ID Q0BW66_GRABC Unreviewed; 295 AA.
AC Q0BW66;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-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_0038 {ECO:0000313|EMBL:ABI60936.1};
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165 {ECO:0000313|EMBL:ABI60936.1, ECO:0000313|Proteomes:UP000001963};
RN [1] {ECO:0000313|EMBL:ABI60936.1, 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; ABI60936.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0BW66; -.
DR STRING; 391165.GbCGDNIH1_0038; -.
DR KEGG; gbe:GbCGDNIH1_0038; -.
DR eggNOG; COG0726; Bacteria.
DR HOGENOM; CLU_932580_0_0_5; -.
DR OrthoDB; 9784220at2; -.
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; cd10941; CE4_PuuE_HpPgdA_like_2; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR045235; CE4_PuuE_HpPgdA-like_2.
DR InterPro; IPR022560; DUF3473.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:ABI60936.1};
KW Nodulation {ECO:0000256|ARBA:ARBA00022458};
KW Reference proteome {ECO:0000313|Proteomes:UP000001963}.
FT DOMAIN 45..136
FT /note="NodB homology"
FT /evidence="ECO:0000259|Pfam:PF01522"
FT DOMAIN 154..272
FT /note="DUF3473"
FT /evidence="ECO:0000259|Pfam:PF11959"
SQ SEQUENCE 295 AA; 32595 MW; 8F5236899A6C3F8F CRC64;
MIRSKANRLL PARSLTALIL GRPDHPVTFS VDLEDHGGGL DRLAGNASRL LDWLASNHVR
ATIFTVGELG RTAPAIIRRF AEAGHEIACH GEVHERLEQL SPAQLRTGLI AARQRLSDLS
GQSVEGFRAP EFSLTPLTPW VPNVLAEAGY LWSSSVMPTR LRGGKAPIGW AGLPARPFLW
PSGVLEIPVP LLRIGPFHVP FMGGMWLRYL PLPLLRLAVK RMGGQPSWAY CHPYDIDTKE
KFSLLPGRSC VASMAMWANR GRMVERMTIL AANPAPCFGE RVPLWRQQAV TIQKQ
//
