ID A0A1Z1WAB9_9ACTN Unreviewed; 648 AA.
AC A0A1Z1WAB9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 Name=bgaB {ECO:0000313|EMBL:ARX83384.1};
GN ORFNames=SMD44_02802 {ECO:0000313|EMBL:ARX83384.1};
OS Streptomyces alboflavus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67267 {ECO:0000313|EMBL:ARX83384.1, ECO:0000313|Proteomes:UP000195880};
RN [1] {ECO:0000313|EMBL:ARX83384.1, ECO:0000313|Proteomes:UP000195880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDJK44 {ECO:0000313|EMBL:ARX83384.1,
RC ECO:0000313|Proteomes:UP000195880};
RA Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Wang C., Yao L.;
RT "Streptomyces alboflavus Genome sequencing and assembly.";
RL Submitted (MAY-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; CP021748; ARX83384.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z1WAB9; -.
DR STRING; 67267.GCA_000716675_03440; -.
DR KEGG; salf:SMD44_02802; -.
DR eggNOG; COG1874; Bacteria.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000195880; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate 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 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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000195880};
KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}.
FT DOMAIN 37..406
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 419..603
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT ACT_SITE 173
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 648 AA; 71644 MW; 9A3148CE15B08786 CRC64;
MTPDGTGGTD GIGGSSDSSG NLDRFYDRLT SLAYGGDYNP EQWGPDVHAE DIELMRAAGV
NLVTLGIFGW ATTEPTPGAY DFTWLDAHLD RLAAAGVAVC LATMTASPPP WLARLHPETL
PVLADGTRLH PGSRQHWCPS SPVFRSHAVR LTERLATRYA DHPALALWHI GNEYGCHISR
HCHCEVSTAA FRDWLRERYG TVDALNDAWS TTFWSQRYGT WEEIHTPRAA PSFRNPAQQA
DFLRFSSDEL LACYLAEKAV LARVTPHTPV TTNFVPVAKT LDLFRWAPHL DVVSYDSYPD
PHDPDAAQRT AFSYDVMRGL KAGQPWMLLE QAPSAVNWRA HNGRKPPGRM RLDSWQAVAH
GADAVLFFQW RQSRGGAEKF QSAMVPHAGP ETRTFREVTE LGAELAAHAD LLRSRPERAD
AALLLDWPNW WALETDAHPS EVDYLEGALA HHKALYDASV ACDVVPVDGD LAAYRLLLVP
HLYSLSLDTA ARLTDYVRGG GTLVVSYFSG ITDEHDRVHL GGYPGPLREV LGLTVEEFDP
RPDGAWAEEI RLEGAEQVLA YDEGGPAVTR HEYGRGTAWY LGLRPDPKTM RELLDRVRAE
AGVSPVVAGL PEGVQVRTRV TAAGERVRLR LDHRDGSVTV ERGQASRQ
//
