ID A0A1I5H695_9BACT Unreviewed; 673 AA.
AC A0A1I5H695;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Carbohydrate binding module (Family 6) {ECO:0000313|EMBL:SFO43782.1};
GN ORFNames=SAMN04487852_101139 {ECO:0000313|EMBL:SFO43782.1};
OS Prevotella sp. tf2-5.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1761889 {ECO:0000313|EMBL:SFO43782.1, ECO:0000313|Proteomes:UP000198673};
RN [1] {ECO:0000313|EMBL:SFO43782.1, ECO:0000313|Proteomes:UP000198673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF2-5 {ECO:0000313|EMBL:SFO43782.1,
RC ECO:0000313|Proteomes:UP000198673};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOWK01000001; SFO43782.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5H695; -.
DR STRING; 1761889.SAMN04487852_101139; -.
DR OrthoDB; 9803461at2; -.
DR Proteomes; UP000198673; Unassembled WGS sequence.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd08990; GH43_AXH_like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR005084; CMB_fam6.
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; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000198673};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..673
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011705232"
FT DOMAIN 370..482
FT /note="CBM6"
FT /evidence="ECO:0000259|Pfam:PF03422"
FT SITE 151
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 673 AA; 76768 MW; 8DCF521D14325098 CRC64;
MRNIILSISI LSTLAVSAQN PVIRDQFAAD PTARVFNNKV YVYPSHDIPA PEGQRQDWFC
MADYHVFSSE NLTDWTDHGV ILSQEQVPWG KTDAYSMWAP DCVYKNGKYY FYFPNAPKDG
RGFAVGVAIA NQPEGPFTCV QEPIMGISGI DPCVLIDDDC SAYIYWSGMG IRGARLKENM
LELDGELQEV KIPKRDGMPE MPPMKMGGQV MEGLPDGFKE GPFAFKRNGW YYLTFPWVRG
NTSNGANPTE TLAYAMSKSP LGPWDFKGII MAEHDNHCWT NHHSILEYKG QWYIFYHRND
FSPNMDKRRS TRIEKIAFNS DGTIQEVKQT MRGVGINQAV ERIEIDRYSS ASNDVTTQLI
DTVNTFRSFE AILSQKGSWL RYNDIDFNSV TDAYLVVNVK AADNTEFFVR EKSAKGKIIA
KVPMTVKSET RFPGSPTPFR RDQSNQWLTM TVPMEYLPKG VTDIVITNEG NAAFSINWIQ
FKNRPKYFSP VPATAAPSQP DQEGFIRRWR LLEPIAVDVR SNVVFTYSWL RHKFGEELAK
FNTNSKKGKW YVMDSETYNM KLFRFAEKYG KQTYGSFYWC ETVIDSPEEM RNVRLACGSN
GASLWWLNGE EVLMLEGDRR MVEDDGMSPR LTLKKGRNTL RVAVINGPGL SDMCARFIDE
KGKPITDYNV KVQ
//
