ID A0A0Q8XR91_9SPHN Unreviewed; 992 AA.
AC A0A0Q8XR91;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=ASE13_15140 {ECO:0000313|EMBL:KRC80471.1};
OS Sphingomonas sp. Root241.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736501 {ECO:0000313|EMBL:KRC80471.1, ECO:0000313|Proteomes:UP000051629};
RN [1] {ECO:0000313|EMBL:KRC80471.1, ECO:0000313|Proteomes:UP000051629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root241 {ECO:0000313|EMBL:KRC80471.1,
RC ECO:0000313|Proteomes:UP000051629};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC80471.1, ECO:0000313|Proteomes:UP000051629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root241 {ECO:0000313|EMBL:KRC80471.1,
RC ECO:0000313|Proteomes:UP000051629};
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|ARBA:ARBA00001412};
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:KRC80471.1}.
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DR EMBL; LMIV01000002; KRC80471.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q8XR91; -.
DR STRING; 1736501.ASE13_15140; -.
DR OrthoDB; 9813184at2; -.
DR Proteomes; UP000051629; 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; 2.102.20.10; Beta-galactosidase, domain 2; 1.
DR Gene3D; 2.60.390.10; Beta-galactosidase, domain 3; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR018954; Betagal_dom2.
DR InterPro; IPR037110; Betagal_dom2_sf.
DR InterPro; IPR025972; BetaGal_dom3.
DR InterPro; IPR036833; BetaGal_dom3_sf.
DR InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
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; PF13364; BetaGal_ABD2; 2.
DR Pfam; PF10435; BetaGal_dom2; 1.
DR Pfam; PF13363; BetaGal_dom3; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SMART; SM01029; BetaGal_dom2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF117100; Beta-galactosidase LacA, domain 3; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..992
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006362572"
FT DOMAIN 396..575
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
SQ SEQUENCE 992 AA; 106972 MW; 97D1E02B87152652 CRC64;
MRAALLAASA LLALPAAAQE ARQTANFNAP VKTFGRISYD ARSLMIDGKR TIIWSSEMHA
FRLPSPDLWR DVLQKMKASG FNTVAFYFDW GFHSPKKGIY DFSGIRDIDR LLTMAEEEGL
WVITRAGPYV NAELTRGGFP GWLVNQRGRA RTDDPEYLAA SDEWLTRVNA IIARHQVNGD
GKGHKGNVIL HQIENELALT TPAQRRYMDH LYAKARADGI TVPLFHNDQG RNGYWVPEDS
KVEKTVPGPN DLYAFDGYPG GTCTVNGKPT RGSAAPDWGY YGPGGAKGGA SASPNTPGFL
AEFGGGWFDY WGSNGGYECN AIQRGKRFQR VFYGTNLANG IGIQSFYMGF GGTSWGWLPA
PVVFTSYDYG AALSEAREVR PKAEELKQLG GLIAAVPDLA GMIPAGPVQI SSDKIQVYHN
KSPETDARFL LVTHKPSNSQ TNDRFTFTAD LPDGRYTLPM QLDGFDAKWL VAGVNLGGQR
LVYSTSELQA LVRQDGRDVA LIYGRAGEAG ETVLRYASAP KVTVLEGGAT SAFDATKGDL
KLNYAHRGLT RVRISGGGRP DLLLLIGDEA EGAKFWHVGD VLVRGPALVR TASAAKGNLA
LTGDTREPTP LEIWAPAGVR SVTWNGAKVA ITRTASGTVA ANTPLPAPVG FALPALTDWR
VAPGSPEADP AFDDRDWAKI DNRAYASITA RADGQPNMLM DAYGFHEGDV WYRGRFTGSP
DAERLKLHYG AGGAGLVQVF LDGKLIGQDE IPAGLPRPIT TGAPSFTLPD AARTPGEHVL
SVMVRNNGHN WDLDADDFHK EARGLVSASI EPVAGPSFAV PIAWKINGRG EDLPDPVRGV
ANNGGLDGER RGWYLPGFDD RGWKSAPAQA TPGTSWYRTS FDLAVPKGQD ATIGLAFGDT
SKPRSPVAYR VLIFVNGWNM GQFIAHVGPQ RVFPIPEGIL NHRGRNSIAL AVTSDGAPGN
TLEEVKLVTL RNVRGGIPVR MVPAPATPAE LK
//
