ID   H0A8J5_9PROT            Unreviewed;       307 AA.
AC   H0A8J5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE   AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN   ORFNames=HMPREF9946_05156 {ECO:0000313|EMBL:EHL95564.1};
OS   Acetobacteraceae bacterium AT-5844.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae.
OX   NCBI_TaxID=1054213 {ECO:0000313|EMBL:EHL95564.1, ECO:0000313|Proteomes:UP000003292};
RN   [1] {ECO:0000313|EMBL:EHL95564.1, ECO:0000313|Proteomes:UP000003292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AT-5844 {ECO:0000313|Proteomes:UP000003292};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-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   -!- 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:EHL95564.1}.
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DR   EMBL; AGEZ01000230; EHL95564.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0A8J5; -.
DR   STRING; 1054213.HMPREF9946_05156; -.
DR   PATRIC; fig|1054213.3.peg.4682; -.
DR   eggNOG; COG0726; Bacteria.
DR   HOGENOM; CLU_029940_0_0_5; -.
DR   OrthoDB; 9787041at2; -.
DR   BioCyc; ABAC1054213:G1H32-4754-MONOMER; -.
DR   Proteomes; UP000003292; 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; cd10977; CE4_PuuE_SpCDA1; 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; IPR017625; PuuE.
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; 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:UP000003292}.
FT   DOMAIN          74..291
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   307 AA;  34244 MW;  0C4400DC4D8747AC CRC64;
     MTILAPDSCY PRDFVGYGAN PPDPQWPGGA KLAVSFVLNY EEGGENTVLN GDAGSEIYLN
     ETPGGNPVLG MRDIGKESQF DYGARAGVWR VLRLFAERDF KLTVYGVGRA LELNPAIGRA
     FAEAGHEVAS HGWRWINYQN VDEATERQHI AQCVETITRT VGKPPVGWYT GRISEQTRRL
     VAEHGGFLYD SDAYDDDLPY YVTVAGKPLL IIPYTLDNND MKYAVPPGFS SNDGFEQHLR
     DAFDFLRAEG QTSPKMMSIG LHCRLVGRPA RAAALARFMD HVKSCPDVWV TTREQIALHW
     RKVHPPR
//