ID A0A085FPY1_9BURK Unreviewed; 783 AA.
AC A0A085FPY1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN ORFNames=FG94_01304 {ECO:0000313|EMBL:KFC73526.1};
OS Massilia sp. LC238.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1502852 {ECO:0000313|EMBL:KFC73526.1, ECO:0000313|Proteomes:UP000028601};
RN [1] {ECO:0000313|EMBL:KFC73526.1, ECO:0000313|Proteomes:UP000028601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC238 {ECO:0000313|EMBL:KFC73526.1,
RC ECO:0000313|Proteomes:UP000028601};
RA Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT isolate.";
RL Submitted (JUN-2014) 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|RuleBase:RU000675};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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:KFC73526.1}.
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DR EMBL; JNNN01000030; KFC73526.1; -; Genomic_DNA.
DR RefSeq; WP_036208659.1; NZ_JNNN01000030.1.
DR AlphaFoldDB; A0A085FPY1; -.
DR STRING; 1502852.FG94_01304; -.
DR PATRIC; fig|1502852.3.peg.1278; -.
DR eggNOG; COG1874; Bacteria.
DR OrthoDB; 9813184at2; -.
DR Proteomes; UP000028601; Unassembled WGS sequence.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR048912; BetaGal1-like_ABD1.
DR InterPro; IPR048913; BetaGal_gal-bd.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR InterPro; IPR019801; Glyco_hydro_35_CS.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF21317; BetaGal_ABD_1; 1.
DR Pfam; PF21467; BetaGal_gal-bd; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675}.
FT DOMAIN 677..783
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
SQ SEQUENCE 783 AA; 86816 MW; 970EADD3B3698AD8 CRC64;
MPLHPSRRTF LGAAAGTALA LNVPSTTAAS PRFAIGDKDF LLDGKPLQIR CGEMHFARVP
REYWGHRLKA IKAMGLNTVC AYLFWNYHEW REGRYRWEGQ RDATEFCRMA QAEGLWVILR
PGPYACAEWE MGGLPWWLLK HPGDSFLRSR APAFVEPARR WLKEVGRVLA PMQVSQGGPI
LMVQVENEYG FFGDDRDYMR DMRQALLDAR FDVPLFQCNP TNAVAKTHIP ELLSVANFGS
DPERGFKALA AVQQGPLMCG EYYSGWFDTW GTPHKRGDNA RAIRDIDTML KANGSFSLYM
AHGGTTFGLW GGCDRPFRPD TTSYDYDAPI SEAGWLGEKF RTYRECLGRH LEPGETLPEA
PAHLPVMAIP AFALKETAPV FANLPAAVIR DASPRNIEQY DISRGLVAYS IVLPPGPAAR
LEAANARDLA WVYAGGRLVG TMDTRHRRFG VDLPARTQPT RVEILLYTIA RVNFGVEVHD
RKGLQGPVLL RTKDGAAQEL SGWDIRAIDF GDDGELPPLR WQAKRVAGPA FWRGSFDVKE
QADTFLDMSS WGQGIVWING RCLGRYWSIG PTQTMYLPGP WIRAGRNEVV VLDLTGPRAS
RIEGRTTPIL DELHPERDLA RPASTARPRL AGVAPVHAGQ FAGGPATQEA RFEQPARGRQ
LCLEVVDTFD GKPHAAVAEL ALLGLDGKPM NQSTWTIAYA SSEEAHKEDG GALNAINGQA
SDYWHTAYSK GETPAGPARL IIDLGAAVDI AGLRYTPRQG PDTVTGRIRR YRVYVGDRLV
QPM
//