ID   Q0FDI7_9RHOB            Unreviewed;       469 AA.
AC   Q0FDI7;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE   AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN   ORFNames=OM2255_10136 {ECO:0000313|EMBL:EAU52507.1};
OS   Rhodobacterales bacterium HTCC2255.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales.
OX   NCBI_TaxID=367336 {ECO:0000313|EMBL:EAU52507.1, ECO:0000313|Proteomes:UP000009381};
RN   [1] {ECO:0000313|EMBL:EAU52507.1, ECO:0000313|Proteomes:UP000009381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2255 {ECO:0000313|EMBL:EAU52507.1,
RC   ECO:0000313|Proteomes:UP000009381};
RA   Giovannoni S., Cho J.-C., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA   Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (SEP-2006) 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:EAU52507.1}.
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DR   EMBL; AATR01000002; EAU52507.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0FDI7; -.
DR   eggNOG; COG0726; Bacteria.
DR   eggNOG; COG3195; Bacteria.
DR   HOGENOM; CLU_029940_2_0_5; -.
DR   OrthoDB; 9787041at2; -.
DR   BioCyc; RBAC367336:G1GNW-1468-MONOMER; -.
DR   UniPathway; UPA00394; UER00652.
DR   Proteomes; UP000009381; 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:UP000009381}.
FT   DOMAIN          68..284
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   469 AA;  53407 MW;  CEA0AC48916335D8 CRC64;
     MKRYPRDMYG YGKNTPKAQW PNNAKIALQI VINFEEGGEN NILHGDNASE AFLSEIVGAS
     AWPNQRHANM ESIYEYGSRV GFWRLYDIFK ELPVTVYGVA TALARSPNHV HAMKSANWEI
     ASHGLKWIDY KDFEEKDEKA DMNEAIRLHT EVTGSAPKGW YTGRSSENTI KLAASTGIFS
     YIADSYADDL PYWTEFSDND QLIVPYTLDA NDMRFATPQG FNSGTQFLEY LKDSFKTLYQ
     EGANGSPKMM SIGLHCRLVG RPGRFEAIKK FLEFVNEHDS VWMATREQIA DHWKKNHPHN
     RFERPSNMNR EKFINEYGGI FEHSSWVANN AYDLELSHSH DTAIGLHNAL CRAFRSAPKE
     QQLSVLKAHP DLAGKLAQAK RLTAESTSEQ ASAGMDSLTD HEREKFTQLN LAYVKKHGFP
     FIIAVRDHNK ASILNAFEER INNDGDTEFS EACKQVERIA EFRLMDLLP
//