ID E4RVE4_LEAB4 Unreviewed; 859 AA.
AC E4RVE4;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:ADQ16130.1};
DE EC=3.2.1.23 {ECO:0000313|EMBL:ADQ16130.1};
GN OrderedLocusNames=Lbys_0352 {ECO:0000313|EMBL:ADQ16130.1};
OS Leadbetterella byssophila (strain DSM 17132 / JCM 16389 / KACC 11308 / NBRC
OS 106382 / 4M15).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Leadbetterella.
OX NCBI_TaxID=649349 {ECO:0000313|EMBL:ADQ16130.1, ECO:0000313|Proteomes:UP000007435};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17132;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Teshima H., Brettin T., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Leadbetterella byssophila DSM 17132.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADQ16130.1, ECO:0000313|Proteomes:UP000007435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17132 / JCM 16389 / KACC 11308 / NBRC 106382 / 4M15
RC {ECO:0000313|Proteomes:UP000007435};
RX PubMed=21475582; DOI=10.4056/sigs.1413518;
RA Abt B., Teshima H., Lucas S., Lapidus A., Del Rio T.G., Nolan M., Tice H.,
RA Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K.,
RA Pati A., Tapia R., Han C., Goodwin L., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M., Tindall B.J.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Leadbetterella byssophila type strain
RT (4M15).";
RL Stand. Genomic Sci. 4:2-12(2011).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; CP002305; ADQ16130.1; -; Genomic_DNA.
DR RefSeq; WP_013407185.1; NC_014655.1.
DR AlphaFoldDB; E4RVE4; -.
DR STRING; 649349.Lbys_0352; -.
DR CAZy; CBM57; Carbohydrate-Binding Module Family 57.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR KEGG; lby:Lbys_0352; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_006501_5_0_10; -.
DR OrthoDB; 857501at2; -.
DR Proteomes; UP000007435; Chromosome.
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; 2.60.120.430; Galactose-binding lectin; 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; 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 InterPro; IPR021720; Malectin_dom.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 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 Pfam; PF11721; Malectin; 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.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:ADQ16130.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADQ16130.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007435};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..859
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003185850"
FT DOMAIN 38..161
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 183..284
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 291..592
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 684..849
FT /note="Malectin"
FT /evidence="ECO:0000259|Pfam:PF11721"
SQ SEQUENCE 859 AA; 97738 MW; 19DF2D4F65241B88 CRC64;
MKFQSKSGLA ILFFALSPLL LYAQNYSINE GWTFKTEDTK EQKVSFPHTW NAMDAQDETP
GYSRTIGTYT RKLSTPASYA GKVVYLQFEG ANQITEVFLD EKRVGKHQGG YTRFNFDLTP
YLRPGRTQEL RIVVDNRHHV DIAPLSADFT FFGGIYRDVY LDVREDLHIS PLDFASSGVY
VKTPKVSTSE AILEISTLIN NHSSEKKEIQ VLHTLKDPDG KVITSLTLKV DPEANTSNQR
VEGKIQVPKP RLWTPGTPFL YTVETKILEK GQLRDECTTK TGFRWFEFHA DTGFHLNGKP
LKLIGTSRHQ DFKDKGYALE DAHHIRDIEL LKNMGGNFLR IAHYPQDPLI LEMCDKLGIL
ASVEIPIVNA VTESAAFSNQ SIFMAEEMVK QNTNHPSLIV WSYMNEVMLR PPYKNTEAAY
GPYCQEVYKQ AKAIQDKIKQ LDPSRPTMIA FHGNVKAYED ANLFTVPDII GWNLYQGWYS
DRPEQLDTFL KKYREKYPSK PTILSEYGAD VDVRIHTYSP ERFDYSVEYG DLYHEHYLKT
ILNSPFLAGA AIWNLNDFYS EVRKNTIPHV NSKGISGLDR KPKNTYFLYQ AHLLKQAFVR
FASKEWQQRP EGNHEIKIYS NASQVTLYLN NKKWGKLKVN AGIAKTHLNL PAGTHTLRAH
ISGAEDSFEI HTLPSQNFNE LNVALGSKRF FWDENTKTLW QPEKAYEPGS YGFIGGQALR
PKTRYGELPT AEVRIKGTDL SPLFLTQRIG IEKFKADLPA GKYAVYLYWA ELNGTEPADA
IAYNLGNDAI QELAGKRSFN VKANGVSFLE NYEIDKEAGI QQAAVKKFNI DVKENGLTIE
FIPIEGTTLL NAIKIIKRD
//
