ID S9QDC8_9RHOB Unreviewed; 465 AA.
AC S9QDC8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN ORFNames=thalar_02261 {ECO:0000313|EMBL:EPX79436.1};
OS Litoreibacter arenae DSM 19593.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Litoreibacter.
OX NCBI_TaxID=1123360 {ECO:0000313|EMBL:EPX79436.1, ECO:0000313|Proteomes:UP000015351};
RN [1] {ECO:0000313|Proteomes:UP000015351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19593 {ECO:0000313|Proteomes:UP000015351};
RX PubMed=24501650; DOI=10.4056/sigs.4258318;
RA Riedel T., Fiebig A., Petersen J., Gronow S., Kyrpides N.C., Goker M.,
RA Klenk H.P.;
RT "Genome sequence of the Litoreibacter arenae type strain (DSM 19593(T)), a
RT member of the Roseobacter clade isolated from sea sand.";
RL Stand. Genomic Sci. 9:117-127(2013).
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:EPX79436.1}.
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DR EMBL; AONI01000010; EPX79436.1; -; Genomic_DNA.
DR RefSeq; WP_021100816.1; NZ_KE557306.1.
DR AlphaFoldDB; S9QDC8; -.
DR STRING; 1123360.thalar_02261; -.
DR PATRIC; fig|1123360.3.peg.2238; -.
DR eggNOG; COG0726; Bacteria.
DR eggNOG; COG3195; Bacteria.
DR HOGENOM; CLU_029940_2_0_5; -.
DR OrthoDB; 9787041at2; -.
DR UniPathway; UPA00394; UER00652.
DR Proteomes; UP000015351; 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:UP000015351}.
FT DOMAIN 68..284
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 465 AA; 52316 MW; 0CDD057936749B50 CRC64;
MKRYPRDMRG HGAKPPNANW PGGAKIAVQI VLNYEEGGEN CVLHGDTASE AFLSEITGAA
PWPGQRHWNM ESVYEYGARS GFWRLHRLLE NLPVTVFGVA TALARSPEQV AAMKDAGWEI
ASHGLKWIDY RDHDEEDERA DMVAAVKLHT EVVGEAPRGW YTGRCSANTV MLAAELGQFD
YIADSYADDL PYYMRHDGRD QLIVPYTLDC NDMRFATTQG FNSGDQFESY LRDSFDALYE
DGTAGRPKMM SIGLHCRLIG RPGRVQALKR FLSYVQSHDE VWFASRLQIA QRWLAEHPPT
PATRPTLMDK STFVSTYGDV FEQSPWVAER AWNLELGPAH DSAEGLWSAM SRVFRAASPT
QRLEVLDAHP DLASMLTGES QPTSEQSGQW LGGLTDDERQ TLSELNEDYI TKHGFPFIIA
LGDTDEEGVL SSLERRIRHD SAAEFDEACR QVERIAQLRL KKLLP
//
