ID A0A0Q4Q1Z3_9SPHN Unreviewed; 300 AA.
AC A0A0Q4Q1Z3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN ORFNames=ASE90_17880 {ECO:0000313|EMBL:KQN89907.1};
OS Sphingomonas sp. Leaf67.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736230 {ECO:0000313|EMBL:KQN89907.1, ECO:0000313|Proteomes:UP000051342};
RN [1] {ECO:0000313|EMBL:KQN89907.1, ECO:0000313|Proteomes:UP000051342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf67 {ECO:0000313|EMBL:KQN89907.1,
RC ECO:0000313|Proteomes:UP000051342};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN89907.1, ECO:0000313|Proteomes:UP000051342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf67 {ECO:0000313|EMBL:KQN89907.1,
RC ECO:0000313|Proteomes:UP000051342};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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}.
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:KQN89907.1}.
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DR EMBL; LMLP01000004; KQN89907.1; -; Genomic_DNA.
DR RefSeq; WP_055998148.1; NZ_LMLP01000004.1.
DR AlphaFoldDB; A0A0Q4Q1Z3; -.
DR STRING; 1736230.ASE90_17880; -.
DR Proteomes; UP000051342; 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; cd10977; CE4_PuuE_SpCDA1; 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 InterPro; IPR017625; PuuE.
DR NCBIfam; TIGR03212; uraD_N-term-dom; 1.
DR PANTHER; PTHR43123; POLYSACCHARIDE DEACETYLASE-RELATED; 1.
DR PANTHER; PTHR43123:SF1; POLYSACCHARIDE DEACETYLASE-RELATED; 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}.
FT DOMAIN 66..285
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 300 AA; 32923 MW; A7B8D29BA9AD086A CRC64;
MIPERDLIGY GASPPDPRWP GRARVAVQFV VNVEEGAENS VLHGDAGSEA FLSEMVGAAS
HPARAMAMES LYEYGSRAGF WRLHRLFVER QVPVTAFAVA TAMAANPASV DAMLAAEWEI
ASHGLRWIDY QRVPPEVERA HIAEAIALHA RLTGARPLGW YQGRTSPATA ALVAAEGGFV
YDADSYADDL PYWDRRHAAA NGGRAQLIVP YTLDANDMKF VAYNGFADGE PFFRYLRDTF
EQLRSEGGRM MSVGLHGRIA GRPGRAAALA RFVDHVIASG DAWIARRIDI ARHWQQVHPA
//