ID A0A1I0U5V4_9SPHI Unreviewed; 611 AA.
AC A0A1I0U5V4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:SFA59429.1};
GN ORFNames=SAMN04488511_12222 {ECO:0000313|EMBL:SFA59429.1};
OS Pedobacter suwonensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=332999 {ECO:0000313|EMBL:SFA59429.1, ECO:0000313|Proteomes:UP000198836};
RN [1] {ECO:0000313|Proteomes:UP000198836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18130 {ECO:0000313|Proteomes:UP000198836};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR EMBL; FOJM01000022; SFA59429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0U5V4; -.
DR STRING; 332999.SAMN04488511_12222; -.
DR OrthoDB; 703126at2; -.
DR Proteomes; UP000198836; Unassembled WGS sequence.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR026283; B-gal_1-like.
DR InterPro; IPR048912; BetaGal1-like_ABD1.
DR InterPro; IPR048913; BetaGal_gal-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF21317; BetaGal_ABD_1; 1.
DR Pfam; PF21467; BetaGal_gal-bd; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PIRSF; PIRSF006336; B-gal; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SUPFAM; SSF51445; (Trans)glycosidases; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..611
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011755632"
FT DOMAIN 32..347
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 391..500
FT /note="Beta-galactosidase 1-like first all-beta"
FT /evidence="ECO:0000259|Pfam:PF21317"
FT DOMAIN 521..579
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
FT ACT_SITE 180
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT ACT_SITE 255
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ SEQUENCE 611 AA; 69037 MW; AF861A80B9D3C0AF CRC64;
MKAKLLWLVA LCCSLSAFAQ QAKHTFKLGE KEFLLDGKPF QIISGEMHYP RVPKEAWRAR
MKMAKAMGLN TIGTYVFWNL HEPQKGKFDF TGNNNIAEFV KIAQQEGLWV ILRPSPYVCA
EWEFGGYPYW LQTEKGLVVR STEKQYLDEY KKYIIEVGKQ LAPLQINHGG NIIMVQVENE
YGSYAADKNY LDINRKMFIE AGFDGLLYTC DPAADVKDGH LDGLLPALNG IDNPSKIRQL
VNENHGGKGP YFIAEWYPAW FDWWGTPHHT VPAEQYTQKL DSVLAAGISI NMYMFHGGTT
RDFMNGANYK DTSPYEPQIS SYDYDAPLNE AGNVTEKFKA FRSVIEKHLP AGQSLPPIPT
AKPSMAIAPF KLATKVALFN ALPKAVKNNT PLAFEDLSQD YGYVLYRTTI KGGRKGELQL
KQLRDYALVF INQKRVGILD RRLNQNTLSL DLPAGEVQLD IFVENMGRIN FGKYLLENKK
GITEQVTFDG TEIKGWAMYG FPFSNDRVAA SRQSKANGYG PTLQKGSFQI STVADTYLDM
TDWGKGVVWV NGHNLGKYWA IGPQQTLYVP QEWLKKGKNE ISVLELLKPD QNTLKAIDQP
ILNTLKKINL D
//
