ID A0A168FDY6_9MICO Unreviewed; 681 AA.
AC A0A168FDY6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=I598_1939 {ECO:0000313|EMBL:ANC31486.1};
OS Isoptericola dokdonensis DS-3.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Isoptericola.
OX NCBI_TaxID=1300344 {ECO:0000313|EMBL:ANC31486.1, ECO:0000313|Proteomes:UP000076794};
RN [1] {ECO:0000313|EMBL:ANC31486.1, ECO:0000313|Proteomes:UP000076794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-3 {ECO:0000313|EMBL:ANC31486.1,
RC ECO:0000313|Proteomes:UP000076794};
RA Kwon S.-K., Kim J.F.;
RT "Complete genome sequence of a soil Actinobacterium, Isoptericola
RT dokdonensis DS-3.";
RL Submitted (JAN-2016) 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; CP014209; ANC31486.1; -; Genomic_DNA.
DR RefSeq; WP_068202777.1; NZ_CP014209.1.
DR AlphaFoldDB; A0A168FDY6; -.
DR STRING; 1300344.I598_1939; -.
DR KEGG; ido:I598_1939; -.
DR PATRIC; fig|1300344.3.peg.1946; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000076794; 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, ECO:0000313|EMBL:ANC31486.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:ANC31486.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076794}.
FT DOMAIN 17..384
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 397..607
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 615..670
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 153
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 309
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 681 AA; 73668 MW; 9223696F34290E0D CRC64;
MAVTTWPTGS ALGYGGDYNP EQWPRETWDA DVALMAEAGV NFVSVGIFSW AMLEPREGEH
DFAWLDELLD LLHSRGIMVD LATPTAAPPA WFFATYPEAR VVTRDGVPMG PGSRGAASPS
HPAYQRAARD IASRIAERYA DHPAVVMWHV HNEYGAPVGE DFSEAALTAW RIWLRQRYGT
LDGLNAAWGT KFWGQVYGEW EHVMLPGPTP SVRNQAQVLD FARFTDHQLR ALFVAERDAI
RRYSDKPVTT NFMANECPTT DLWAWAREVD VVSNDHYLTA ADPRAHVGLA LAADLTRSVA
GGRPWILMEH SSSGVNWQPR NIAKRPGEMA RNSLSHVARG ADVVGFFQWR ASRVGAEKFH
SAMLPHAGTD SRVWREVVDL GAHVGALAPV QGSTVRADVA LLWDTESHWA QDQEWRPSVD
LTHRERTRAY YERLWRDGVT TDFAHPEADL SGYRLVVAPA SYLLTAAAAA NLTRYVEAGG
TLVVSCFSAV VDEHDAVHAG GFAAPLRDVL GVRVQEFLPL REAESTKVAW SGSAESAGRT
LAASVWHEHV TPVGAETVAT HLDGPAAGMP AVTRNAHGAG HAWYVATVLD VTELATVLGD
VYADAGVTPS GLAEDLEVVV RRADDADYTF AINHTDSPAV VPGVTGTALG DGTDVGPDLT
VPAGDVVVVR TPATPGGDPA S
//
