ID A0A1Y1CGD2_9BACT Unreviewed; 1010 AA.
AC A0A1Y1CGD2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:BAX79082.1};
GN ORFNames=ALGA_0693 {ECO:0000313|EMBL:BAX79082.1};
OS Labilibaculum antarcticum.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinifilaceae;
OC Labilibaculum.
OX NCBI_TaxID=1717717 {ECO:0000313|EMBL:BAX79082.1, ECO:0000313|Proteomes:UP000218267};
RN [1] {ECO:0000313|Proteomes:UP000218267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPP2 {ECO:0000313|Proteomes:UP000218267};
RA Watanabe M., Kojima H., Fukui M.;
RT "Complete genome sequence of Marinifilaceae bacterium strain SPP2, isolated
RT from the Antarctic marine sediment.";
RL Mar. Genomics 0:0-0(2017).
RN [2] {ECO:0000313|EMBL:BAX79082.1, ECO:0000313|Proteomes:UP000218267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPP2 {ECO:0000313|EMBL:BAX79082.1,
RC ECO:0000313|Proteomes:UP000218267};
RA Watanabe M., Kojima H., Fukui M.;
RT "Complete genome sequence of Marinifilaceae bacterium strain SPP2, isolated
RT from the Antarctic marine sediment.";
RL Mar. Genomics 39:1-2(2018).
RN [3] {ECO:0000313|Proteomes:UP000218267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPP2 {ECO:0000313|Proteomes:UP000218267};
RA Watanabe M., Kojima H., Fukui M.;
RT "Labilibaculum antarcticum sp. nov., a novel facultative anaerobic,
RT psychrotorelant bacterium isolated from marine sediment of Antarctica.";
RL Antonie Van Leeuwenhoek 113:349-355(2020).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; AP018042; BAX79082.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1CGD2; -.
DR KEGG; mbas:ALGA_0693; -.
DR OrthoDB; 9802773at2; -.
DR Proteomes; UP000218267; Chromosome.
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; IPR026876; Fn3_assoc_repeat.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR040605; Glyco_hydro2_dom5.
DR InterPro; IPR006101; Glyco_hydro_2.
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; PF16355; DUF4982; 1.
DR Pfam; PF13287; Fn3_assoc; 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; 2.
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1010
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013141253"
FT DOMAIN 24..167
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 185..282
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 291..492
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 621..680
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 694..788
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
SQ SEQUENCE 1010 AA; 114161 MW; 2BC1DBFAB6683D98 CRC64;
MKKLLFLIFF AISMNLLAHE RINFNSDWKF KLNDQLGAEA VSYEDDSWRI LDLPHDWSIE
GEYNENNPMG GQCGYLPSGI GWYRKTIAVP ANWKGKQVEV AFDGVFMNSE VWANGRKLGV
RPYGWISFAY DISKETLSSD SITFAVRVDN DKQPSARWYT GSGIYANTWI DVKEQVHVAN
SGIFIRTKGS TVEIDTEIAN QLSKLTKASF TTSIKDPGGK IVAAAQNKLK IEAGKSEKIT
QSIKLETPQL WSIENPNLYT AVTEVKVGKK VMDVVETHFG VRDIEWKAET GMWINGKNVK
LQGVCNHQDA GALGAAVPDK ILRFRIQQLK DMGCNAIRTA HNPQTPQFYD MCDEMGMLVM
DEIFDGWMKK AANDYGAHSF DEWWNRDLTD WIKRDRNHPS VVIYSVGNET HGEIGKDIVA
RCHELDHTRP LTSGHSGSEY MDVFGVNGSS EKMGWFDTME KDRVFIGTEN THTWQVRGFY
RTKTWYRDGY PNKRQKSYFY PDLTEEEVFS YDWTNAAGRN NYKQIFNSSY DNGMVRLTSR
QNIEQLRDIP YYAGSFRWTG YDYIGEATYV HGGWPFKSFM GGAIDMANFE KDLFYLYQSQ
WTSKPMVHIL PHWTHPTLKE GVEIPVWVYS NCDEVELFLN GKSLGKQKPG LTWDKMQCQW
MVGWTPGELK AIAYKNGKSV VEKIIRTADA PSRIALSVDG ENMDDENRDI VQLRVTATDE
KGAFYPYGEN RTYFHVIGSG KIRALDNGSP IDVEKHFEAT NRIAFFGLTR AYIESTDETG
DVAVLASCIL GEKKQISSNK VNIDAELISL RGELPSADIQ IYYTLDGSVP STKSNLYEKS
FDVELGTSVK ALVLMNGKEI QQMEERFAND EGFVWNAAVV AANPGGDQAE DASFDGANIE
SNGSDFKGKG YIDFGRNSGG YVEWYQENDG SPGEFTLQIR YSANDKIRPE YKALLTINGK
KQEVVLPALT NYRKDWAVFE LKAKLGSGAN TIRITALEDD GLSIDELLVK
//
