ID   B3PD60_CELJU            Unreviewed;       334 AA.
AC   B3PD60;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   02-SEP-2026, entry version 87.
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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Cellvibrionales; 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 CA(2+).
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   RefSeq; WP_012488597.1; NC_010995.1.
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   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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd18618; GH43_Xsa43E-like; 1.
DR   Gene3D; 2.115.10.20; Glycosyl hydrolase domain, family 43; 1.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   InterPro; IPR052176; Glycosyl_Hydrlase_43_Enz.
DR   PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR   PANTHER; PTHR43772:SF2; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04480)-RELATED; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   PDBsum; 3QED; -.
DR   PDBsum; 3QEE; -.
DR   PDBsum; 3QEF; -.
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:3QEF"
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: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
//