A238V876_9FLAO        Unreviewed;       812 AA.
AC   A0A238V876;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:SNR30401.1};
GN   ORFNames=SAMN04487979_102152 {ECO:0000313|EMBL:SNR30401.1};
OS   Flavobacterium sp. ov086.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1761785 {ECO:0000313|EMBL:SNR30401.1, ECO:0000313|Proteomes:UP000198291};
RN   [1] {ECO:0000313|EMBL:SNR30401.1, ECO:0000313|Proteomes:UP000198291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV086 {ECO:0000313|EMBL:SNR30401.1,
RC   ECO:0000313|Proteomes:UP000198291};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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; FZNL01000002; SNR30401.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238V876; -.
DR   OrthoDB; 9801077at2; -.
DR   Proteomes; UP000198291; 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; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR032311; DUF4982.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR040605; Glyco_hydro2_dom5.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR023232; Glyco_hydro_2_AS.
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; IPR008964; Invasin/intimin_cell_adhesion.
DR   PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF16355; DUF4982; 1.
DR   Pfam; PF18565; Glyco_hydro2_C5; 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; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          41..188
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          204..304
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          312..516
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          631..690
FT                   /note="DUF4982"
FT                   /evidence="ECO:0000259|Pfam:PF16355"
FT   DOMAIN          703..804
FT                   /note="Glycoside hydrolase family 2"
FT                   /evidence="ECO:0000259|Pfam:PF18565"
SQ   SEQUENCE   812 AA;  92321 MW;  BF46EAFA21C22D1E CRC64;
     MNRLNSYKKQ YFAKQIVFLF ILFISFFSGY AQNSMERKQL FDYNWKFFLG DDAEAKTSNF
     NDTSWRNLDL PHDWSIEGKI HPKNTTGAGG GYFPSGIGWY RKTFQVSDEM KAKKTAIYFE
     GVYMNSEVFI NGKSLGVYPY GYSSFSYDLT PYLIFGKENV IAVRVDNSQQ MNSRWYSGSG
     IYRHVWMMVT DPVHVTNWGV AISTPEVSSK KAVVLVKTKV KNETESAQSI VVKTVLSNNT
     SKNIGNGQMQ IELPAHSEKE ITQTIQVSNP KLWTPETPFL YQAQIQIVKD KKVVDNTKTN
     FGIRSIKFTA ENGFQLNGKT VKINGGCVHH DNGCLGAAAF DRAEERKVEL LKAGGFNAVR
     TSHNPPSEAF LEACDRLGLL VMDESFDCWK IGKNSNDYAK YFEQWWKKDL QAMILRDRNH
     PSIVMWSIGN EIVERGKPEA VETAKMLMQE VKKIDTTRPV TSAVVNLDKW ENLDSLINVH
     DVAGYNYNLN TAPDDHKRVP SRIIVQTESY PKDAFNNWKL VQENNYVIGD FVWTAMDYLG
     ESGIGRWYYS GEVPGQHWEN DFFPYHGAYC GDIDLLGWRK PISHYRSMLY NNNEKLYMAV
     REPAPEPLEI KETWWSVWPT WESWTWPVFE GKTVQVEVYS KYPKVRLYLN DKLVGEQKTS
     KEEQFKATFS IPYSPGLLKA VGVENDKEVA STILQTAGDA AKIKLTADRN EILANGQDLS
     YITIEITDKD GIFQPNAANR LDFKIEGPGV IAGVDNADIK DTEQYVGSTR KAWHGRALVV
     IKSNHEAGEI KLSVIPNGLE AKSIVIKSKH NN
//