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Database: UniProt
Entry: F6IKM1_9SPHN
LinkDB: F6IKM1_9SPHN
Original site: F6IKM1_9SPHN 
ID   F6IKM1_9SPHN            Unreviewed;       305 AA.
AC   F6IKM1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE   AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN   ORFNames=PP1Y_AT10458 {ECO:0000313|EMBL:CCA91973.1};
OS   Novosphingobium sp. PP1Y.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=702113 {ECO:0000313|EMBL:CCA91973.1, ECO:0000313|Proteomes:UP000009242};
RN   [1] {ECO:0000313|EMBL:CCA91973.1, ECO:0000313|Proteomes:UP000009242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=sp. PP1Y {ECO:0000313|Proteomes:UP000009242};
RX   PubMed=21685292; DOI=10.1128/JB.05349-11;
RA   D'Argenio V., Petrillo M., Cantiello P., Naso B., Cozzuto L., Notomista E.,
RA   Paolella G., Di Donato A., Salvatore F.;
RT   "De novo sequencing and assembly of the whole genome of Novosphingobium sp.
RT   strain PP1Y.";
RL   J. Bacteriol. 193:4296-4296(2011).
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   -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC       {ECO:0000256|ARBA:ARBA00010973}.
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DR   EMBL; FR856862; CCA91973.1; -; Genomic_DNA.
DR   RefSeq; WP_013832373.1; NC_015580.1.
DR   AlphaFoldDB; F6IKM1; -.
DR   KEGG; npp:PP1Y_AT10458; -.
DR   eggNOG; COG0726; Bacteria.
DR   HOGENOM; CLU_029940_0_2_5; -.
DR   OrthoDB; 9787041at2; -.
DR   Proteomes; UP000009242; Chromosome.
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; cd10979; CE4_PuuE_like; 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; PTHR43123:SF4; POLYSACCHARIDE DEACETYLASE; 1.
DR   PANTHER; PTHR43123; POLYSACCHARIDE DEACETYLASE-RELATED; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Nodulation {ECO:0000256|ARBA:ARBA00022458};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009242}.
FT   DOMAIN          89..170
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|Pfam:PF01522"
SQ   SEQUENCE   305 AA;  33639 MW;  1AE5769102B0AD8A CRC64;
     MTLDPAYLEY PMRRRGMDHH LYAWSNMHER EPLRLPGGAK MAVAPLVSLE WFPIVPGKAP
     FAAPGHMQTA YPDYRHYTAR EYGTRVGFYR LLDAFAKVGV KATIAVNAAI AERYPSIIAD
     VVAAGHEIVA HATGMDATID STVPEADERA MIVKARDTLG GAIGEAPKGW LSIARQQSWN
     TPRLLVEEGF GYCLDWVNDD LPYLQTTEAG SLVSVPYNHE LSDRQIIVVQ QHSAESYVQQ
     MQDAFGWLAA ESGPRVLPLH LTPYVMGLPF RMGAFEGLLE WLAAQAETRF VTASELAASL
     PENAA
//
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