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Database: UniProt
Entry: A0A0Q9KXY2_9BACL
LinkDB: A0A0Q9KXY2_9BACL
Original site: A0A0Q9KXY2_9BACL 
ID   A0A0Q9KXY2_9BACL        Unreviewed;       816 AA.
AC   A0A0Q9KXY2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Beta-galactosidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASG81_12315 {ECO:0000313|EMBL:KRE46177.1};
OS   Paenibacillus sp. Soil522.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1736388 {ECO:0000313|EMBL:KRE46177.1, ECO:0000313|Proteomes:UP000051180};
RN   [1] {ECO:0000313|Proteomes:UP000051180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil522 {ECO:0000313|Proteomes:UP000051180};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE46177.1, ECO:0000313|Proteomes:UP000051180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil522 {ECO:0000313|EMBL:KRE46177.1,
RC   ECO:0000313|Proteomes:UP000051180};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KRE46177.1}.
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DR   EMBL; LMRV01000039; KRE46177.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q9KXY2; -.
DR   STRING; 1736388.ASG81_12315; -.
DR   Proteomes; UP000051180; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
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   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR000421; FA58C.
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; 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; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR   Pfam; PF00754; F5_F8_type_C; 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; 2.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          57..155
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          167..270
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          278..446
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          564..658
FT                   /note="Glycoside hydrolase family 2"
FT                   /evidence="ECO:0000259|Pfam:PF18565"
FT   DOMAIN          702..804
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|Pfam:PF00754"
SQ   SEQUENCE   816 AA;  91477 MW;  7A534A7B55A86203 CRC64;
     METGLTKRHQ ALINNDWTFM YGDIAEGKEV LFDDSSWYDI GIPHSFGIPY FMENEFYVGY
     GCYRKHFVIQ QEWLGKSISL DFQGAFQDAD IYVNGQWAGN HKGGYTAFHI DITELVHEGN
     NLLFVRLNNL WNPRLAPRAG EHVFNGGIYR DVSLIVTERV HVAWYGTFVT SSDVSAESAA
     LKVKTEVVNE EVRTADCLLV SVVEYQGTDI CEMRSRHSIA PGQSFEFSQQ QLLVEPMLWH
     PDSPNLYQLK SYVYVDDVLK DEYETNFGVR SIAFDAKEGF FLNGEHYDII GANVHQDHAG
     WGDAVTRAGM ARDVKLIKDC GMNFIRGSHY PHHTHFSAEC DKQGLLFWSE LCFWGIGGAN
     TEGYWASSAY PIHDEDKEEF EASCMRALQE MIRTNRNHPS IITWSMSNEP FFSDAEVMDD
     ARAFIVRLVE ESHRLDASRP ASVGGAQRQG FDVLGDIAGY NGDGASLYID PGVPSFVSEY
     GSVIAVRPGE YAPGYTDGVE RNPRWRSGKA LWCGFHHGSI ASNMGYMGMI DYYRLPLNAW
     YWYRNELLDI APPQPASEGT AYTLRLTADR HVIATDGTDD THIIVEVIDR EGKRISNPLQ
     VELEITHGGG LFPTGKSIRF SPENNSYLDG MGAIEMRSYY AGTIKVEARA EGVRPAEISI
     EAVGGTLWSG QSLRLQPSPP SVMKAPAHGS SYNIARSRPV FCSSYEAGHP AMNVTDDLAD
     TYWKPSNEAE GQWIMVDLEG CKKAEHAVIT FIGTIALSLQ EVFYSLDGKA FFLLEASKHE
     ETNKIIIAEL PSEGLRYLKV VFKEAYAAIK QIEMYT
//
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