ID   NODB_NEOGA              Reviewed;         214 AA.
AC   P50354;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Chitooligosaccharide deacetylase;
DE            EC=3.5.1.-;
DE   AltName: Full=Nodulation protein B;
GN   Name=nodB;
OS   Neorhizobium galegae (Rhizobium galegae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Neorhizobium.
OX   NCBI_TaxID=399;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HAMBI 1174;
RX   PubMed=10474187; DOI=10.1111/j.1574-6968.1999.tb13735.x;
RA   Suominen L., Paulin L., Saano A., Saren A.-M., Tas E., Lindstroem K.;
RT   "Identification of nodulation promoter (nod-box) regions of Rhizobium
RT   galegae.";
RL   FEMS Microbiol. Lett. 177:217-223(1999).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC       {ECO:0000305}.
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DR   EMBL; X87578; CAA60878.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50354; -.
DR   SMR; P50354; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   InterPro; IPR026402; Nodulat_NodB.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; SSF88713; 1.
DR   TIGRFAMs; TIGR04243; nodulat_NodB; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metal-binding; Nodulation.
FT   CHAIN           1..214
FT                   /note="Chitooligosaccharide deacetylase"
FT                   /id="PRO_0000172750"
FT   DOMAIN          19..211
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT   ACT_SITE        26
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        172
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         81
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   SITE            146
FT                   /note="Raises pKa of active site His"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   214 AA;  22779 MW;  47003C7EB066319B CRC64;
     MKNLNIIDSV DVDAGADDPC VYLTFDDGPN PFCTPHILDV LAQHAVSATF FVIGANAEVH
     PGLVQRIVSE GHGVANHTMT HPDLATCSRP QVEREIDEAN RAIISACPGA SIRHIRAPYG
     KWTEEALVKS ASLGLAPVHW SVDPRDWSCP GVDAIVDRVL AAAKPGSIVL LHEDGPPGAA
     DPTKLPTLRD QTLAAISAII KSLRSRGLTI RSLP