ID A0A1I0DY45_THASX Unreviewed; 356 AA.
AC A0A1I0DY45;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Glycosyl hydrolases family 43 {ECO:0000313|EMBL:SET37653.1};
GN ORFNames=SAMN05660429_01652 {ECO:0000313|EMBL:SET37653.1};
OS Thalassotalea agarivorans (Thalassomonas agarivorans).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Thalassotalea.
OX NCBI_TaxID=349064 {ECO:0000313|EMBL:SET37653.1, ECO:0000313|Proteomes:UP000199308};
RN [1] {ECO:0000313|EMBL:SET37653.1, ECO:0000313|Proteomes:UP000199308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19706 {ECO:0000313|EMBL:SET37653.1,
RC ECO:0000313|Proteomes:UP000199308};
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; FOHK01000007; SET37653.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0DY45; -.
DR STRING; 349064.SAMN05660429_01652; -.
DR OrthoDB; 9794572at2; -.
DR Proteomes; UP000199308; 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:InterPro.
DR CDD; cd08992; GH117; 1.
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.
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:UP000199308};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SITE 202
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 356 AA; 40259 MW; 4B246C2B28131CDD CRC64;
MSEKKLSLAS KRAIERGYDE KGPEWLTEFD ITPLKGDFAF EEGVIRRDPT SVIKVDGLYH
CWYTKGSGET VGFGGNPEDK VFPWDLTEVW HATSEDAETW TEQSVAISRG EPGSFDDRAV
FTPEILAHNG KYYLVYQTVQ YPYTNRQYEE IALATADTPF GPWEKSKAPI LSPSKDGQWK
GDEDNRFHVY EKGSFDSHKV HDPCLLVFND KFYLYYKGET MGESMNFGGR EIKHGVAIAD
NIEGPYVKSE YNPISNSGHE VVVWNYQGGV ATLLTTDGPE KNTIQFAPDG INFDIKAHVK
GGPEAMGLYR PEQELPEPGL SWGLCHKYDP SWNWNYICKF TPRKQVLDAG TFQNTA
//