NODB_RHILO
ID NODB_RHILO Reviewed; 219 AA.
AC Q52845;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Chitooligosaccharide deacetylase;
DE EC=3.5.1.-;
DE AltName: Full=Nodulation protein B;
GN Name=nodB; OrderedLocusNames=mlr6175;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.
RC STRAIN=NZP 2213;
RX PubMed=8850088; DOI=10.1094/mpmi-9-0187;
RA Scott D.B., Young C.A., Collins-Emerson J.M., Terzaghi E.A., Rockman E.S.,
RA Lewis P.E., Pankhurst C.E.;
RT "Novel and complex chromosomal arrangement of Rhizobium loti nodulation
RT genes.";
RL Mol. Plant Microbe Interact. 9:187-197(1996).
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; BA000012; BAB52508.1; -; Genomic_DNA.
DR EMBL; X65620; CAA46575.1; -; Genomic_DNA.
DR PIR; S21412; S21412.
DR RefSeq; WP_010913829.1; NC_002678.2.
DR AlphaFoldDB; Q52845; -.
DR SMR; Q52845; -.
DR STRING; 266835.14025909; -.
DR EnsemblBacteria; BAB52508; BAB52508; BAB52508.
DR KEGG; mlo:mlr6175; -.
DR eggNOG; COG0726; Bacteria.
DR HOGENOM; CLU_021264_0_1_5; -.
DR OMA; NHAMRDE; -.
DR OrthoDB; 1701876at2; -.
DR Proteomes; UP000000552; 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.
FT CHAIN 1..219
FT /note="Chitooligosaccharide deacetylase"
FT /id="PRO_0000172751"
FT DOMAIN 21..213
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 CONFLICT 9..10
FT /note="KV -> EA (in Ref. 2; CAA46575)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 219 AA; 24091 MW; 6A6E5AAC8B506C26 CRC64;
MRRLDDRWKV QSECADGTGR RSVYLTFDDG PNPCFTPQIL DVLAQNRVPA TFFVIGAYAA
EHPELIQRMI AEGHEVGNHT MSHPDLSKCG LGEVQREVFE ANQAIMLACP QASIRYIRAP
YGAWSEEVFT ASEIAGLAAL HWSIDPRDWS RPGTDAIVDA VLASVRPGAI VLLHDGCPPD
ESTRSTQASL RNQTVMALSN LIPALDACGY EIRSLPEHH