ID E8TAC4_MESCW Unreviewed; 472 AA.
AC E8TAC4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN OrderedLocusNames=Mesci_0372 {ECO:0000313|EMBL:ADV09545.1};
OS Mesorhizobium ciceri biovar biserrulae (strain HAMBI 2942 / LMG 23838 /
OS WSM1271).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=765698 {ECO:0000313|EMBL:ADV09545.1, ECO:0000313|Proteomes:UP000007471};
RN [1] {ECO:0000313|Proteomes:UP000007471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAMBI 2942 / LMG 23838 / WSM1271
RC {ECO:0000313|Proteomes:UP000007471};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Nandasena K., Reeve W.G., Howieson J.G., O'Hara G.,
RA Tiwari R.P., Woyke T.;
RT "Complete sequence of chromosome of Mesorhizobium ciceri bv. biserrulae
RT WSM1271.";
RL Submitted (JAN-2011) 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000256|ARBA:ARBA00010973}.
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DR EMBL; CP002447; ADV09545.1; -; Genomic_DNA.
DR RefSeq; WP_013528243.1; NC_014923.1.
DR RefSeq; YP_004139595.1; NC_014923.1.
DR AlphaFoldDB; E8TAC4; -.
DR STRING; 765698.Mesci_0372; -.
DR KEGG; mci:Mesci_0372; -.
DR PATRIC; fig|765698.3.peg.790; -.
DR eggNOG; COG0726; Bacteria.
DR eggNOG; COG3195; Bacteria.
DR HOGENOM; CLU_029940_2_0_5; -.
DR OrthoDB; 9787041at2; -.
DR UniPathway; UPA00394; UER00652.
DR Proteomes; UP000007471; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 Hydrolase {ECO:0000313|EMBL:ADV09545.1};
KW Nodulation {ECO:0000256|ARBA:ARBA00022458};
KW Purine metabolism {ECO:0000256|ARBA:ARBA00022631}.
FT DOMAIN 67..285
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 472 AA; 53154 MW; F24616D2BB831741 CRC64;
MRYSRDMRGY GANPPDPKWP GGAHVAVQFV VNYEEGGENC VLHGDKASEA FLSEIVGAAP
WVGQRHWNME SIYEYGARAG FWRLLRLFTE SQVPITCYGV ATALARSPDQ VAAMQDAGWE
IASHGLRWID YRDHSAEDER RDLEAAIKLH YEVTGARPTG WYTGRTSINT VRIVAEEGGF
DYVSDTYDDE LPYWFEHEGG AQLIIPYTLD ANDMRFATPQ GFNSGDQFFA YLKDSFDTLY
AEGKAGRPRM MNIGLHCRLV GRPGRVAALK RFVDYVKSHD KVWLARRIDI AKHWQEVNPY
QPAALRPSKM EFETFVHTFG GVFEHSPWIA ERAYELELGP AHDTSGGLHN ALCRIFRSAS
ETERLSVLNA HPDLAGKLAK AKRLTAESTR EQASAGLDAL TDKERELFSK LNAAYVTTFG
FPFIIAVKGK TKQEILAEFE ARIGNSRGVE FETACKQVER IALLRLKDML PQ
//
