ID A0A0Q0VDY2_9SPHI Unreviewed; 901 AA.
AC A0A0Q0VDY2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Beta-galactosidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AQF98_10975 {ECO:0000313|EMBL:KQC01176.1};
OS Pedobacter sp. Hv1.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1740090 {ECO:0000313|EMBL:KQC01176.1, ECO:0000313|Proteomes:UP000050543};
RN [1] {ECO:0000313|EMBL:KQC01176.1, ECO:0000313|Proteomes:UP000050543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hv1 {ECO:0000313|EMBL:KQC01176.1,
RC ECO:0000313|Proteomes:UP000050543};
RA Ott B.M., Beka L., Graf J., Rio R.;
RT "Draft Genome Sequence of a Pedobacter sp. Strain Hv1, an Isolate From
RT Medicinal Leech Mucosal Castings.";
RL Submitted (OCT-2015) 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:KQC01176.1}.
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DR EMBL; LLWP01000004; KQC01176.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q0VDY2; -.
DR STRING; 1740090.AQF98_10975; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000050543; 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; IPR032311; DUF4982.
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; PF16355; DUF4982; 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:UP000050543};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..901
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006185208"
FT DOMAIN 39..183
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 207..307
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 315..617
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 646..699
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 766..885
FT /note="Malectin"
FT /evidence="ECO:0000259|Pfam:PF11721"
SQ SEQUENCE 901 AA; 101798 MW; CA656C6C942DBE8D CRC64;
MYQATCLKKI IPFLLFFAFS STFAQKPKDI LPARISVNLN QNWSFAKDPS KQVSSLNLKD
LKWAVVHIPH TWNAFDVMDD VPGYYRGIGW YKKKLSLKPE WKNKKIYLYF EGANQETTVY
LNGKKAGYHV DGYNAFRIPL ENLKFDGSDE VAVKVDNSFN ESIAPLTADF TFFGGIYRNV
SLWVLQPVHF EDNLYASKGV YVHGDRVSKT GAEVVVNGNL INSSKTVKKL SIVTTFSDAA
GKKIEEVKSS VTADLNQLIS FKQPVIAVKQ PNLWSPENPY LYQASTRLLE AETGKVLDEV
KVSVGLRFFS FDAEKGFFLN GMPYKLIGAS RHQDFEGMGN AVPSALQVKD ITLLKGVGGN
FLRVAHYPQD QAVLDACDRM GILTSVEIPI VNEITETEDF YRNSRNMQLE MIKQNYNHPS
VIIWAYMNEV LLKMKFNNDP ERKQKYLTNI ATLAQSLEDL TRATDPTRYT MMANHGDING
YTKAGLTKIP MLIGWNLYQG WYGGKSEDFG PNLDKIHQLM PDKPILVTEY GADADPRIHA
AEPIRFDKSL EYAMLYHQIY IKDILKRPFV AGAAVWNLSD FNSETREETM PHVNNKGLLT
LSRKPKNTFY LYKANFQTKP FVKIGDGSWT LRGGLANTGA NQSIQRLQVI SNTDTVELWV
NGKSLGKKNT VERLSNWEVA FKNGKNEIRA VSFVNGVKIE DRSTIEFQVI PKALANFKAI
NIVLGSQRQF IDEQKQEIWF PSQPYQPGSW GHNGGEAFKI KNSGRQSYGT DKNIRGTFND
PIYQTQLLGL ESYQLDVPKG KYEVTLHFAE LMGNGIQSVL PYNLDSLIAV SKDVPEQRIF
DVYLNDKLVI KNINIAATYG IANSVQKKFE CIVADDRGIK ILFKSIKGKP VLNALQVKKI
N
//
