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Database: UniProt
Entry: A0A2P8FJG1_9RHOB
LinkDB: A0A2P8FJG1_9RHOB
Original site: A0A2P8FJG1_9RHOB 
ID   A0A2P8FJG1_9RHOB        Unreviewed;       471 AA.
AC   A0A2P8FJG1;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE   AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN   ORFNames=CLV88_101257 {ECO:0000313|EMBL:PSL21833.1};
OS   Shimia abyssi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae.
OX   NCBI_TaxID=1662395 {ECO:0000313|EMBL:PSL21833.1, ECO:0000313|Proteomes:UP000240418};
RN   [1] {ECO:0000313|EMBL:PSL21833.1, ECO:0000313|Proteomes:UP000240418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100673 {ECO:0000313|EMBL:PSL21833.1,
RC   ECO:0000313|Proteomes:UP000240418};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAR-2018) 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:PSL21833.1}.
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DR   EMBL; PYGJ01000001; PSL21833.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P8FJG1; -.
DR   OrthoDB; 9787041at2; -.
DR   UniPathway; UPA00394; UER00652.
DR   Proteomes; UP000240418; 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:UP000240418}.
FT   DOMAIN          68..286
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   471 AA;  52983 MW;  30BD968726915BE9 CRC64;
     MTRYPRDLRG YGPTPPNPQW PGDAKVAVQF VLNYEEGGEN CVLHGDAASE AFLSDIPGAA
     QWPDQRHWNM ESIYEYGARA GFWRLHRLFT TANIPITIYG VATALARSPE QVAAMKSANW
     EIASHGLKWV EHKDMPAEEE RAAIADAIRL HTEVVGEPPR GWYTGRCSEN TVRLVGETGA
     FDYISDTYDD DLPYWLEFGD RDQLIIPYTL EANDMRFATA PGYTTGEQFF QYLKDAFDVL
     YAEGDAGAPK MMSIGLHCRL IGRPGKIAGL KRFIDYIQSF DHVWTPRRLD IAQHWAATHP
     PKRFERPSRM NRDTFVATYG GIFEHSPWIA ERAFDLELGP AHDSATGVHN ALCRMFRSAS
     TNERMGVLTA HPDLAGKLAS AGRLTAESTS EQSGAGLDML TDEERDTFTR LNTAYVEKHG
     FPFIIAVRDH DKSSIMAAFH RRIDNASDVE FAEACKQVER IAEFRLMDLL P
//
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