ID A0A1I1QYM6_9FLAO Unreviewed; 454 AA.
AC A0A1I1QYM6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Carbohydrate binding module (Family 6) {ECO:0000313|EMBL:SFD27234.1};
GN ORFNames=SAMN04487987_1087 {ECO:0000313|EMBL:SFD27234.1};
OS Algibacter pectinivorans.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Algibacter.
OX NCBI_TaxID=870482 {ECO:0000313|EMBL:SFD27234.1, ECO:0000313|Proteomes:UP000199439};
RN [1] {ECO:0000313|Proteomes:UP000199439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25730 {ECO:0000313|Proteomes:UP000199439};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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; FOMI01000008; SFD27234.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1QYM6; -.
DR STRING; 870482.SAMN04487987_1087; -.
DR OrthoDB; 9763933at2; -.
DR Proteomes; UP000199439; Unassembled WGS sequence.
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; 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; 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:UP000199439};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
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 454 AA; 52358 MW; 00D48CDD0EE8FA89 CRC64;
MLELVHLRNN YAFLLLVGIC NLYAQNPIVP NQGLNDPHIH IFNDTAYVYA SHDKSIDNKK
FIMEDWWVLS SPDLVNWTKR SVLNPKDTYI GKDFSRCWAT DAAYKNGKYY WYFSEGNEQT
GVVVGDTPTG PWKDHLGKPL LNSDLTPTHE YDMAVFEDNG AHYIIFGVWD YYMAKLNDDM
ISLAEKPRKL IINNPKGPYN PEGNNLEKPT DDKPFMHKRN GKYYLSWGCF YAMSDNLYGP
YEYKDSVIKE ESFAKGYNAP TWPNGFLQGR HGSFFEWNNQ WYYAYCDISQ TGNRYFRDTF
ISYIHYKENG EMATIRVDGV GVGQYNANQS NIEAEDYFKA DGLLKKEFEN GFVVKTAANK
SYLSFPNING LDKYSILNMK VNAPNGGQFS IQIRKNGLDG EIINQKIVNL KPNTNTFKTI
QIDLQDLKST ENFYFLVQQL DSNSLQIDSF SFSK
//
