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Database: UniProt
Entry: A0A0Q5NQU0_9BURK
LinkDB: A0A0Q5NQU0_9BURK
Original site: A0A0Q5NQU0_9BURK 
ID   A0A0Q5NQU0_9BURK        Unreviewed;       657 AA.
AC   A0A0Q5NQU0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
DE            Short=Beta-gal {ECO:0000256|PIRNR:PIRNR001084};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
GN   ORFNames=ASG35_12330 {ECO:0000313|EMBL:KQR77051.1};
OS   Burkholderia sp. Leaf177.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1736287 {ECO:0000313|EMBL:KQR77051.1, ECO:0000313|Proteomes:UP000051826};
RN   [1] {ECO:0000313|EMBL:KQR77051.1, ECO:0000313|Proteomes:UP000051826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf177 {ECO:0000313|EMBL:KQR77051.1,
RC   ECO:0000313|Proteomes:UP000051826};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQR77051.1, ECO:0000313|Proteomes:UP000051826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf177 {ECO:0000313|EMBL:KQR77051.1,
RC   ECO:0000313|Proteomes:UP000051826};
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   -!- 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         ECO:0000256|PIRNR:PIRNR001084};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC       {ECO:0000256|ARBA:ARBA00005940, ECO:0000256|PIRNR:PIRNR001084}.
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:KQR77051.1}.
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DR   EMBL; LMPF01000022; KQR77051.1; -; Genomic_DNA.
DR   RefSeq; WP_056361506.1; NZ_LMPF01000022.1.
DR   AlphaFoldDB; A0A0Q5NQU0; -.
DR   OrthoDB; 9800974at2; -.
DR   Proteomes; UP000051826; Unassembled WGS sequence.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
DR   CDD; cd03143; A4_beta-galactosidase_middle_domain; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR013739; Beta_galactosidase_C.
DR   InterPro; IPR013738; Beta_galactosidase_Trimer.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR003476; Glyco_hydro_42.
DR   InterPro; IPR013529; Glyco_hydro_42_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1.
DR   PANTHER; PTHR36447:SF2; BETA-GALACTOSIDASE YESZ; 1.
DR   Pfam; PF02449; Glyco_hydro_42; 1.
DR   Pfam; PF08533; Glyco_hydro_42C; 1.
DR   Pfam; PF08532; Glyco_hydro_42M; 1.
DR   PIRSF; PIRSF001084; B-galactosidase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR001084};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001084};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051826}.
FT   DOMAIN          6..391
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          405..598
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   DOMAIN          606..652
FT                   /note="Beta-galactosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08533"
FT   ACT_SITE        142
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        315
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         323
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   657 AA;  73819 MW;  1AD163D3FC039265 CRC64;
     MQLGVCYYPE QWPRSMWADD SKRMAEIGIT HVRIAEFAWS RMEPKAGEYV WAWLDEAIET
     LAAAGLRIVL GTPTASPPKW LIDAYPDVLP VRADGTSWNF GSRRHYDITS ASYRRECLRI
     VTEMAGRYGK HPAVVAWQTD NELGCHETVP SYSRQALTRF QAWLEQRYER IERLNEDWGN
     VFWSMEYPSF GAIGLPNLTP TDANPIHLLD FRRFMSAEVA SFHREQVDVL RRLAPAADVL
     HNFMGFFTTF DHYEFVKDKA IDVAAWDSYP IARTESIGLP EEQKALYART SHPDVSAFDH
     DRYRSIGGGR FWIMEQQAGP VNWAPWNPVP AKGMVRLWAL EAFAHGAELV SYFRWRQCPY
     AQEQMHSGLN LPNNELSPGG LEVQEVAREI AASSVLSRLP ATTPADVALI FDYETQWICE
     IQRHGKTFDY QMLAFDYYEA LREMGLDVDI VSAHADLSAY RMVVVPSIAV IDDALVEQIE
     RSSAQWVFGP RSGSKTPQFA LPAGLPPGVL QRVLPMQVLE VESLRSSLAP TTSIGATKGT
     AVHWREHVRA NSDSVVKARF GDEWPAVVAK GRIRYVAGWL THALHRALLE QAANTAGLRV
     TMLPEGVRIR RRGSLTFAFN FGAKTVSSLA PDGAHFVLGT NRLGTGDVCV WENGSAT
//
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