ID A6LH37_PARD8 Unreviewed; 746 AA.
AC A6LH37;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN OrderedLocusNames=BDI_3296 {ECO:0000313|EMBL:ABR45001.1};
OS Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS 5825 / NCTC 11152).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=435591 {ECO:0000313|EMBL:ABR45001.1, ECO:0000313|Proteomes:UP000000566};
RN [1] {ECO:0000313|EMBL:ABR45001.1, ECO:0000313|Proteomes:UP000000566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152
RC {ECO:0000313|Proteomes:UP000000566};
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC in beta-D-galactosides.; EC=3.2.1.23;
CC Evidence={ECO:0000256|ARBA:ARBA00001412};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000140; ABR45001.1; -; Genomic_DNA.
DR RefSeq; WP_008779094.1; NZ_LR215978.1.
DR AlphaFoldDB; A6LH37; -.
DR STRING; 435591.BDI_3296; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR PaxDb; 435591-BDI_3296; -.
DR KEGG; pdi:BDI_3296; -.
DR PATRIC; fig|435591.13.peg.3257; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_417794_0_0_10; -.
DR BioCyc; PDIS435591:G1G5A-3383-MONOMER; -.
DR Proteomes; UP000000566; Chromosome.
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; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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 PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 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 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, ECO:0000313|EMBL:ABR45001.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABR45001.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000566};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..746
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002698918"
FT DOMAIN 88..190
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 236..312
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 318..457
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 746 AA; 86630 MW; C1A1062C2E94C7DE CRC64;
MKRIILIMCC FLSVFAWADD GRTTISLNGE WDFDQTEHAF PPRKYTRKIP VPGLVHLARP
KISQYEKFFK KPDGVELVEQ FNFLERDYTP MYNWYKRKVF IDEKFKDEQL FLTIKKSQYV
TRVFVNGHQV GSSMECYTPM DFNITSAVKY GSDNEILIQV GDRAWLPSEA AGGTDKEKVH
YLPGIWDDVF ITATGKMRVD KILFLPSLAK GLVTVKTLVR SLYPPQMLYG DKMKDSCKIE
FCVKEKTTGQ VVGKKVIEGE VKRDNRTYFE TSISLDNPKA WTPDSPFLYE GEVSVYDQDE
LVDRYSVNFG MRDFSRKGKF FTLNGDKFYL RGSNITLQRF FEDPDCQALA WDREWVKKLM
IDLPKSIDWN AMRICVGIVP DFWYDLCDEY GIVLQNEWLY WQNHGWDEQV RKEYTNWVWS
DGNHPSIVIW DAINENWDSY IGNTLIPELK ELDPTRIWDA GYMTSDQMGT NDEMDEPHPY
RALTLMHSSE LNDYFKNNPY NLGALHENWV GFSSILDAGV PQLVNEYGWI WLWRDGRPSK
LTLNNYNYYL GENATPAQCR ELQAYWLQLE TEWLRSERSV GGILAFCHLT NNYGFTGDWF
INDIKDLQPS PAFRWFKHCF APTAVFIDLT DHRYTKHLPA LKPGSDLVFN LVGVNDLNKD
SSGKVLLKLL DEKGTIISTQ EESIVIEPFG KRLQPCLLKL PSKAGGYLLI AEYHEKGGAK
PVLSRRYLKV GDAVTSFKDY FEYTLN
//
