ID B3PCV3_CELJU Unreviewed; 338 AA.
AC B3PCV3;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Beta-xylosidase/alpha-L-arabinfuranosidase, putative, gly43F {ECO:0000313|EMBL:ACE84353.1};
DE EC=3.2.1.- {ECO:0000313|EMBL:ACE84353.1};
GN Name=gly43F {ECO:0000313|EMBL:ACE84353.1};
GN OrderedLocusNames=CJA_1316 {ECO:0000313|EMBL:ACE84353.1};
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211 {ECO:0000313|EMBL:ACE84353.1, ECO:0000313|Proteomes:UP000001036};
RN [1] {ECO:0000313|EMBL:ACE84353.1, ECO:0000313|Proteomes:UP000001036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107 {ECO:0000313|EMBL:ACE84353.1,
RC ECO:0000313|Proteomes:UP000001036};
RX PubMed=18556790; DOI=10.1128/JB.01701-07;
RA Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; CP000934; ACE84353.1; -; Genomic_DNA.
DR RefSeq; WP_012486952.1; NC_010995.1.
DR AlphaFoldDB; B3PCV3; -.
DR STRING; 498211.CJA_1316; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR KEGG; cja:CJA_1316; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_009397_4_1_6; -.
DR OrthoDB; 9760116at2; -.
DR Proteomes; UP000001036; Chromosome.
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:UP000001036};
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; 38110 MW; 479035B6DA74C964 CRC64;
MSTENEVVDY KALAARAISQ PLVTHIYTAD PSAHVFNGKV YIYPSHDIDA GIPFNDNGDH
FGMEDYHVLR MDSPEGKAED CGVALHVKDV PWAERQMWAP DAITKDGKYY LYFPARARDG
LFKIGVAIGD QPEGPFVAEP EPIAGSYSID PAVFGDDDGE FYLYFGGIWG GQLQKYRDNT
YSEIHEEPTA DQPALGARVA RLSADMKSFV EASREVVILD EQGQPLLAGD NSRRYFEGPW
MHKYQGKYYL SYSTGDTHFL CYATSDNPYG PFTYQGQILT PVVGWTTHHS ICEFEGKWYL
FYHDSVLSEG VTHLRSVKVT ELHYEADGKI KTIHPYRD
//
