ID A0A164AU74_9BRAD Unreviewed; 294 AA.
AC A0A164AU74;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN ORFNames=A4A58_02350 {ECO:0000313|EMBL:KZD25310.1};
OS Tardiphaga robiniae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Tardiphaga.
OX NCBI_TaxID=943830 {ECO:0000313|EMBL:KZD25310.1, ECO:0000313|Proteomes:UP000076574};
RN [1] {ECO:0000313|EMBL:KZD25310.1, ECO:0000313|Proteomes:UP000076574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vaf07 {ECO:0000313|EMBL:KZD25310.1,
RC ECO:0000313|Proteomes:UP000076574};
RA Kopat V., Chirak E., Kimeklis A., Andronov E.;
RT "Microsymbionts genomes from the relict species Vavilovia formosa (Stev.)
RT Fed.";
RL Submitted (MAR-2016) 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}.
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:KZD25310.1}.
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DR EMBL; LVYV01000001; KZD25310.1; -; Genomic_DNA.
DR RefSeq; WP_068729442.1; NZ_LVYV01000001.1.
DR AlphaFoldDB; A0A164AU74; -.
DR STRING; 943830.A4A58_02350; -.
DR OrthoDB; 9787041at2; -.
DR Proteomes; UP000076574; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd10979; CE4_PuuE_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 PANTHER; PTHR43123:SF4; POLYSACCHARIDE DEACETYLASE; 1.
DR PANTHER; PTHR43123; POLYSACCHARIDE DEACETYLASE-RELATED; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE 3: Inferred from homology;
KW Nodulation {ECO:0000256|ARBA:ARBA00022458};
KW Reference proteome {ECO:0000313|Proteomes:UP000076574}.
FT DOMAIN 72..175
FT /note="NodB homology"
FT /evidence="ECO:0000259|Pfam:PF01522"
SQ SEQUENCE 294 AA; 33666 MW; ACC3B95ADE56518B CRC64;
MLPTERISYS PIDARPPLKL PNGKRMAVWI IVNVEEWDAK QPMPRTVLTP PAGGSPSPDV
PNWAWHEYGN RVGFWRMLKV FDDYKLPAAL AINGSAIAAY PPIVEAAKAR NWEFMGHGFT
QRNMQKVENE REDIRKTADV IEKATGKRPR GWLGPGLTET WETPDLLKQE GYDYVADWVL
DDQPVWLKTT TMPIVNVPYT QECNDVAMML IQHHKASEYC DRAVDQFEQI YEDSENSARV
MALVVHPYIM GAPHRLKHFR RIFETIQKKS DVAFMTGEQI LDWYLSVGPK APEA
//
