ID A0A1H0ZX06_9GAMM Unreviewed; 338 AA.
AC A0A1H0ZX06;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Glycosyl hydrolases family 43 {ECO:0000313|EMBL:SDQ31892.1};
GN ORFNames=SAMN05216569_0622 {ECO:0000313|EMBL:SDQ31892.1};
OS Pseudoxanthomonas sp. CF125.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1855303 {ECO:0000313|EMBL:SDQ31892.1, ECO:0000313|Proteomes:UP000199049};
RN [1] {ECO:0000313|EMBL:SDQ31892.1, ECO:0000313|Proteomes:UP000199049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF125 {ECO:0000313|EMBL:SDQ31892.1,
RC ECO:0000313|Proteomes:UP000199049};
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; FNLD01000001; SDQ31892.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0ZX06; -.
DR STRING; 1855303.SAMN05216569_0622; -.
DR Proteomes; UP000199049; 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; cd18619; GH43_CoXyl43_like; 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:UP000199049};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SITE 150
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 338 AA; 37961 MW; 53182439205D55D5 CRC64;
MSDESAFVDL QALAAKAISQ PLVSHIYTAD PSAHVFDGCL YIYPSHDIDA GIPFNDDGDH
FGMQDYHVLR MESPDGEAID CGVALHIKDV PWAERQMWAP DVAYRDGNYY LYFPAKRADG
IFQIGVAVSD NPAGPFVAER QAIEGSYSID PAAFTDDDGT CYLYFGGLWG GQLQKYRDNA
YDTSHEEPMA DRPALGPRVA RLEEGMKRFA EAPREVLIVD EAGQPLRADD HARRYFEGPW
MHKHLGKYYL SYSTGNTHLL CYALSDSPYG PFVYQGVILQ PVVGWTTHHS ICQFQDRWYL
FYHDSLLSGG VTHLRSVKVT ELHYDGQGRI RTIDPYGG
//
