ID A0A1Y0N1K1_9FLAO Unreviewed; 444 AA.
AC A0A1Y0N1K1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=CBM6 domain-containing protein {ECO:0000259|PROSITE:PS51175};
GN ORFNames=BTO07_16255 {ECO:0000313|EMBL:ARV16593.1};
OS Polaribacter sp. SA4-12.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1312072 {ECO:0000313|EMBL:ARV16593.1, ECO:0000313|Proteomes:UP000195470};
RN [1] {ECO:0000313|EMBL:ARV16593.1, ECO:0000313|Proteomes:UP000195470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA4-12 {ECO:0000313|EMBL:ARV16593.1,
RC ECO:0000313|Proteomes:UP000195470};
RA Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; CP019334; ARV16593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0N1K1; -.
DR OrthoDB; 9763933at2; -.
DR Proteomes; UP000195470; 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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd04084; CBM6_xylanase-like; 1.
DR CDD; cd08990; GH43_AXH_like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
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; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SMART; SM00606; CBD_IV; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51175; CBM6; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000195470};
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..444
FT /note="CBM6 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012463066"
FT DOMAIN 313..443
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT SITE 152
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 444 AA; 49877 MW; 32802E7394716644 CRC64;
MKKVVTIIII CLTINSFAQN PLVTNIHTAD PTARVFNGKL YIYPSHDAVP PEGIVAPRFC
MPDYHIFSLE NGNTWKDYGV ILDQNEVPWG KKNSYGMWAP DCIERDGKYY YYYPAPPKDG
TSFRRIGVGV SKSPTGPFKW EKNYIKGIDG IDPGLMIDDD GKGYIFFAGD KTIKGAKLNK
NMKKIDGEAI KIEGIPAGYV EGPFPFKHNG NYYLTFAHVF PDEGYTIGYA MSKKPLGPYV
YAGKIMDNID NGTNHHSIVK YKGKWILFYH WWSVSGYSKL RSMRADYMEF KKDGTIKKVK
PTLRGIGNPR VNDTIQVDRY NDIYNAKATF VGGNEPNGWM VSDTKMMSTV RFNGVDFGKG
EAKKIQARVA SGQRNGSFEV RLGGTKGKLI ATFPVNYTGG YNKWQTIETE LVGNPTGIKD
ITVVFKSVWG ATKIVNLNWL LLKK
//
