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NODB_AZOC5
ID   NODB_AZOC5              Reviewed;         210 AA.
AC   Q07740; A8IP10;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Chitooligosaccharide deacetylase;
DE            EC=3.5.1.-;
DE   AltName: Full=Nodulation protein B;
GN   Name=nodB; OrderedLocusNames=AZC_3817;
OS   Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS   6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Azorhizobium.
OX   NCBI_TaxID=438753;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2615763; DOI=10.1007/bf00261190;
RA   Goethals K., Gao M., Tomekpe K., van Montagu M., Holsters M.;
RT   "Common nodABC genes in Nod locus 1 of Azorhizobium caulinodans: nucleotide
RT   sequence and plant-inducible expression.";
RL   Mol. Gen. Genet. 219:289-298(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB
RC   13405 / ORS 571;
RA   Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA   Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA   Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT   "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT   caulinodans ORS571.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; L18897; AAB51163.1; -; Genomic_DNA.
DR   EMBL; AP009384; BAF89815.1; -; Genomic_DNA.
DR   PIR; JQ0394; JQ0394.
DR   RefSeq; WP_012172340.1; NC_009937.1.
DR   AlphaFoldDB; Q07740; -.
DR   SMR; Q07740; -.
DR   STRING; 438753.AZC_3817; -.
DR   EnsemblBacteria; BAF89815; BAF89815; AZC_3817.
DR   KEGG; azc:AZC_3817; -.
DR   eggNOG; COG0726; Bacteria.
DR   HOGENOM; CLU_021264_0_0_5; -.
DR   OMA; NHAMRDE; -.
DR   OrthoDB; 1701876at2; -.
DR   Proteomes; UP000000270; Chromosome.
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; Reference proteome.
FT   CHAIN           1..210
FT                   /note="Chitooligosaccharide deacetylase"
FT                   /id="PRO_0000172746"
FT   DOMAIN          15..207
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT   ACT_SITE        22
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        168
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   SITE            142
FT                   /note="Raises pKa of active site His"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        44..45
FT                   /note="AT -> TA (in Ref. 1; AAB51163)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        53
FT                   /note="A -> T (in Ref. 1; AAB51163)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        137
FT                   /note="S -> P (in Ref. 1; AAB51163)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        162
FT                   /note="G -> S (in Ref. 1; AAB51163)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   210 AA;  23348 MW;  2915069D19E46091 CRC64;
     MSVLGQAARI TQNQSSIYIT FDDGPHPSVT PAVCEILREH SALATFFQIG RFAKEYPSIS
     RQCQLDGHAI GNHTFDHPNL QDRAGEEVEY QISSAQKCLE HICGRGFVRH FRAPYGAWST
     QILNVVNKIG LRPVSWSVDP RDWEAPRIEN LINEILDNAR PGSIILLHDG CPPDEAAMWD
     VRGGRAQTLA ALRYVVPALQ ARGFALQPLP
 
 
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