ID B3PW75_RHIE6 Unreviewed; 307 AA.
AC B3PW75;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN OrderedLocusNames=RHECIAT_CH0003364 {ECO:0000313|EMBL:ACE92312.1};
OS Rhizobium etli (strain CIAT 652).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=491916 {ECO:0000313|EMBL:ACE92312.1, ECO:0000313|Proteomes:UP000008817};
RN [1] {ECO:0000313|EMBL:ACE92312.1, ECO:0000313|Proteomes:UP000008817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIAT 652 {ECO:0000313|EMBL:ACE92312.1,
RC ECO:0000313|Proteomes:UP000008817};
RA Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA Palacios R., Davila G.;
RT "Genome diversity and DNA divergence of Rhizobium etli.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Is involved in generating a small heat-stable compound (Nod),
CC an acylated oligomer of N-acetylglucosamine, that stimulates mitosis in
CC various plant protoplasts. {ECO:0000256|ARBA:ARBA00003236}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000256|ARBA:ARBA00010973}.
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DR EMBL; CP001074; ACE92312.1; -; Genomic_DNA.
DR AlphaFoldDB; B3PW75; -.
DR KEGG; rec:RHECIAT_CH0003364; -.
DR eggNOG; COG0726; Bacteria.
DR HOGENOM; CLU_029940_0_0_5; -.
DR Proteomes; UP000008817; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd10977; CE4_PuuE_SpCDA1; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR InterPro; IPR017625; PuuE.
DR NCBIfam; TIGR03212; uraD_N-term-dom; 1.
DR PANTHER; PTHR43123; POLYSACCHARIDE DEACETYLASE-RELATED; 1.
DR PANTHER; PTHR43123:SF1; POLYSACCHARIDE DEACETYLASE-RELATED; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS51677; NODB; 1.
PE 3: Inferred from homology;
KW Nodulation {ECO:0000256|ARBA:ARBA00022458}.
FT DOMAIN 70..289
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 307 AA; 34993 MW; 4A8F96D76214F8CE CRC64;
MVSESYPRNL VGYGRQTPDP KWPEEACVAV QFVINYEEGG ESSILDGDPA SENLLSEIVG
AAAWPGQRNL NMESIYEYGS RAGFWRLWRM FTDLKVQATV YGVTLAMARN PEAVAAMKEA
GWEIASHGYR WLEYKDFPED LERKHILEAV RLHTELTGER PYGMYQGKPS DNTLRLVQEE
GGFLYSSDSY ADDLPYWVKG VDGKPFLIIP YTLETNDMRF ATPQGFNAGD QFFTYLKDAF
DTLYEEGQAG SPKMMSVGLH CRLVGRPGRA AALKRFIEYV LKHDKVWIPR RIEIAEHWHQ
HHQPGAL
//
