ID A0A0Q8XMM0_9SPHN Unreviewed; 966 AA.
AC A0A0Q8XMM0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:KRC80317.1};
GN ORFNames=ASE13_15105 {ECO:0000313|EMBL:KRC80317.1};
OS Sphingomonas sp. Root241.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736501 {ECO:0000313|EMBL:KRC80317.1, ECO:0000313|Proteomes:UP000051629};
RN [1] {ECO:0000313|EMBL:KRC80317.1, ECO:0000313|Proteomes:UP000051629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root241 {ECO:0000313|EMBL:KRC80317.1,
RC ECO:0000313|Proteomes:UP000051629};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC80317.1, ECO:0000313|Proteomes:UP000051629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root241 {ECO:0000313|EMBL:KRC80317.1,
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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:KRC80317.1}.
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DR EMBL; LMIV01000002; KRC80317.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q8XMM0; -.
DR STRING; 1736501.ASE13_15105; -.
DR OrthoDB; 9758603at2; -.
DR Proteomes; UP000051629; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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 Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR032311; DUF4982.
DR InterPro; IPR048230; GalA-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR040605; Glyco_hydro2_dom5.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR NCBIfam; NF041462; GalA; 1.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF16355; DUF4982; 1.
DR Pfam; PF18565; Glyco_hydro2_C5; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..966
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006362446"
FT DOMAIN 60..222
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 233..338
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 348..582
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 642..699
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 712..813
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
FT REGION 29..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 966 AA; 106196 MW; 955B439C8D7126CB CRC64;
MDRRAFLATT ALATALPAFP ARAKAVDTYN GGDVPMPAPR DGLDPRPTPE EPGRLLLDQG
WRFHLGDVPM PEIKGHQATY ENAKAGAAHG AAAMTFDDSD WREVTLPHDW AIEGAVDPQA
NVSQGYRRRG IGWYRRTIRL DPALQGKFLE IDFGGIATNA TIWINGTIVD RNWSGFNGVH
VDLTPYARFG DELNTIAIRV DAEPMEGWWY EGAGIYRHVW LAVRAPVYIV TDGVHCDPRR
AADGSWSVPV EVTLGNISTE NRTVMVQVTL ASTDNVGIVV QSVHAEVRPL VTATARLDLP
VTDPQLWSPE SPTLYPLEVR VLDGDKLIDT RHFNIGFRTF TFDSRTGFHL NGQPLKIKGT
CNHQDHAGVG TAIPDSLWDW RVRRLKALGS NAIRMSHNAP PTELLDACDR HGLLVMNENR
QFNPSPDYMA QLEWLVRRDR NRPSVFLWSV FNEEPMQGSP QGYEMVRRMA ATVKALDDSR
PVTAAMNDGM FTPSNVSQAV DVVGFNYQIP QYDKYHAAFP DKPLTSSEDT SAFSTRGEWV
TDKTRNIMTS YDDEGAPWGA THAAAWKAIA ERPFVAGGFV WTGFDYHGEP TPFEWPSTSS
FFGIMDICGF PKLAFHQHRA QWIDDTPVLA LQPHWNWPGK EGTPIRVVVL TNAERVTLLL
NGKKVGEAAV DRLKQPEFQV PYAPGKLEAI GYRGGREVAR AVIETVGAAV KLRLTPDRRV
MAGDGEDAQP ITVDAVDSRG RHVPLVNLPA GFTIEGGEII GLGNGNPNDH DPEKGSARKL
FNGLAQVIVR AAAGRGKLVL RATAPGLEPT TLTIDRVVAT PRAQVADTRP EMLLSFWARV
PFTATRPDPN AKVGTDDRYA TARGRSGRLE GPSDAGRWNG YQMNFTPPAS VRRRGGVLTF
TELAGSAEIW LDGKKIGEKR DPASARLDVT LPAGQGERSL VVLVQAEPGK ASGFGKMVVV
REKVDQ
//
