ID C9RS20_FIBSS Unreviewed; 740 AA.
AC C9RS20;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Putative endo-1,4-beta-xylanase {ECO:0000313|EMBL:ADL25037.1};
GN OrderedLocusNames=FSU_2263 {ECO:0000313|EMBL:ADL25037.1};
OS Fibrobacter succinogenes (strain ATCC 19169 / S85).
OC Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC Fibrobacter.
OX NCBI_TaxID=59374 {ECO:0000313|EMBL:ADL25037.1, ECO:0000313|Proteomes:UP000000517};
RN [1] {ECO:0000313|Proteomes:UP000000517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19169 / S85 {ECO:0000313|Proteomes:UP000000517};
RA Durkin A.S., Nelson K.E., Morrison M., Forsberg C.W., Wilson D.B.,
RA Russell J.B., Cann I.K.O., Mackie R.I., White B.A.;
RT "Complete sequence of Fibrobacter succinogenes subsp. succinogenes S85.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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DR EMBL; CP002158; ADL25037.1; -; Genomic_DNA.
DR RefSeq; WP_014546433.1; NC_017448.1.
DR AlphaFoldDB; C9RS20; -.
DR STRING; 59374.FSU_2263; -.
DR CAZy; CBM6; Carbohydrate-Binding Module Family 6.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR GeneID; 34756109; -.
DR KEGG; fsc:FSU_2263; -.
DR PATRIC; fig|59374.8.peg.2172; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_009397_11_2_0; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000000517; Chromosome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd04080; CBM6_cellulase-like; 1.
DR CDD; cd04084; CBM6_xylanase-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF03422; CBM_6; 2.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SMART; SM00606; CBD_IV; 2.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS51175; CBM6; 2.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:ADL25037.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADL25037.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000313|EMBL:ADL25037.1}; Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000313|EMBL:ADL25037.1}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..740
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003000424"
FT DOMAIN 350..488
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 532..656
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT REGION 516..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..547
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 34
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 219
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 159
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 740 AA; 80622 MW; D237275BA74D2024 CRC64;
MKLLKKVTMF GLLAGFGVSA LADNPISTYH YLADPGAAAD DDYFYIITDS DDPAPANSNG
YKIYALYAFR SRDMQNWTDY GIIYDARKVS GINDIWASGI AVHNGTFYIV FPDGGGGGIG
YIKAPAIEGP WTNAVGQGKD KLVGGRGIIG CDGVSWCFDP GIFIDDDGTT YVTWGGGEST
SRPNTDNFDI VKLNDAKNAP VGNGSHVKVN NLPTRKMLEA SYIHKHKGTY YFSYSTGWQQ
GAPTIDYGTS NNVMGPYTWK GTILGDPSMN GRSINGNNNH HGIAEFKGHS YVVYHDRRIA
KGHNGLEIIP ADDGQPKPNE GYHRSVSVDE MFYNADGTIQ TVKVTDEGPA QIENFDPYDW
YPALTSSKQK GIRSRSNFVQ GKAAEHVLLP LSSKESWLRV SGVDFGTAAT GFTVEAASAA
DNNKIEIRTG SATGTLAGTC TLKNTGNKNT YAENKCEVEG LKGIVKQLFL VFKGDRDSTM
AIKAWGFEGS GTTPPEPQKP FSGKAWEIPG KIEMEDFDIP GSGRGSEIKS YSENDSEDHG
IENGGKSYRE DTGVDIYKKA TGYVVGYNQS GEWLEYTVNV KEAGDYTMFA SVATDNSTAS
FTLSIDDKSI AEVPVSGDSW DDFVKVKANV TLPAGEHVLR FTVTGDWFDI DYMTFAKGKD
AKDPDDETIG IKGFRVLGAD AVANFDVFDL TGKKVSSFTA RNIHEAKKLW RENPQSRNVQ
GVCIIRNRYN GAVARVRTTR
//
