ID W9H5X3_9PROT Unreviewed; 302 AA.
AC W9H5X3;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN ORFNames=N825_23975 {ECO:0000313|EMBL:EWY41610.1};
OS Skermanella stibiiresistens SB22.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Skermanella.
OX NCBI_TaxID=1385369 {ECO:0000313|EMBL:EWY41610.1, ECO:0000313|Proteomes:UP000019486};
RN [1] {ECO:0000313|EMBL:EWY41610.1, ECO:0000313|Proteomes:UP000019486}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB22 {ECO:0000313|EMBL:EWY41610.1,
RC ECO:0000313|Proteomes:UP000019486};
RA Zhu W., Wang G.;
RT "The genome sequence of Skermanella stibiiresistens.";
RL Submitted (AUG-2013) 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:EWY41610.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AVFL01000003; EWY41610.1; -; Genomic_DNA.
DR AlphaFoldDB; W9H5X3; -.
DR STRING; 1385369.N825_23975; -.
DR PATRIC; fig|1385369.3.peg.1126; -.
DR OrthoDB; 9784220at2; -.
DR Proteomes; UP000019486; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd10938; CE4_HpPgdA_like; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR InterPro; IPR037950; PgdA-like.
DR PANTHER; PTHR47561; POLYSACCHARIDE DEACETYLASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G05030); 1.
DR PANTHER; PTHR47561:SF1; POLYSACCHARIDE DEACETYLASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G05030); 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS51677; NODB; 1.
PE 3: Inferred from homology;
KW Nodulation {ECO:0000256|ARBA:ARBA00022458};
KW Reference proteome {ECO:0000313|Proteomes:UP000019486}.
FT DOMAIN 37..261
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 302 AA; 33975 MW; 46AF26D72822F2A6 CRC64;
MIQNPPPWPN GARCAVCFSF DMDVESLLHL NHREAAPSRL ATSSALRYGP FVAIPRIIDI
FRHYGLKQTV FVPGWCIEAY PRAVEALVEA GHEIGHHGWL HERPNTLSPG DEARVLDRAL
EAFDRIVGSR PTGYRAPAYA LSEHTPDLLV ERGFTYDASL VGDDVPYLLK SSKGTLVELP
SDFALDDWVQ YVNMKEFGYM MPIQAPERAM EVFRAEFDAA WTHGGMWVSV WHPFVSGRLA
RADAMARLIQ YMMDKGDVWF APMTEIAAHV QGLVDRGEWT PRTDEVPFWA APVDHLVTPS
RG
//