ID Q8P413_XANCP Unreviewed; 243 AA.
AC Q8P413;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=Hydrolase {ECO:0000313|EMBL:AAM43125.1};
GN OrderedLocusNames=XCC3903 {ECO:0000313|EMBL:AAM43125.1};
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485 {ECO:0000313|EMBL:AAM43125.1, ECO:0000313|Proteomes:UP000001010};
RN [1] {ECO:0000313|EMBL:AAM43125.1, ECO:0000313|Proteomes:UP000001010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25
RC {ECO:0000313|Proteomes:UP000001010};
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F.Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P.Jr., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A.Jr., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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DR EMBL; AE008922; AAM43125.1; -; Genomic_DNA.
DR RefSeq; NP_639243.1; NC_003902.1.
DR RefSeq; WP_011038978.1; NC_003902.1.
DR AlphaFoldDB; Q8P413; -.
DR STRING; 190485.XCC3903; -.
DR EnsemblBacteria; AAM43125; AAM43125; XCC3903.
DR KEGG; xcc:XCC3903; -.
DR PATRIC; fig|190485.4.peg.4178; -.
DR eggNOG; COG1011; Bacteria.
DR HOGENOM; CLU_045011_8_2_6; -.
DR OrthoDB; 367448at2; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.1600; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR023214; HAD_sf.
DR NCBIfam; TIGR01549; HAD-SF-IA-v1; 1.
DR NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR PANTHER; PTHR43316:SF3; HALOACID DEHALOGENASE, TYPE II (AFU_ORTHOLOGUE AFUA_2G07750)-RELATED; 1.
DR PANTHER; PTHR43316; HYDROLASE, HALOACID DELAHOGENASE-RELATED; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:AAM43125.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001010}.
SQ SEQUENCE 243 AA; 26827 MW; 747C3B03645831E0 CRC64;
MSFQISAITI DLDDTLWPFA PIGARIDQVL YDWMREHSPV TAARFPVEAM RELRERSFAD
NPHLHHDLSA LRRLTLEMAL RDSGGDLALL EPAYEVFYAA RNQVECYPDA LDALARIAAH
VPVAALSNGN ADLERIGLMH HFAFQLGSRE HGSAKPDPSI FLAACARLQA PPAQVLHVGD
HVRMDVLGAL DAGLRACWIN REQAQWSHPT QQPDLEFDSL TGLADWLDVH HTPAAHAGVC
VPG
//