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Database: UniProt
Entry: A0A1X4NK33_9RHOB
LinkDB: A0A1X4NK33_9RHOB
Original site: A0A1X4NK33_9RHOB 
ID   A0A1X4NK33_9RHOB        Unreviewed;       470 AA.
AC   A0A1X4NK33;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, 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=MGEO_12215 {ECO:0000313|EMBL:OSQ50559.1};
OS   Marivita geojedonensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Marivita.
OX   NCBI_TaxID=1123756 {ECO:0000313|EMBL:OSQ50559.1, ECO:0000313|Proteomes:UP000193926};
RN   [1] {ECO:0000313|EMBL:OSQ50559.1, ECO:0000313|Proteomes:UP000193926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DPG-138 {ECO:0000313|EMBL:OSQ50559.1,
RC   ECO:0000313|Proteomes:UP000193926};
RA   Lai Q., Shao Z.;
RT   "The draft genome sequence of Marivita geojedonensis KCTC 23882.";
RL   Submitted (MAR-2014) 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:OSQ50559.1}.
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DR   EMBL; JFKC01000011; OSQ50559.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X4NK33; -.
DR   STRING; 1123756.MGEO_12215; -.
DR   UniPathway; UPA00394; UER00652.
DR   Proteomes; UP000193926; 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:UP000193926}.
FT   DOMAIN          68..284
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   470 AA;  52514 MW;  B020294D422F7013 CRC64;
     MQRYPRDMIG YGANPPKANW PKGAKIAVQI VLNYEEGGEN NILHGDKASE AFLSEITGAQ
     PWPGQRHWNM ESIYEYGSRA GFWRLHRMMK DIPITIYGVA TALARAPEQV AAMKDAGWEI
     ASHGLKWVEH KDMPEDEERA QILEAIRLHT EVVGEPPKGW YTGRCSNNTI RLVAEQGGFD
     YVADSYADDL PYWMRFGDID QLIMPYTMDC NDMRFGIQAG YTNGDQFESY LKDSFDYLYA
     EGIEGSPKML SIGLHCRIVG RPGRAAALKR ALDYMAGHDG VWFATRQQIA QHWAREHPAP
     TAQRPSEMSQ DDFVAAFGGI FEHSPWIAER ACAYESGPTH DTARGVHNLL CRAFRSASDE
     ERLGVLNAHP DLAGKLAAAG RLTAESTAEQ AGAGLDMLTD DERATFQKLN ADYVARHGFP
     FIIAVKDNTK ASILDAFHRR IGNDRATEFA EACRQVERIA ELRLLDKLGA
//
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