ID F0BD24_9XANT Unreviewed; 855 AA.
AC F0BD24;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:EGD09626.1};
DE EC=3.2.1.23 {ECO:0000313|EMBL:EGD09626.1};
GN ORFNames=XVE_2040 {ECO:0000313|EMBL:EGD09626.1};
OS Xanthomonas vesicatoria ATCC 35937.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=925775 {ECO:0000313|EMBL:EGD09626.1, ECO:0000313|Proteomes:UP000003299};
RN [1] {ECO:0000313|EMBL:EGD09626.1, ECO:0000313|Proteomes:UP000003299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35937 {ECO:0000313|EMBL:EGD09626.1,
RC ECO:0000313|Proteomes:UP000003299};
RX PubMed=21396108; DOI=10.1186/1471-2164-12-146;
RA Potnis N., Krasileva K., Chow V., Almeida N.F., Patil P.B., Ryan R.P.,
RA Sharlach M., Behlau F., Dow J.M., Momol M.T., White F.F., Preston J.F.,
RA Vinatzer B.A., Koebnik R., Setubal J.C., Norman D.J., Staskawicz B.J.,
RA Jones J.B.;
RT "Comparative genomics reveals diversity among xanthomonads infecting tomato
RT and pepper.";
RL BMC Genomics 12:146-146(2011).
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:EGD09626.1}.
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DR EMBL; AEQV01000061; EGD09626.1; -; Genomic_DNA.
DR RefSeq; WP_005991924.1; NZ_CP018725.1.
DR AlphaFoldDB; F0BD24; -.
DR GeneID; 46983593; -.
DR KEGG; xve:BJD12_19905; -.
DR eggNOG; COG3250; Bacteria.
DR Proteomes; UP000003299; 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; 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; 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 SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:EGD09626.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EGD09626.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..855
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030168505"
FT DOMAIN 153..249
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 259..364
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 373..449
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 453..532
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 672..725
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 740..841
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
SQ SEQUENCE 855 AA; 93177 MW; 5C9BD2941B7A5CC2 CRC64;
MTGINRRALL RGMLASGVSA ALPVGTAAAA VPGSAAAASA TAKTAASVGP LGDATLAPRE
RLLFDFGWRF HLGHASDPSR DFEFGTFQRT FAKAGKDTAT AAQLAFDDTA WQQVDLPHDW
AATLPFRPEP TSASMSEEDP AAAHGYKALG TSFPENSVGW YRRTLQIPAS DLGKRICLVF
DGVFRDCVVF CNGHIVGRNA SGYCGFEVDL SEVLDYGKPN VIAVRVDATL GEGWFYEGAG
IYRHLWLQKT DPLHLPQDGV FVRSTVQGDS ATAQVSAEVR NDGTAPRQCS VQVHITAPDG
RVVAQGVSAA VTVAPGQVQL LEQTLPLGQA ALWSIDTPQL YTLTTSVHSD GKATDAVVTP
FGVRSIAFDA QRGFLLNGAP LKLHGTNNHQ DHAGVGTAIP DALHEWRLRQ LKSMGCNAYR
SSHNPATPEL LALCDRLGMF VIEETRRMST DPEAMRELET MVRRGRNHPS VILRSLGNEE
PQQVTERGAR IVSRMQQRVR QLDPTRPTTF AMDKGFGDGV GQVVDVVGFN YRTSQMDGFH
AQYPDIPIYG SETGSTVSVR GNYQRDDARG YRRAYDLDHP WWASTAEAWW SYVAQRPYIA
GGFIWTGFDY RGEPTPYNRW PNVASQFGVL DSCGFPKDNY WYYRAQWTSE PVLHLFPHWN
WDGLLQADDN GHVQVWCHSN LDAVELLVNG ISQGLQQVPA YGHVEWRVTY APGAIEARGY
RGGTLVLSQR RETGGKPAAI RLSCDRDSLH ADGEDVAVVK VEIVDAQGRI VPNADNLVHF
ALRGPARLIG VGNGDPSSHE DDKTPRRKAF NGLCMALLQS ALAHGDIVLQ ATAPGLTSAT
LRIPAEVTST RKAVA
//
