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Database: UniProt
Entry: A0A0S9DBN6_9MICC
LinkDB: A0A0S9DBN6_9MICC
Original site: A0A0S9DBN6_9MICC 
ID   A0A0S9DBN6_9MICC        Unreviewed;       690 AA.
AC   A0A0S9DBN6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=ASF21_02950 {ECO:0000313|EMBL:KQO03284.1};
OS   Arthrobacter sp. Leaf234.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1736303 {ECO:0000313|EMBL:KQO03284.1, ECO:0000313|Proteomes:UP000053418};
RN   [1] {ECO:0000313|Proteomes:UP000053418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf234 {ECO:0000313|Proteomes:UP000053418};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf234 {ECO:0000313|Proteomes:UP000053418};
RA   Vorholt J.;
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:KQO03284.1}.
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DR   EMBL; LMLU01000001; KQO03284.1; -; Genomic_DNA.
DR   RefSeq; WP_055766561.1; NZ_LMLU01000001.1.
DR   AlphaFoldDB; A0A0S9DBN6; -.
DR   STRING; 1736303.ASF21_02950; -.
DR   Proteomes; UP000053418; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF1; BETA-GALACTOSIDASE GANA; 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.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR001084};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001084};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT   DOMAIN          42..408
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          423..624
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   DOMAIN          632..685
FT                   /note="Beta-galactosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08533"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        178
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        335
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT   BINDING         343
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   690 AA;  75635 MW;  4530370EEBC94728 CRC64;
     MSLDQSEATG AAVTTTAVPA TSTAPATRSW PGGTQKLRYG GDYNPEQWPR DTWLEDIALM
     QQTGINLVSI GIFSWALLEP RDGEFDFTFL DDIMDLLASA GIDVDLGTPT AAPPAWFWKK
     YPQARPVTRE GVQLGHGSRG MASPSSPDYR RHAARITGEL ARRYAGHPAL RLWHVHNEYG
     APISECYSDA SVVAFREWLG HRYGSLDAVN DAWGTTFWGQ RYGSWEEIDA PRLSATVVNP
     AQRLDFKRFT SDSLLECYVL ERDTIREYTP DLPVTTNFMA TSCPSLDYWS WAREVDVVAN
     DHYLTAERTD NHVLLALDAD FTRSLAGGKP WMLMEHSTSA VNWQPRNIAK RPGEMTRNSL
     GHVARGADAV MFFQFRASRS GAEKFHSAMV PHQGTDSRIF REVTELGHLL GRSSAVRGST
     VDARVAILWD QQSFWAQDLE WRPSEDLDHR ERIEAWYTAL WQRNVTVDFA HPEQDLGHYD
     LVLAPALYAV SAAARENLEA YVAEGGNFVV SFFSGIVDDH DAVPAGGHPG QLRAVLGLTV
     AEWLPLRRHE TVTLDDGSSA DIWAEDIELH GARTRTSYTS GPAEGQAAIT VNTFGKGTAW
     YVSTRPTSGT LDALLGEALA ATGIPDGPST PGVETVTRTG DGVTFTFVLN HTDVDAPLPV
     GGSDLVSGRT VSAGELLAAG ACAVIEKQEK
//
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