ID A0A0Q4FL01_9SPHN Unreviewed; 973 AA.
AC A0A0Q4FL01;
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:KQM63432.1};
GN ORFNames=ASE75_13400 {ECO:0000313|EMBL:KQM63432.1};
OS Sphingomonas sp. Leaf17.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1735683 {ECO:0000313|EMBL:KQM63432.1, ECO:0000313|Proteomes:UP000051777};
RN [1] {ECO:0000313|EMBL:KQM63432.1, ECO:0000313|Proteomes:UP000051777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf17 {ECO:0000313|EMBL:KQM63432.1,
RC ECO:0000313|Proteomes:UP000051777};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM63432.1, ECO:0000313|Proteomes:UP000051777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf17 {ECO:0000313|EMBL:KQM63432.1,
RC ECO:0000313|Proteomes:UP000051777};
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:KQM63432.1}.
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DR EMBL; LMKL01000008; KQM63432.1; -; Genomic_DNA.
DR RefSeq; WP_055934428.1; NZ_LMKL01000008.1.
DR AlphaFoldDB; A0A0Q4FL01; -.
DR STRING; 1735683.ASE75_13400; -.
DR OrthoDB; 9758603at2; -.
DR Proteomes; UP000051777; 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; 1.
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 InterPro; IPR006311; TAT_signal.
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; 2.
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.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000051777}.
FT DOMAIN 110..231
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 242..346
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 356..427
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 435..532
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 650..706
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 720..822
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
FT REGION 30..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 973 AA; 105003 MW; 2BA0AA6299382155 CRC64;
MTFDRRTMLL GSAGMGAALL VEGPTIAAAP SGSGGSGGSA GGLPMPAPTD RLPDPLPVSD
PSRMLLDHGW LFHEGDIPVP EPVGHHATYL RVKAGNAGGA AAMDYDDSDW QPVTLPHDWA
SAQPFVKTAN VSQGFRPRGI GWYRRTLRLD PADRGKAIEL QFDAIATNAT IWVNGSVVAH
NWSGYSSVYV DLTPFARFGD DLNVIVVRAD ATAMEGWWYE GAGLYRHVWL ARRAPVSIVT
DGVHCDPRHD ASGWRVPVAV TLASVAPGDV AVTVELLLID PDGREVGVAK GAVTVPALDR
AEAVLDLRVD NPRRWSVERP ELYTVHTRIL RDGAVVDERR TPIGFRTIRF DATHGFFLND
VSVKLKGVCI HQDHAGVGVA VPDALLAWRL ERLKAMGCNA IRCSHNAPAA ELLDLCDRMG
FLVMDENRNF NPSPDYMAQL EWLVRRDRNH PSVILWSVFN EEPMQGTEAG VEMVRRMRAT
VRRLDDSRPV TAAMNGSFYD PANVSQVVDV MGFNYYQADY DKFHALNPHM PITSSEDTSA
FETRGAFATD AARGVSTSYD TEAASWGDTH RATWKAVVER PFVAGTFVWT GFDYHGEPTP
YEWPSIASVF GIMDLCGFPK TAFDIHRAHW VDDAAVVSIA PHWTWPGKEG QPITVFVASN
AERVVLRLNG KVVGEKPVDR VMGMEWQVPY VPGRIEAIAY RGTRDVARAV HETTGVPVAL
RLSPARRVMA GDGEDTQPVT IDAVDAAGRH VPTANLMTRF TVSGATIIGV GNGDPTSHEP
EKGNARSLFN GLAQVIVQAE AGGRGKVTLR ATADGLRPAT LTINRAAVAP RAQVPVTVAP
MAIPQWRRSP PLTTRPDPTL APADGDNNSW AFVRSGVATP PEGAAGWRVY RTMVTPRRGV
AQKGGVIRFD GIAGRATLWV DGRCVGTKPD PATAPLSAPL LPASGPRTIV LIVEAPAGAP
SGIVAPVSVL PMP
//
