ID B3PD60_CELJU Unreviewed; 334 AA.
AC B3PD60;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Beta-xylosidase/alpha-L-arabinfuranosidase, putative, gly43N {ECO:0000313|EMBL:ACE83886.1};
DE EC=3.2.1.- {ECO:0000313|EMBL:ACE83886.1};
GN Name=gly43N {ECO:0000313|EMBL:ACE83886.1};
GN OrderedLocusNames=CJA_3018 {ECO:0000313|EMBL:ACE83886.1};
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:ACE83886.1, ECO:0000313|Proteomes:UP000001036};
RN [1] {ECO:0000313|EMBL:ACE83886.1, ECO:0000313|Proteomes:UP000001036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107 {ECO:0000313|EMBL:ACE83886.1,
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).
RN [2] {ECO:0007829|PDB:3QED, ECO:0007829|PDB:3QEE}
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 28-334 IN COMPLEX WITH CALCIUM.
RX PubMed=21339299; DOI=10.1074/jbc.M110.215962;
RA Cartmell A., McKee L.S., Pena M.J., Larsbrink J., Brumer H., Kaneko S.,
RA Ichinose H., Lewis R.J., Vikso-Nielsen A., Gilbert H.J., Marles-Wright J.;
RT "The structure and function of an arabinan-specific alpha-1,2-
RT arabinofuranosidase identified from screening the activities of bacterial
RT GH43 glycoside hydrolases.";
RL J. Biol. Chem. 286:15483-15495(2011).
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; ACE83886.1; -; Genomic_DNA.
DR PDB; 3QED; X-ray; 2.99 A; A/B/C/D=28-334.
DR PDB; 3QEE; X-ray; 1.64 A; A/B=28-334.
DR PDB; 3QEF; X-ray; 1.79 A; A/B=28-334.
DR PDBsum; 3QED; -.
DR PDBsum; 3QEE; -.
DR PDBsum; 3QEF; -.
DR AlphaFoldDB; B3PD60; -.
DR SMR; B3PD60; -.
DR STRING; 498211.CJA_3018; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR KEGG; cja:CJA_3018; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_009397_4_1_6; -.
DR OrthoDB; 9760116at2; -.
DR EvolutionaryTrace; B3PD60; -.
DR Proteomes; UP000001036; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd18618; GH43_Xsa43E-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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:3QED, ECO:0007829|PDB:3QEE};
KW Calcium {ECO:0007829|PDB:3QED, ECO:0007829|PDB:3QEE};
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 Metal-binding {ECO:0007829|PDB:3QED, ECO:0007829|PDB:3QEE};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000001036};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..334
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002793942"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007829|PDB:3QED, ECO:0007829|PDB:3QEE"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007829|PDB:3QED, ECO:0007829|PDB:3QEE"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007829|PDB:3QED, ECO:0007829|PDB:3QEE"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007829|PDB:3QED, ECO:0007829|PDB:3QEE"
FT SITE 168
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 334 AA; 37550 MW; C474606B29DD4322 CRC64;
MTTSLNSRRL WLHRLCALLL GTGSALVQAE NPIFTDVFTA DPAALVHKGR VYLYAGRDEA
PDNTTFFVMN EWLVYSSDDM ANWEAHGPGL RAKDFTWAKG DAWASQVIER NGKFYWYVTV
RHDDTKPGFA IGVAVGDSPI GPFKDALGKA LITNDMTTDT PIDWDDIDPS VFIDDDGQAY
LFWGNTRPRY AKLKKNMVEL DGPIRAIEGL PEFTEAIWVH KYQDNYYLSY AMGFPEKIGY
AMGKSIKGPW VYKGILNEVA GNTPTNHQAI IEFNNKHYFI YHTGAGRPDG GQYRRSVSID
ELFYNPDGTI KRIVMTTEGV APNKSPERVK KAAK
//
