ID A0A1P8M3X2_9MICC Unreviewed; 677 AA.
AC A0A1P8M3X2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=BWQ92_14330 {ECO:0000313|EMBL:APX02730.1};
OS Arthrobacter sp. QXT-31.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1357915 {ECO:0000313|EMBL:APX02730.1, ECO:0000313|Proteomes:UP000186821};
RN [1] {ECO:0000313|EMBL:APX02730.1, ECO:0000313|Proteomes:UP000186821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QXT-31 {ECO:0000313|EMBL:APX02730.1,
RC ECO:0000313|Proteomes:UP000186821};
RA Liang J.S.;
RT "Microbe-microbe interactions indirectly alter the fate of arsenic in
RT presence of MnII.";
RL Submitted (JAN-2017) 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}.
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DR EMBL; CP019304; APX02730.1; -; Genomic_DNA.
DR RefSeq; WP_076800506.1; NZ_CP019304.1.
DR AlphaFoldDB; A0A1P8M3X2; -.
DR SMR; A0A1P8M3X2; -.
DR STRING; 1357915.BWQ92_14330; -.
DR KEGG; arq:BWQ92_14330; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000186821; Chromosome.
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: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}.
FT DOMAIN 30..401
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 413..613
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 622..663
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 166
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 324
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 165
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 332
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 677 AA; 74000 MW; BB150EDD91241F9C CRC64;
MPEHQASSRA PGWNSAPRWN SGPGLAFGGD YNPEQWPADV RREDIGLMKE AGVTLLSVAI
FSWALLEPRE GEYDFGWLDE VLDSLDGAGI KVALATATAA PPAWLVRRHP GVLPVTAEGT
VLERGSRRHY SPSSAAYRRY ATGITRKLAE RYKDHPALAL WHVDNELGCH VSEFYGDEDA
AAFRRWLEQR YGSVEALNEA WGTAFWSQHY ASFQEIIPPR AAPAILNPTQ RLDFQRFSSW
ALLDYYRCLL AVIREVTPDI PATTNLMVSS ATKSMDYFHW AGALDVVAND HYLVAADRER
EIELAFSADL TRGIAGNRPW ILMEHSTSAV NWQPRNQPKM PGEMLRNSLA HVARGADAVM
FFQWRQSVAG AEKFHSAMVP HGGRDTRVWR EVVALGEALG KLGAVKGSTV ESRVAIVFDY
EAWWASELDS HPSMDVKYLD LIREFHRSLF LRGVGVDFVH PAADLTGYDL VLVCTLYCVT
DAAAANIVGA AEAGATVLVS YFSGIVDERD HVRLGGYPGA FRELLGIRTE EFHPLLEDYQ
VALSDGTTGR VWSEHVHAEG AETLATFTGY PLAGVPALTR RATGSGAAWY LATLPDRDGI
ENLLDKLLAE AGVAAVAEAA AGVELTRRVT ADGRRFLFAI NHGRADAAVK ADGEELLGGG
RFAGFVPGGG AAVIAED
//
