ID A9CFR8_AGRFC Unreviewed; 747 AA.
AC A9CFR8;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=Chitooligosaccharide deacetylase {ECO:0000256|ARBA:ARBA00020071};
DE AltName: Full=Nodulation protein B {ECO:0000256|ARBA:ARBA00032976};
GN OrderedLocusNames=Atu3860 {ECO:0000313|EMBL:AAK89558.1};
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299 {ECO:0000313|EMBL:AAK89558.1, ECO:0000313|Proteomes:UP000000813};
RN [1] {ECO:0000313|EMBL:AAK89558.1, ECO:0000313|Proteomes:UP000000813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813};
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F.Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D.Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.Y., Dolan M., Chumley F., Tingey S.V., Tomb J.F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2] {ECO:0000313|EMBL:AAK89558.1, ECO:0000313|Proteomes:UP000000813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813};
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
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; AE007870; AAK89558.1; -; Genomic_DNA.
DR PIR; AG3031; AG3031.
DR PIR; D98254; D98254.
DR RefSeq; NP_356773.1; NC_003063.2.
DR RefSeq; WP_010973382.1; NC_003063.2.
DR AlphaFoldDB; A9CFR8; -.
DR STRING; 176299.Atu3860; -.
DR DNASU; 1135734; -.
DR EnsemblBacteria; AAK89558; AAK89558; Atu3860.
DR GeneID; 66224119; -.
DR KEGG; atu:Atu3860; -.
DR PATRIC; fig|176299.10.peg.3683; -.
DR eggNOG; COG0726; Bacteria.
DR eggNOG; COG3919; Bacteria.
DR HOGENOM; CLU_372090_0_0_5; -.
DR OrthoDB; 9782872at2; -.
DR BioCyc; AGRO:ATU3860-MONOMER; -.
DR Proteomes; UP000000813; Chromosome linear.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd10968; CE4_Mlr8448_like_5s; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR011761; ATP-grasp.
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; PF15632; ATPgrasp_Ter; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS51677; NODB; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nodulation {ECO:0000256|ARBA:ARBA00022458};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000000813};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 119..311
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 499..747
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 747 AA; 81736 MW; 1A04199C13D9DD61 CRC64;
MTIPGVVIIG GAHGTLALAR SLGVLNVPVY YLTHDSPLPG WSRFVRETIR WAGPHDDGAM
AFLREMAEKP GLKGCLLVPS GDGEVQLVSQ HREELSALYK IILPEWTNLQ WLCEKPLLYK
RAAELGVSIP RTYALTSAAD IDGLDVMFPV ILKPHMGGGN TSIARAKVIR ADDREELKAA
FVDASGEIGP DNVVVQELIP GGGESQFSYA ALWLNGEPIA EFTARRARQY PVDFGYTSTR
VEVVDNRQAI EAARKILKSA GHSGLVEVEF KLDGRDGALK LLDVNPRPWS WFGLCSAAGI
NLGGLLWRVA NDMPTGQAVI ARQGTSWSYL VRDAVAAFTL ARRGEARLGD YLASLGRIRS
WAAFAPNDPL PGMIDLPLTA LRVLKKRILP GLASGQSARA MLPPVKRFVK YGAIRVGLEV
SSLPPVRSAF PSLAGRGVIF TLHHVRPGQA VSAFAPNVQL SVTPQFLEEA IKAALESGLV
PVHLHDLPAL LADTSEVRSF CAFTLDDGYR NNAEHAAPIF RKYAVPYTIF ITPGFVERSR
SVWWETAAAL TKKVTSFEFD FGAGPEQVEC ATPSQKVEAF ARLENFVQES PEDEAVERID
RVARQHGIDP IAIVDDLVMD AAELRTLSND PLVHFGAHTM THVNMRKIDA TRLVHEIEES
TRRVEAYVGQ RPQSFSYPYG WVRAVGEREA KAVSEAGFSV AVTTQAGVLG PHSLEKPAQL
PRVSLNGRFQ KKRFVKALIS GLPFRFI
//
