ID A4XMX0_CALS8 Unreviewed; 810 AA.
AC A4XMX0;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 2.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Glycoside hydrolase family 2, sugar binding protein {ECO:0000313|EMBL:ABP68255.2};
GN OrderedLocusNames=Csac_2686 {ECO:0000313|EMBL:ABP68255.2};
OS Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T
OS 6331).
OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX NCBI_TaxID=351627 {ECO:0000313|EMBL:ABP68255.2, ECO:0000313|Proteomes:UP000000256};
RN [1] {ECO:0000313|Proteomes:UP000000256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331
RC {ECO:0000313|Proteomes:UP000000256};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A.,
RA VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J.,
RA Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M.,
RA Kengen S.M.W., Richardson P.;
RT "Genome sequence of the thermophilic hydrogen-producing bacterium
RT Caldicellulosiruptor saccharolyticus DSM 8903.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABP68255.2, ECO:0000313|Proteomes:UP000000256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331
RC {ECO:0000313|Proteomes:UP000000256};
RX PubMed=18776029; DOI=10.1128/AEM.00968-08;
RA van de Werken H.J., Verhaart M.R., VanFossen A.L., Willquist K.,
RA Lewis D.L., Nichols J.D., Goorissen H.P., Mongodin E.F., Nelson K.E.,
RA van Niel E.W., Stams A.J., Ward D.E., de Vos W.M., van der Oost J.,
RA Kelly R.M., Kengen S.W.;
RT "Hydrogenomics of the extremely thermophilic bacterium Caldicellulosiruptor
RT saccharolyticus.";
RL Appl. Environ. Microbiol. 74:6720-6729(2008).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; CP000679; ABP68255.2; -; Genomic_DNA.
DR RefSeq; WP_011918171.1; NC_009437.1.
DR AlphaFoldDB; A4XMX0; -.
DR STRING; 351627.Csac_2686; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR KEGG; csc:Csac_2686; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_006501_0_1_9; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000000256; 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; 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; 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; 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; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABP68255.2}.
FT DOMAIN 59..152
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 158..269
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 277..464
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 633..691
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 705..805
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
SQ SEQUENCE 810 AA; 91939 MW; 834C5587A2227E5A CRC64;
MKKVNIDKSW ECAESSLYSV LNVANLECEW RPVDLPHDAV IERPRCENNP SGASEGYTPG
CSLYYKKELM LEEEWKGKNL ILEFEGIMGI SEVFVNGRLV AKHFNGYTSF FVDITKHVKF
DDKNTIVVHV ENTHKPSSRW YAGCGIYRHV WLHVGGKVYI KPWHLHVETK AIENETAILE
VRAAVANSTN ESVQGVMEFS IFSNDGELIT SSQEQLILGE NEEKTVSKII TLSPFKYWDI
ENPYLYKILA TIKIDEDIED SSSAFFGIRT ISVNPKEGLK LNGRVIKLKG GCIHHDNGPL
GSASYDRAEE RKVELLKASG FNAVRLAHNP FAPAFLDACD RLGMLVIEEF FDVWTAGKVS
YDYHLFFDKY WEEDLKATIM RDYNHPSIIM WSIGNEITWG VGIDVDDEEG YSSIYTWCER
LSQKVKELDS TRLVTAAFCA IPADYESLLT TIEDGNYVIR MLKQEAVAGN DKWGKVTEKF
FEFLDVAGYN YKVDRYSYDL EKYPGRIICG TETYPYTLFR NWTETIKNPN VVGDFVWTAI
DYLGEAGIGR VCTDENEAKI FGGKFPWFYA NCGDIDICGD KRPQSYYRDI VWGLRKEPYI
VVLPPQLFGK KLYFRPWAWE PVERSYTFPG YEGMPIAVHV YADADEVEVF VNGRSLGRKV
CGINTQFKAV YNTVYEPGVI EAVAYKNGKE IGKDKIETTD RPVALKLLPD RNVISSCGDL
CYIKIIAVDK NEREVPYADN TVTVEVEGAG RFMALGTADP LSTELFVSSQ RKLYKGRALA
VVKSIREKGE IRVRVLAEGL KSAEVVIKCI
//
