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Database: UniProt
Entry: A0A1G6W483_9PROT
LinkDB: A0A1G6W483_9PROT
Original site: A0A1G6W483_9PROT 
ID   A0A1G6W483_9PROT        Unreviewed;       307 AA.
AC   A0A1G6W483;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE   AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN   ORFNames=SAMN04488071_0943 {ECO:0000313|EMBL:SDD59835.1};
OS   Kordiimonas lacus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Kordiimonadales;
OC   Kordiimonadaceae; Kordiimonas.
OX   NCBI_TaxID=637679 {ECO:0000313|EMBL:SDD59835.1, ECO:0000313|Proteomes:UP000183685};
RN   [1] {ECO:0000313|EMBL:SDD59835.1, ECO:0000313|Proteomes:UP000183685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.9109 {ECO:0000313|EMBL:SDD59835.1,
RC   ECO:0000313|Proteomes:UP000183685};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNAK01000002; SDD59835.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6W483; -.
DR   STRING; 637679.GCA_001550055_02658; -.
DR   OrthoDB; 9784220at2; -.
DR   Proteomes; UP000183685; 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:UP000183685}.
FT   DOMAIN          38..307
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   307 AA;  34963 MW;  9E08EF1DA908B5FF CRC64;
     MTSRDASILT SIEPVATGTN FGDRSAFSVD VEEWFQVGAF ENTLHREDWP SLESRVERQT
     HKVLELLDRH RVKGTFFCLG WVVERHPLLI KAIHDAGHEV ACHGRDHKRL FTMTRGQFLQ
     DVAGAKAQLE DATGVAVKGY RAPSFSLRPD TWWAYECLEE LGFHYSSSIY PIQHDHYGMP
     EAPRRPFWPI GAGRILEVPM SVYRLGRAWP ASGGGYFRLL PYMLGKGLFS LSVRQSGLPG
     VFYMHPWEMD PGQPYVENAP WLSRFRHYTN QARMAKKVGR LCDSRKWARM DEIYGGMFAQ
     AGQAGNP
//
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