ID H5YRJ0_9BRAD Unreviewed; 352 AA.
AC H5YRJ0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN ORFNames=Bra471DRAFT_07207 {ECO:0000313|EMBL:EHR06353.1};
OS Bradyrhizobium sp. WSM471.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=319017 {ECO:0000313|EMBL:EHR06353.1};
RN [1] {ECO:0000313|EMBL:EHR06353.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM471 {ECO:0000313|EMBL:EHR06353.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA Howieson J., Reeve W., Woyke T.;
RT "The Noncontiguous Finished sequence of Bradyrhizobium sp. WSM471.";
RL Submitted (NOV-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; CM001442; EHR06353.1; -; Genomic_DNA.
DR RefSeq; WP_007615709.1; NZ_CM001442.1.
DR AlphaFoldDB; H5YRJ0; -.
DR HOGENOM; CLU_030024_1_2_5; -.
DR OrthoDB; 9782872at2; -.
DR Proteomes; UP000005774; Chromosome.
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:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd10968; CE4_Mlr8448_like_5s; 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; PTHR34216; -; 1.
DR PANTHER; PTHR34216:SF7; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE N-DEACETYLASE; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000313|EMBL:EHR06353.1};
KW Nodulation {ECO:0000256|ARBA:ARBA00022458};
KW Polysaccharide degradation {ECO:0000313|EMBL:EHR06353.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Xylan degradation {ECO:0000313|EMBL:EHR06353.1}.
FT DOMAIN 91..281
FT /note="NodB homology"
FT /evidence="ECO:0000259|Pfam:PF01522"
SQ SEQUENCE 352 AA; 39022 MW; 381A48990989D7EA CRC64;
MKQLRNNVIR AGLEALYFSG AHHLLRPLLS GVGAIFMLHH VRPARAAAFQ PNRHLEVTPE
FLRATLCHLR SREIDIVSMD ELHERLVRRR FDRRFAAFTL DDGYRDNLDF ALPVLHEFDA
PLAVYVASDF AEGTGRLWWE ALEAVIAKTE QIEVTIGNAA LRLDATTPAA KQAAFDRLHG
WLRALPGEHD LKREIEALCT KYGVDMAALC RSLCLSWDEV KTFAADPLVT IGAHSVSHCN
LAKQSEEIAT QEMAVSRARI EQALGRNVQH LAYPYGDREA AGEREFALAA SAGFKTAVTT
RPGMLFAENA GHMTALPRVS LNGNYQDTRI LPVLTSGAAT AMWNGFRRIA AA
//
