ID A0A1I1BVK5_9BACL Unreviewed; 299 AA.
AC A0A1I1BVK5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Glycosyl hydrolases family 43 {ECO:0000313|EMBL:SFB54311.1};
GN ORFNames=SAMN05216312_112159 {ECO:0000313|EMBL:SFB54311.1};
OS Cohnella sp. OV330.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=1855288 {ECO:0000313|EMBL:SFB54311.1, ECO:0000313|Proteomes:UP000198686};
RN [1] {ECO:0000313|EMBL:SFB54311.1, ECO:0000313|Proteomes:UP000198686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV330 {ECO:0000313|EMBL:SFB54311.1,
RC ECO:0000313|Proteomes:UP000198686};
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, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; FOKE01000012; SFB54311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1BVK5; -.
DR Proteomes; UP000198686; 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; cd18827; GH43_XlnD-like; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR PANTHER; PTHR43772:SF7; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04480)-RELATED; 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:ARBA00022651};
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:UP000198686};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SITE 133
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 299 AA; 34326 MW; 94251B7D2E6EED32 CRC64;
MKMNNPIVPG WYADPEARTY AGKHWIFATR SFTEYTMQMN LDAFSSDDLV HWDKHEGIVD
MADFPWIWRA VWAPTHIEHR GRYYLVFASN DIQSNEETGG LEIAVADRPE GPYRGYLGRP
LVDKFIHQAQ PIDAHLFKDD DGTVYLYYGG WGHCNVARMN EEMTGFVSLM GESDEVFRSI
TPEGYVEGPC MIKKDGLYYL MWSMGGWTNG TYRVAYGVSD NPLGPFENQG TILERQEPIA
EGPGHHGYLH LQETDEWLIV YHRRTIGDTE PGNRRLCIDR MRIGGGTIEP VVMTDTWER
//
