ID   B3PFB4_CELJU            Unreviewed;       288 AA.
AC   B3PFB4;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   02-SEP-2026, entry version 68.
DE   SubName: Full=Polysaccharide deacetylase, putative, pda4C {ECO:0000313|EMBL:ACE85263.1};
DE            EC=4.2.2.- {ECO:0000313|EMBL:ACE85263.1};
GN   Name=pda4C {ECO:0000313|EMBL:ACE85263.1};
GN   OrderedLocusNames=CJA_3428 {ECO:0000313|EMBL:ACE85263.1};
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:ACE85263.1, ECO:0000313|Proteomes:UP000001036};
RN   [1] {ECO:0000313|EMBL:ACE85263.1, ECO:0000313|Proteomes:UP000001036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ueda107 {ECO:0000313|EMBL:ACE85263.1,
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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01014}.
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DR   EMBL; CP000934; ACE85263.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3PFB4; -.
DR   STRING; 498211.CJA_3428; -.
DR   KEGG; cja:CJA_3428; -.
DR   eggNOG; COG0726; Bacteria.
DR   HOGENOM; CLU_066872_0_0_6; -.
DR   Proteomes; UP000001036; Chromosome.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd10941; CE4_PuuE_HpPgdA_like_2; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   InterPro; IPR022560; DUF3473.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   InterPro; IPR045235; PuuE_HpPgdA-like.
DR   InterPro; IPR014344; XrtA_polysacc_deacetyl.
DR   NCBIfam; TIGR03006; pepcterm_polyde; 1.
DR   PANTHER; PTHR47561; POLYSACCHARIDE DEACETYLASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G05030); 1.
DR   PANTHER; PTHR47561:SF1; POLYSACCHARIDE DEACETYLASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G05030); 1.
DR   Pfam; PF11959; DUF3473; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:ACE85263.1};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01014};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001036}.
FT   DOMAIN          12..288
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   BINDING         20
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01014"
FT   BINDING         73
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01014"
FT   BINDING         77
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01014"
SQ   SEQUENCE   288 AA;  33477 MW;  DF10330D6A08A5C1 CRC64;
     MEDYYHVAAF AKVIKPSEWD QWPSRVEANT QRLLQVFSDH GITITFFILG WVAERYPQLV
     RDIQTQGHEI ASHGYSHQLI YRQDPQTFRR ETEKSKQLLE DITQAPITGY RAASYSITRS
     SLWALDILAE LGFTWDSSIF PTRHDNYGIP GSPEEPYRII TRSGASLIEF PLTTAKVWGQ
     SIPAAGGGYF RQYPYALSRW LFQRASDNQS KPQIFYLHPW EIDPEQPRVP NASWFSNFRH
     YTNLKRCLPR LERMIQDFPF GTMSKSLGST RVERELHVTE LAQQPLTE
//