ID B9NQ93_9RHOB Unreviewed; 476 AA.
AC B9NQ93;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN ORFNames=RKLH11_1042 {ECO:0000313|EMBL:EEE37206.1};
OS Rhodobacteraceae bacterium KLH11.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=467661 {ECO:0000313|EMBL:EEE37206.1, ECO:0000313|Proteomes:UP000005135};
RN [1] {ECO:0000313|Proteomes:UP000005135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLH11 {ECO:0000313|Proteomes:UP000005135};
RX PubMed=21742885; DOI=10.1128/jb.05556-11;
RA Zan J., Fricke W.F., Fuqua C., Ravel J., Hill R.T.;
RT "Genome Sequence of Ruegeria sp. Strain KLH11, an N-Acylhomoserine Lactone-
RT Producing Bacterium Isolated from the Marine Sponge Mycale laxissima.";
RL J. Bacteriol. 193:5011-5012(2011).
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; DS999531; EEE37206.1; -; Genomic_DNA.
DR AlphaFoldDB; B9NQ93; -.
DR STRING; 467661.RKLH11_1042; -.
DR eggNOG; COG0726; Bacteria.
DR eggNOG; COG3195; Bacteria.
DR HOGENOM; CLU_029940_2_0_5; -.
DR UniPathway; UPA00394; UER00652.
DR Proteomes; UP000005135; Unassembled WGS sequence.
DR GO; GO:0051997; F:2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0000255; P:allantoin metabolic process; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019628; P:urate catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd10977; CE4_PuuE_SpCDA1; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR Gene3D; 1.10.3330.10; Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR InterPro; IPR018020; OHCU_decarboxylase.
DR InterPro; IPR017580; OHCU_decarboxylase-1.
DR InterPro; IPR036778; OHCU_decarboxylase_sf.
DR InterPro; IPR017625; PuuE.
DR NCBIfam; TIGR03164; UHCUDC; 1.
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; PF09349; OHCU_decarbox; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF158694; UraD-Like; 1.
DR PROSITE; PS51677; NODB; 1.
PE 3: Inferred from homology;
KW Nodulation {ECO:0000256|ARBA:ARBA00022458};
KW Purine metabolism {ECO:0000256|ARBA:ARBA00022631};
KW Reference proteome {ECO:0000313|Proteomes:UP000005135}.
FT DOMAIN 74..290
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 476 AA; 53291 MW; 7684A298A3B87A57 CRC64;
MEDIMQPPRY PRDMIGYGAN PPDAAWPGGA KLAVQIVLNY EEGGENCVLH GDAASEAFLS
EIVGAAQWPG QRHWNMESIY EYGARAGFWR LHRLMQGLPI TVYGVATALA RSPDQVAAMK
SAGWEIASHG LKWVEHKDMP EEEERAQIAE AIRLHTEVVG DRPRGWYTGR CSDNTVRLVA
EEGGFAYVAD TYADDLPYWM QTGGRDQLIV PYTLDCNDMR FATPQGFNAG DQFYSYLKDS
FDALYEEGEA GAPKMLSIGL HCRLIGRPGR VMALKRFLDY ARGFSDVWFA TRLQIAEHWR
QNHPPAENPK PSQMAREEFI AAYGGIFEHS AWIAERAYDL ELGAAHDTAG GLHSALTRMF
RSASGAERLG VLTAHPDLAG KLAQAKRLTQ ESTSEQASAG LDALTDQEHA AFTDLNRRYT
EKFGFPFIIA VRDHDKASIL QAFQRRIEQD RDTEFAEACR QVERIAEFRL RDVLPA
//