ID A0A0P0D7L3_9FLAO Unreviewed; 451 AA.
AC A0A0P0D7L3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=CBM6 domain-containing protein {ECO:0000259|Pfam:PF16990};
GN ORFNames=APS56_05980 {ECO:0000313|EMBL:ALJ04709.1};
OS Pseudalgibacter alginicilyticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Pseudalgibacter.
OX NCBI_TaxID=1736674 {ECO:0000313|EMBL:ALJ04709.1, ECO:0000313|Proteomes:UP000057981};
RN [1] {ECO:0000313|EMBL:ALJ04709.1, ECO:0000313|Proteomes:UP000057981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ-22 {ECO:0000313|Proteomes:UP000057981};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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; CP012898; ALJ04709.1; -; Genomic_DNA.
DR RefSeq; WP_054725993.1; NZ_CP012898.1.
DR AlphaFoldDB; A0A0P0D7L3; -.
DR STRING; 1736674.APS56_05980; -.
DR KEGG; ahz:APS56_05980; -.
DR PATRIC; fig|1736674.3.peg.1222; -.
DR OrthoDB; 9763933at2; -.
DR Proteomes; UP000057981; 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; cd08990; GH43_AXH_like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
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; PF16990; CBM_35; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 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:UP000057981};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..451
FT /note="CBM6 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006043380"
FT DOMAIN 330..446
FT /note="CBM6"
FT /evidence="ECO:0000259|Pfam:PF16990"
FT SITE 148
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 451 AA; 51272 MW; 204FC009B6C2696F CRC64;
MKTKLLLLTA LLSVAIGVSQ NPIFTNVFTA DPSPHVWPDD PNTLWVYTSH DEPGSNNHYG
MTGYHAFSTT DLVNWTDHGR ILHLENVEWA ESHAWAMDAT YYRGQYYLVY CMKEAGIGLF
RTGIARSDVP QGPFTDLGYV KGVEFGQDPA IFIDDDGTPY LYWGHDRQCY AAELNEDLMS
IKPETYVDLT KQLTHVFEGP WVHKRNGTYY LTYPGLTPRR WPEKMFYAVA DKPLGPYTFK
GVFIDDFEGQ SGTNHGGVVN YKGKDIMFYH SAWLSGGLSE TRSSMADYLE YDKAGNIIPI
IPSKKGLGKA ERTRVTMKLE AESGFAAGGN LYNVFVDTYL KDYSGKGYVT NFDNPYDHVS
MLAQVAKPSK FRFKVRYASP EGESNHNILI NSHLYREFKF PQSKTFTEID FGIVELKEGD
NLVRIFKSDW KPSKGELAID YIKLEQVFEN E
//
