ID G6EEP5_9SPHN Unreviewed; 269 AA.
AC G6EEP5;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN ORFNames=NSU_2816 {ECO:0000313|EMBL:EHJ60226.1};
OS Novosphingobium pentaromativorans US6-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1088721 {ECO:0000313|EMBL:EHJ60226.1, ECO:0000313|Proteomes:UP000004030};
RN [1] {ECO:0000313|EMBL:EHJ60226.1, ECO:0000313|Proteomes:UP000004030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=US6-1 {ECO:0000313|EMBL:EHJ60226.1,
RC ECO:0000313|Proteomes:UP000004030};
RX PubMed=22275104; DOI=10.1128/JB.06476-11;
RA Luo Y.R., Kang S.G., Kim S.J., Kim M.R., Li N., Lee J.H., Kwon K.K.;
RT "Genome sequence of benzo(a)pyrene-degrading bacterium Novosphingobium
RT pentaromativorans US6-1.";
RL J. Bacteriol. 194:907-907(2012).
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 -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000256|ARBA:ARBA00010973}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHJ60226.1}.
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DR EMBL; AGFM01000041; EHJ60226.1; -; Genomic_DNA.
DR AlphaFoldDB; G6EEP5; -.
DR STRING; 1088721.JI59_06025; -.
DR PATRIC; fig|1088721.3.peg.2782; -.
DR eggNOG; COG0726; Bacteria.
DR Proteomes; UP000004030; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000004030}.
FT DOMAIN 40..253
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 269 AA; 30215 MW; 413D282D5EDDEE1D CRC64;
MQFVINYEEG AENCVLNGDA GSECFLSDMV GAVSHPDRAM AMESLYEYGS RAGFWRLHRL
FVQRGLPVTV FGVARALEMN PDAVEAMLAA DWEIASHGLR WIDYQNVPED VERAHISQAI
ALHAQVTGQR PLGWYQGRTS PNTARLIAEE GGFLYDADSY ADDVPYWSRH HGKPQLIVPY
SLDANDMKMV ALNGFTEGEQ FFRYLRDTFD QLRDEGGRMM SIGLHARIAG HPARARAVAR
FIDHVVASGD AWVARRIDIA RHWIAEHPA
//
