ID A0A0Q6LBV2_9SPHN Unreviewed; 617 AA.
AC A0A0Q6LBV2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN ORFNames=ASG67_00090 {ECO:0000313|EMBL:KQU61640.1};
OS Sphingomonas sp. Leaf339.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736343 {ECO:0000313|EMBL:KQU61640.1, ECO:0000313|Proteomes:UP000051371};
RN [1] {ECO:0000313|EMBL:KQU61640.1, ECO:0000313|Proteomes:UP000051371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf339 {ECO:0000313|EMBL:KQU61640.1,
RC ECO:0000313|Proteomes:UP000051371};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQU61640.1, ECO:0000313|Proteomes:UP000051371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf339 {ECO:0000313|EMBL:KQU61640.1,
RC ECO:0000313|Proteomes:UP000051371};
RA Schulze-Lefert P.;
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|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:KQU61640.1}.
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DR EMBL; LMRS01000001; KQU61640.1; -; Genomic_DNA.
DR RefSeq; WP_056523611.1; NZ_LMRS01000001.1.
DR AlphaFoldDB; A0A0Q6LBV2; -.
DR STRING; 1736343.ASG67_00090; -.
DR OrthoDB; 9813184at2; -.
DR Proteomes; UP000051371; 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; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR026283; B-gal_1-like.
DR InterPro; IPR048912; BetaGal1-like_ABD1.
DR InterPro; IPR048913; BetaGal_gal-bd.
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 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; PF01301; Glyco_hydro_35; 1.
DR PIRSF; PIRSF006336; B-gal; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051371};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..617
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006282790"
FT DOMAIN 40..355
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 398..508
FT /note="Beta-galactosidase 1-like first all-beta"
FT /evidence="ECO:0000259|Pfam:PF21317"
FT DOMAIN 526..584
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
FT ACT_SITE 188
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT ACT_SITE 264
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ SEQUENCE 617 AA; 68371 MW; 8288031047493349 CRC64;
MKMVVRSILG AALTASMLPA APVAAQTAVP AHSFAVGGSQ FLKDGKPYQV ISAEMHYVRI
PRAYWRDRLR KARAMGLNTI TTYAFWNAHE PRPGVYDFTG QNDIAGFIRD AQAEGLDVIL
RPGPYVCAEW ELGGYPSWLL KDRGLLLRST DPTYTAAVER WMVRLGQEVK PLLLRNGGPI
VAVQLENEYG AFGDDKAYLK GLEATYRRAG LADGVLFTSN QAGDLAKGSL PHLPSVVNFG
SGGAPNAVAK LEAFRPNGVR MVGEYWAGWF DKWGEDHHET DGRKEAEELR FMLKRGYSVS
LYMFHGGTTF GWMNGADSHT GTDYHPDTTS YDYDAPLDEA GNPRYKYALL ASVIAEVTGK
PAAPAPALSV AATFPVSQIR RSASLWDNLP DPVRARRPMT FEELEQNYGY VLYRVALAKG
QAGPLMLKGM HSYAQVYLDR KLVGTLDRRL GQETVNLPQR DGPVTLDILV ENTGRVNYSH
AIRTEQTGLT GAVTLNGQPL EDWRMFRLPM NDLSTLRLTT APCVGPCFYE TEMTVDRPAD
TYLDMRGLHK GQLWLGEHNL GRFWSIGPVH TLYTPAPWMK QGANRILFFD LTGDATDRLT
TVNAPVFGKV TKIREAQ
//
