NODB_RHIME
ID NODB_RHIME Reviewed; 217 AA.
AC P02963; O52477;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Chitooligosaccharide deacetylase;
DE EC=3.5.1.-;
DE AltName: Full=Nodulation protein B;
GN Name=nodB; OrderedLocusNames=RA0474; ORFNames=SMa0868;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymA (megaplasmid 1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=4006668; DOI=10.1089/dna.1985.4.241;
RA Egelhoff T.T., Fisher R.F., Jacobs T.W., Mulligan J.T., Long S.R.;
RT "Nucleotide sequence of Rhizobium meliloti 1021 nodulation genes: nodD is
RT read divergently from nodABC.";
RL DNA 4:241-248(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=41;
RX PubMed=6336331; DOI=10.1093/nar/12.24.9509;
RA Toeroek I., Kondorosi E., Stepkowski T., Posfai J., Kondorosi A.;
RT "Nucleotide sequence of Rhizobium meliloti nodulation genes.";
RL Nucleic Acids Res. 12:9509-9524(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=042B;
RA Yang X., Gao W.M., Yang S.S.;
RT "The complete sequence of S. meliloti 042B nodABC.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481432; DOI=10.1073/pnas.161294798;
RA Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F.,
RA Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L.,
RA Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C.,
RA Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A.,
RA Long S.R.;
RT "Nucleotide sequence and predicted functions of the entire Sinorhizobium
RT meliloti pSymA megaplasmid.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
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; M11268; AAA98361.1; -; Genomic_DNA.
DR EMBL; X01649; CAA25809.1; -; Genomic_DNA.
DR EMBL; AF038577; AAB95330.1; -; Genomic_DNA.
DR EMBL; AE006469; AAK65132.1; -; Genomic_DNA.
DR PIR; A03483; ZZZRBM.
DR PIR; A03484; ZZZRB4.
DR PIR; B95321; B95321.
DR RefSeq; NP_435720.1; NC_003037.1.
DR RefSeq; WP_003532851.1; NC_003037.1.
DR AlphaFoldDB; P02963; -.
DR SMR; P02963; -.
DR EnsemblBacteria; AAK65132; AAK65132; SMa0868.
DR GeneID; 25011385; -.
DR GeneID; 61599276; -.
DR KEGG; sme:SMa0868; -.
DR PATRIC; fig|266834.11.peg.485; -.
DR HOGENOM; CLU_021264_0_0_5; -.
DR OMA; NHAMRDE; -.
DR BRENDA; 3.5.1.41; 5347.
DR PRO; PR:P02963; -.
DR Proteomes; UP000001976; Plasmid pSymA.
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; Plasmid;
KW Reference proteome.
FT CHAIN 1..217
FT /note="Chitooligosaccharide deacetylase"
FT /id="PRO_0000172755"
FT DOMAIN 21..211
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT ACT_SITE 28
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 174
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT SITE 148
FT /note="Raises pKa of active site His"
FT /evidence="ECO:0000250"
FT VARIANT 10
FT /note="V -> M (in strain: 41)"
FT VARIANT 59
FT /note="A -> T (in strain: 41)"
FT VARIANT 116
FT /note="H -> R (in strain: 41)"
FT VARIANT 195..198
FT /note="ALSR -> GFPV (in strain: O42B)"
FT CONFLICT 108..118
FT /note="ACPQAAVRHIR -> LVLRPRSDTYE (in Ref. 1; AAA98361)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 217 AA; 23672 MW; 01F82A0C75EA662D CRC64;
MKHLDYIHEV PSNCDYGTED RSIYLTFDDG PNPHCTPEIL DVLAEYGVPA TFFVIGTYAK
SQPELIRRIV AEGHEVANHT MTHPDLSTCG PHEVEREIVE ASEAIIAACP QAAVRHIRAP
YGVWSEEALT RSASAGLTAI HWSADPRDWS RPGANAIVDA VLDSVRPGAI VLLHDGCPPD
ESGALTGLRD QTLMALSRIV PALHERGFAI RPLPPHH
