ID A0A246K032_9SPHN Unreviewed; 286 AA.
AC A0A246K032;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN ORFNames=CDQ92_01215 {ECO:0000313|EMBL:OWQ98845.1};
OS Sphingopyxis bauzanensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=651663 {ECO:0000313|EMBL:OWQ98845.1, ECO:0000313|Proteomes:UP000197361};
RN [1] {ECO:0000313|EMBL:OWQ98845.1, ECO:0000313|Proteomes:UP000197361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22271 {ECO:0000313|EMBL:OWQ98845.1,
RC ECO:0000313|Proteomes:UP000197361};
RX PubMed=20023054; DOI=10.1099/ijs.0.018218-0;
RA Zhang D.C., Liu H.C., Xin Y.H., Zhou Y.G., Schinner F., Margesin R.;
RT "Sphingopyxis bauzanensis sp. nov., a psychrophilic bacterium isolated from
RT soil.";
RL Int. J. Syst. Evol. Microbiol. 60:2618-2622(2010).
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:OWQ98845.1}.
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DR EMBL; NISK01000001; OWQ98845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A246K032; -.
DR OrthoDB; 9784220at2; -.
DR Proteomes; UP000197361; 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; cd10941; CE4_PuuE_HpPgdA_like_2; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR045235; CE4_PuuE_HpPgdA-like_2.
DR InterPro; IPR022560; DUF3473.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR InterPro; IPR014344; PEP-CTERM_polysacc_deacetyl.
DR NCBIfam; TIGR03006; pepcterm_polyde; 1.
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; PF11959; DUF3473; 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:UP000197361}.
FT DOMAIN 16..286
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 286 AA; 32013 MW; 55B55E430CE697AF CRC64;
MQNGLSVDVE DWFQVGAFER TIHRADWPTL ECRVEANCDA VLQIFADAET KGTFFTLGWV
AERYPALIKR IVAAGHELAS HGYDHERVFN MTADEFAADL QKTQAILEDL GGVAVRGYRA
PSFSVDQRTP WAHQVLAEQG YAYSSSVAPV VHDHYGWPQS PRHAWRPLPD SELVEWPVTT
ARFAGRTLAA GGGGFMRMLP YGFTRWAIAR MNEEGHPAIL YFHPWEIDPG QPRVTDAPIK
SKIRHYSGLS AMAGKLKKLL ADFDWTRADA LLPAQQQRAA PWRAAA
//