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Database: UniProt
Entry: A0A0U3SL84_9BACT
LinkDB: A0A0U3SL84_9BACT
Original site: A0A0U3SL84_9BACT 
ID   A0A0U3SL84_9BACT        Unreviewed;       805 AA.
AC   A0A0U3SL84;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:ALW86918.1};
GN   ORFNames=AUC43_18635 {ECO:0000313|EMBL:ALW86918.1};
OS   Hymenobacter sedentarius.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1411621 {ECO:0000313|EMBL:ALW86918.1, ECO:0000313|Proteomes:UP000059542};
RN   [1] {ECO:0000313|EMBL:ALW86918.1, ECO:0000313|Proteomes:UP000059542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG5B {ECO:0000313|EMBL:ALW86918.1,
RC   ECO:0000313|Proteomes:UP000059542};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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DR   EMBL; CP013909; ALW86918.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U3SL84; -.
DR   STRING; 1411621.AUC43_18635; -.
DR   KEGG; hyg:AUC43_18635; -.
DR   OrthoDB; 1007335at2; -.
DR   Proteomes; UP000059542; 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; 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; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR023230; Glyco_hydro_2_CS.
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; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059542}.
FT   DOMAIN          93..198
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          227..325
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          330..512
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          636..698
FT                   /note="DUF4982"
FT                   /evidence="ECO:0000259|Pfam:PF16355"
FT   DOMAIN          712..800
FT                   /note="Glycoside hydrolase family 2"
FT                   /evidence="ECO:0000259|Pfam:PF18565"
SQ   SEQUENCE   805 AA;  89203 MW;  6CE014A35C7A2032 CRC64;
     MPVPSQLSTA VLRSCGGIFL LAALGQCAGQ PGTSGHRTKA PAVITNFNQD WQFVKDVDTT
     VTAALFAKTG GPGQWATVSL PHTPRIEPVV TDQQQWQGVS FYRKFFRVPS DGPYPRVTVE
     FGAAMHTADV YLNGQRLQRH MGGYLPFTVD ISKQVKYSEE NCLVVRLDNR DNPVVPPGKP
     LKGLDFNFYG GLYRTVKLRL CNPLYISDAV QAGHAAGGGL LLHYENISSE SATLHVQTEV
     QNNTSEDQNA QVRTVLFNEK GKEVARGLSE AISMAPAAFG QVKHQLTIAQ PQLWSPEQPY
     LYRVVVEVLR DGKVIDRQQT TTGVRSIKFA AKTLTLNGQP LRLRGTNRHQ EYPYLGYAIS
     DNAQYRDAWK IKDAGFNFVR CSHYPPSPAF LQACDELGLL VMDSTPGWQF FGNEEFAKNS
     MQNIRDMVRR DRNHPSIVLW EAALNETDMP KPFMDAAHRA VHEELPFTEN VYTCGWLDYA
     YDVFIPARQH LKAPDYFNKY AKDKPLFLCE YGDWEYYAHN AGFNQTAFSG LKESERTSRQ
     LRGQGERALA QQALNFQEAH NDNFRGPAVG DANWLMFDYK RGYAPDIESS GVGDIFRLPK
     FAYYFYQSQY GPVADRNGFG KPMAFIANYW QPTSATQVVV YSNCDEVELQ LNGKAVARQR
     PDATAFSDRL ARAPFTFKVP AFAPGTLRAV AYRNGKPAAT AERRTPGAAH HLQLSYDRSG
     RDAGQQDVVF VYAAVVDVNG TVLPEATAAI RFAAQGHAEL VGDNPVRAEA GMATVLLKTG
     LGSGAVQLTA TADGLPSASL KLTIR
//
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