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Database: UniProt
Entry: A3K341_9RHOB
LinkDB: A3K341_9RHOB
Original site: A3K341_9RHOB 
ID   A3K341_9RHOB            Unreviewed;       300 AA.
AC   A3K341;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE   AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN   ORFNames=SSE37_17348 {ECO:0000313|EMBL:EBA08600.1};
OS   Sagittula stellata E-37.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sagittula.
OX   NCBI_TaxID=388399 {ECO:0000313|EMBL:EBA08600.1, ECO:0000313|Proteomes:UP000005713};
RN   [1] {ECO:0000313|EMBL:EBA08600.1, ECO:0000313|Proteomes:UP000005713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E-37 {ECO:0000313|EMBL:EBA08600.1,
RC   ECO:0000313|Proteomes:UP000005713};
RA   Moran M.A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2006) 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:EBA08600.1}.
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DR   EMBL; AAYA01000005; EBA08600.1; -; Genomic_DNA.
DR   RefSeq; WP_005858602.1; NZ_AAYA01000005.1.
DR   AlphaFoldDB; A3K341; -.
DR   eggNOG; COG0726; Bacteria.
DR   OrthoDB; 9784220at2; -.
DR   Proteomes; UP000005713; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
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; 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.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000313|EMBL:EBA08600.1};
KW   Glycosidase {ECO:0000313|EMBL:EBA08600.1};
KW   Hydrolase {ECO:0000313|EMBL:EBA08600.1};
KW   Nodulation {ECO:0000256|ARBA:ARBA00022458};
KW   Polysaccharide degradation {ECO:0000313|EMBL:EBA08600.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005713};
KW   Xylan degradation {ECO:0000313|EMBL:EBA08600.1}.
FT   DOMAIN          77..156
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|Pfam:PF01522"
SQ   SEQUENCE   300 AA;  34166 MW;  6EE4005B9AF873CD CRC64;
     MTPKDTTAPA PDAFQGLVDT ARFQRARRIP IPDFAYPEGV KLAVNFTLDF DAMLLRRLLN
     EPWGQKAKGE FGGRVGVWRI MEMFDAEDVK VTLFTPGRIC ELYPQVLHHV VAKGHELADH
     MWEHEVYADP QIEDAHLTRT LAALSQIAGK PITGTRSSHT PGLLRSKGVV YNSFTSADYL
     PFYELDAQGE NPILQLPFHY ALDDAMFFSF GWLDTPNQAQ RVMDVDEVFE IWWDAFLQQY
     KTGGYVNFLL HPFVSGHAMR VDMLQRLIQR MKTLPGVWFP TCDTLAQHIL TQHPYTPAAE
//
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