ID Q335D3_9BRAD Unreviewed; 68 AA.
AC Q335D3;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
DE Flags: Fragment;
GN Name=nodB {ECO:0000313|EMBL:CAI65292.1};
OS Bradyrhizobium sp. WSM1735.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=319004 {ECO:0000313|EMBL:CAI65292.1};
RN [1] {ECO:0000313|EMBL:CAI65292.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WSM1735 {ECO:0000313|EMBL:CAI65292.1};
RX PubMed=16269740; DOI=10.1128/AEM.71.11.7041-7052.2005;
RA Stepkowski T., Moulin L., Krzyzanska A., McInnes A., Law I.J., Howieson J.;
RT "European origin of Bradyrhizobium populations infecting lupins and
RT serradella in soils of Western Australia and South Africa.";
RL Appl. Environ. Microbiol. 71:7041-7052(2005).
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; AJ890293; CAI65292.1; -; Genomic_DNA.
DR AlphaFoldDB; Q335D3; -.
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 Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR PANTHER; PTHR10587:SF105; CHITIN DEACETYLASE 1-RELATED; 1.
DR PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-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 21..68
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT NON_TER 68
FT /evidence="ECO:0000313|EMBL:CAI65292.1"
SQ SEQUENCE 68 AA; 7582 MW; 3BAB82E9B14DA205 CRC64;
MTYLDRLCEV RSEYADRTES RGVYLTFDDG PDPLCTPDIL DVLAEHGVPA TFFVIGAYAA
DQPKLIQT
//
