ID Q0BV36_GRABC Unreviewed; 311 AA.
AC Q0BV36;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN OrderedLocusNames=GbCGDNIH1_0418 {ECO:0000313|EMBL:ABI61316.1};
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165 {ECO:0000313|EMBL:ABI61316.1, ECO:0000313|Proteomes:UP000001963};
RN [1] {ECO:0000313|EMBL:ABI61316.1, ECO:0000313|Proteomes:UP000001963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1 {ECO:0000313|Proteomes:UP000001963};
RX PubMed=17827295; DOI=10.1128/JB.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA Kupko J.J.III., Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(2007).
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}.
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DR EMBL; CP000394; ABI61316.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0BV36; -.
DR STRING; 391165.GbCGDNIH1_0418; -.
DR KEGG; gbe:GbCGDNIH1_0418; -.
DR eggNOG; COG0726; Bacteria.
DR HOGENOM; CLU_029940_0_0_5; -.
DR OMA; DDLPYWE; -.
DR Proteomes; UP000001963; 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; 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 Hydrolase {ECO:0000313|EMBL:ABI61316.1};
KW Nodulation {ECO:0000256|ARBA:ARBA00022458};
KW Reference proteome {ECO:0000313|Proteomes:UP000001963}.
FT DOMAIN 72..289
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 311 AA; 35427 MW; 689F920459D2A596 CRC64;
MALDNETYPR DLIGYGKTPP FARWPGGARI AVNFVVNYEE GGENSILHGD SASEAFLSEM
IGAQPVPGLR HMNMESLYEY GSRVGFWRLM RLFDSYRLPF TCFAVGMALE RHPEAAQAMM
AAGHEIASHG YRWIDYQFAT EDAERADLAR AIEAHRRVTG KRPLGWYLGR CSPHTHRLIA
EEGGFLYNAD TYADDLPYWD LHHDRPQLMV PYTLDANDMR FATAQGFNTA EHFFTYLRDS
FDTLYEEGAV TPRMMSIGLH CRLAGRPGRL PGLKRFIDHV LAHDGVWICR REDIARHWHE
THPPPAQCVP G
//