ID A0A0M4MVL2_9SPHN Unreviewed; 299 AA.
AC A0A0M4MVL2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN ORFNames=AMC99_01294 {ECO:0000313|EMBL:ALE16588.1};
OS Altererythrobacter epoxidivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Altererythrobacter.
OX NCBI_TaxID=361183 {ECO:0000313|EMBL:ALE16588.1, ECO:0000313|Proteomes:UP000057938};
RN [1] {ECO:0000313|EMBL:ALE16588.1, ECO:0000313|Proteomes:UP000057938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7731 {ECO:0000313|EMBL:ALE16588.1,
RC ECO:0000313|Proteomes:UP000057938};
RA Li Z., Cheng H., Huo Y., Xu X.;
RT "Complete genome sequence of a benzo[a]pyrene-degrading bacterium
RT Altererythrobacter epoxidivorans CGMCC 1.7731T.";
RL Submitted (SEP-2015) 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}.
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DR EMBL; CP012669; ALE16588.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M4MVL2; -.
DR STRING; 361183.AMC99_01294; -.
DR KEGG; aep:AMC99_01294; -.
DR PATRIC; fig|361183.4.peg.1265; -.
DR OrthoDB; 9784220at2; -.
DR Proteomes; UP000057938; 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; 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:UP000057938}.
FT DOMAIN 30..171
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 299 AA; 33301 MW; 729921644372EBD9 CRC64;
MSGHPAAPTA SDHRIVNGLS VDVEEWFQVG AFENVIDPAD WDSLESRVER NIALILDLFE
EAGAKATFFT LGWVAERHPA MIRRIVDAGH EIASHGYDHA RVFTFDRAQF ADDISKARKI
IEDASGQKVI GYRAPSFSID QRTPWAFEVL AEQGYAYSSS VAPVTHDHYG WPSAPRFAFR
PVAGADLVEI PVATAMMRGK RLAAGGGGFF RVLPYAFSRW AIEQLNDEAG RPAPFYFHPW
EVDPDQPRVA GAPLRSRVRH YTNLSRMAGK LRRLLQDFAW GRMDTLASLE AARATDFPG
//
