ID A0A170Z1E5_9BACT Unreviewed; 867 AA.
AC A0A170Z1E5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:GAT62253.1};
GN ORFNames=PJIAN_1846 {ECO:0000313|EMBL:GAT62253.1};
OS Paludibacter jiangxiensis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae;
OC Paludibacter.
OX NCBI_TaxID=681398 {ECO:0000313|EMBL:GAT62253.1, ECO:0000313|Proteomes:UP000076586};
RN [1] {ECO:0000313|Proteomes:UP000076586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM7 {ECO:0000313|Proteomes:UP000076586};
RA Qiu Y., Matsuura N., Ohashi A., Tourlousse M.D., Sekiguchi Y.;
RT "Draft genome sequence of Paludibacter jiangxiensis strain NM7.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000076586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM7 {ECO:0000313|Proteomes:UP000076586};
RA Qiu Y.-L., Tourlousse D.M., Matsuura N., Ohashi A., Sekiguchi Y.;
RT "Draft genome sequence of Paludibacter jiangxiensis NM7(T), a propionate-
RT producing fermentative bacterium.";
RL Genome Announc. 0:0-0(2017).
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:GAT62253.1}.
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DR EMBL; BDCR01000001; GAT62253.1; -; Genomic_DNA.
DR RefSeq; WP_068702289.1; NZ_BDCR01000001.1.
DR AlphaFoldDB; A0A170Z1E5; -.
DR STRING; 681398.PJIAN_1846; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000076586; 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; 2.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
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 PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 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 SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000076586};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..867
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007904938"
FT DOMAIN 70..195
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 222..320
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 330..446
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 710..794
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
FT REGION 831..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..867
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 867 AA; 97795 MW; E030AF629EC6306C CRC64;
MKYKQLLLIL FLPLALSLGA KEYQPAFSAA GFYDLQNSGR QVYNFNVGWR FHKGDVAGAE
KADFKDAAWD VVSTPHTVEL EPAEASGCRN YQGIAWYRKH FTLDKAYAGK KAILYFEAVM
GKCKVYLNGK LVKQHLGGYL PFSIDLLEAG AVPGQKCVVA VYADNSDDKN YPPGKSQKTL
DFAYHGGIYR DIWLVVKNTV NISDPNEAGK VAGGGVFVHY GEINDKLADV FVDTDVQNQS
DVAKSVKVET ALIDPKGNVV VKTVSSVSLK KGESKQVKQS VKVKNPVLWT PDEPLLYHVE
SRVISGKISL DGGMTRIGIR KAEFRGVDGF YLNGKPYEKL IGGNRHQDFA YVGNAVPNSQ
QWRDAKKLRD AGCRIIRSAH YPQDPSFMDA CDELGLFVIV PTPGWQFWNK DPEFAKLIYS
DIRNMIRRDR NHTSVLMWEP ILNETRFPLD FSLNALKITK EEYPYQGRFA AADMNSEGVK
DNYDVVYGWP RDTGTVKQSI FTREFGEYVD DWYAHNTPNR AARAWGEGPQ LIQALHLAKT
YNEMCDAPAQ FVGGCQWHPF DHQRGYHPDP YWGGIMDNFR QYKYSYYMFR SQIDPKRPHP
LADIEPMLFV ASEIGPFSSP DVVVFTNCDE VRLIRYERDT LVQKAPKALR GMPHPPVVFK
NAYDFYEMRQ FPYVQKNWQR VSFKAEGLID GKVVVTEKKM PSRRSTQVRL RLDNEGQQLT
ADGSDFVCVI AEITDDQGNV RRLAKEQILF SVEGEGEIIG DASIQANPRV VEFGSAPVLI
RSTTKAGKIK VNARVLFEGE YAPKSASIEF ASVAPARTLL FEENPKVFIS GKNGSQSNRK
TMTDEEKQKL LNEVEKQQTD FGEVKAN
//
