ID N1MIW2_9SPHN Unreviewed; 285 AA.
AC N1MIW2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN ORFNames=EBBID32_14940 {ECO:0000313|EMBL:CCW17155.1};
OS Sphingobium indicum BiD32.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1301087 {ECO:0000313|EMBL:CCW17155.1, ECO:0000313|Proteomes:UP000013201};
RN [1] {ECO:0000313|EMBL:CCW17155.1, ECO:0000313|Proteomes:UP000013201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BiD32 {ECO:0000313|EMBL:CCW17155.1,
RC ECO:0000313|Proteomes:UP000013201};
RA Le V.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCW17155.1, ECO:0000313|Proteomes:UP000013201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BiD32 {ECO:0000313|EMBL:CCW17155.1,
RC ECO:0000313|Proteomes:UP000013201};
RA Nielsen J.L., Zhou N.A., Kjeldal H.;
RT "Bisphenol A degrading Sphingobium sp. strain BiD32.";
RL Submitted (APR-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:CCW17155.1}.
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DR EMBL; CAVK010000068; CCW17155.1; -; Genomic_DNA.
DR AlphaFoldDB; N1MIW2; -.
DR Proteomes; UP000013201; 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:UP000013201}.
FT DOMAIN 20..285
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 285 AA; 32129 MW; CBFB2A14095AA694 CRC64;
MRNMIQNALS VDVEDWFQVG AFERTIRRAD WDGLAHRVEG NTDAVLDLFA QAGVTGTFFT
LGWVAERYPA LMRRIADAGH EIASHGYDHA RVFTFTPEQF RADLRKSRAI LEDASGQAVT
GYRAPSFSID PRTPWAHPIL AEEGYRYSSS VAPIRHDHYG WPDSPRFAWK PVPGSDLVEL
PVTTAKLGKR TLAAGGGGFF RLLPYQFSRW AIRQVNEQAG RPAIIYFHPW EIDPGQPRRT
DAPLRSRVRH YTNLSVMAAK LRRLTRDFAW TRVDALADAQ GALAP
//
