ID Q89GP0_BRADU Unreviewed; 371 AA.
AC Q89GP0;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN OrderedLocusNames=bll6305 {ECO:0000313|EMBL:BAC51570.1};
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=224911 {ECO:0000313|EMBL:BAC51570.1, ECO:0000313|Proteomes:UP000002526};
RN [1] {ECO:0000313|Proteomes:UP000002526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110
RC {ECO:0000313|Proteomes:UP000002526};
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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. {ECO:0000256|ARBA:ARBA00003236}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000256|ARBA:ARBA00010973}.
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DR EMBL; BA000040; BAC51570.1; -; Genomic_DNA.
DR RefSeq; NP_772945.1; NC_004463.1.
DR AlphaFoldDB; Q89GP0; -.
DR STRING; 224911.AAV28_29085; -.
DR EnsemblBacteria; BAC51570; BAC51570; BAC51570.
DR KEGG; bja:bll6305; -.
DR eggNOG; COG0726; Bacteria.
DR HOGENOM; CLU_030024_1_2_5; -.
DR InParanoid; Q89GP0; -.
DR OrthoDB; 9814639at2; -.
DR PhylomeDB; Q89GP0; -.
DR Proteomes; UP000002526; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd10968; CE4_Mlr8448_like_5s; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR PANTHER; PTHR34216; -; 1.
DR PANTHER; PTHR34216:SF7; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE N-DEACETYLASE; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS51677; NODB; 1.
PE 3: Inferred from homology;
KW Nodulation {ECO:0000256|ARBA:ARBA00022458};
KW Reference proteome {ECO:0000313|Proteomes:UP000002526};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 120..371
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 371 AA; 42159 MW; F4B188DE36A007F0 CRC64;
METAVCDRPV AMHCVCDLAL WDRNPATRRM VLRMNPIVKD CIYYGASRIG ELPFFRAHLA
ARAAIILFHE IQRDARAELM TGTPVALFEY SLNWLRQEGW VIVSVDECIE RLARNDRSER
YAVLTFDDGY RDNASVGLPI LERHNAPFMM YVPTGAPTRS MQSWWLGLRR VFLSRDRVSI
DALGRQFQCS DLRSKTSALA EVTRWVHQDY RRGAMLSSVF EESGISLAEL NDEYFLDERE
LCTLARHPLA SIGGHSTSHQ ALSTLDSDSA RAELADNRSY LENMLQLPVR HVAYPYGVCG
PREEDLARQA GFQTATTTRQ GRLYDDKLNR FALPRIGISS PSGLRARMSG IIEGMQAFAK
RRVVAELRDH Q
//
