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