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Database: UniProt
Entry: N9VZ30_9SPHN
LinkDB: N9VZ30_9SPHN
Original site: N9VZ30_9SPHN 
ID   N9VZ30_9SPHN            Unreviewed;       286 AA.
AC   N9VZ30;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE   AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN   ORFNames=EBMC1_14093 {ECO:0000313|EMBL:ENY80502.1};
OS   Sphingopyxis sp. MC1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1174684 {ECO:0000313|EMBL:ENY80502.1, ECO:0000313|Proteomes:UP000013072};
RN   [1] {ECO:0000313|EMBL:ENY80502.1, ECO:0000313|Proteomes:UP000013072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC1 {ECO:0000313|EMBL:ENY80502.1,
RC   ECO:0000313|Proteomes:UP000013072};
RA   Lolas I.B., Kjeldal H., Almeida B., Le-Quy V., Gough H.L., Nielsen J.L.;
RT   "Differential expression analysis of membrane associated proteins from
RT   triclosan-degrading sphingopyxis.";
RL   Submitted (FEB-2013) 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. {ECO:0000256|ARBA:ARBA00003236}.
CC   -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC       {ECO:0000256|ARBA:ARBA00010973}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ENY80502.1}.
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DR   EMBL; AOUN01000014; ENY80502.1; -; Genomic_DNA.
DR   RefSeq; WP_003049061.1; NZ_AOUN01000014.1.
DR   AlphaFoldDB; N9VZ30; -.
DR   PATRIC; fig|1174684.3.peg.2844; -.
DR   eggNOG; COG0726; Bacteria.
DR   Proteomes; UP000013072; Unassembled WGS sequence.
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; cd10941; CE4_PuuE_HpPgdA_like_2; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   InterPro; IPR045235; CE4_PuuE_HpPgdA-like_2.
DR   InterPro; IPR022560; DUF3473.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   InterPro; IPR014344; PEP-CTERM_polysacc_deacetyl.
DR   NCBIfam; TIGR03006; pepcterm_polyde; 1.
DR   PANTHER; PTHR47561; POLYSACCHARIDE DEACETYLASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G05030); 1.
DR   PANTHER; PTHR47561:SF1; POLYSACCHARIDE DEACETYLASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G05030); 1.
DR   Pfam; PF11959; DUF3473; 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:UP000013072}.
FT   DOMAIN          16..286
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   286 AA;  32045 MW;  8312063AB99F9A37 CRC64;
     MQNGLSVDVE DWFQVGAFER TIDRADWPAL ECRVEANCDA VLHLFAEAGV RGTFFTLGWV
     AERYPALIRR IVDAGHELAS HGYDHKRVFQ MTAGEFAADL EKTRAILENL GGQPVRGYRA
     PSFSVDMRTP WAHAVLAEQG YAYSSSVAPV VHDHYGWAQS PRHAWQPLPD SALIEWPVTT
     ARVAGRTLAA GGGGFMRLLP YRFTRWAIER MNAEGHPAIL YFHPWEIDPG QPRVADAPLR
     SKVRHYTGLS AMAGKLKKLL DDFEWTRADA LLAAQQERAR PWRAAA
//
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