ID Q8P8R4_XANCP Unreviewed; 613 AA.
AC Q8P8R4;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN OrderedLocusNames=XCC2175 {ECO:0000313|EMBL:AAM41455.1};
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:AAM41455.1, ECO:0000313|Proteomes:UP000001010};
RN [1] {ECO:0000313|EMBL:AAM41455.1, 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; AAM41455.1; -; Genomic_DNA.
DR RefSeq; NP_637531.2; NC_003902.1.
DR AlphaFoldDB; Q8P8R4; -.
DR STRING; 190485.XCC2175; -.
DR EnsemblBacteria; AAM41455; AAM41455; XCC2175.
DR KEGG; xcc:XCC2175; -.
DR PATRIC; fig|190485.4.peg.2323; -.
DR eggNOG; COG1574; Bacteria.
DR HOGENOM; CLU_009942_4_3_6; -.
DR OrthoDB; 9031471at2; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01300; YtcJ_like; 1.
DR Gene3D; 3.10.310.70; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR013108; Amidohydro_3.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR033932; YtcJ-like.
DR PANTHER; PTHR22642:SF23; AMIDOHYDROLASE YTCJ-RELATED; 1.
DR PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 1.
DR Pfam; PF07969; Amidohydro_3; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001010}.
FT DOMAIN 48..532
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 613 AA; 67138 MW; 9B807A762545C7FD CRC64;
MVDLILRNAR ITTLDPRQPS ATTLAVADGR IVAVGDDAQI MAMAKQARVI DAQQRRVVPG
LNDSHTHLIR GGLNYNLELR WDGVRSLADA MALLKAQVDR TPAPQWVRVV GGFTAHQFIE
KRLPTLDEIN AIAPDTPVFL LHLYDRALLN RAALRACGYD KTTPDPPGGR IERDKLGNPT
GLLLAKPNAL ILYASLAKGP RLPIEYQANS TRHFMRELNR LGITSVIDAG GGFQNYPEDY
QVIEQLHAAG QLSVRIAYNL FTQNKGKEVA DFRGWTEVLP VRKGDDLLRH NGAGEMLVFS
AADFEQFSEP RPELAPEMEP ELEQVVRLLV EKRWPFRIHA TYDESISRIL DVYERVNADM
PFDGLHWFID HAETITPRNI DRIRALNGGI AVQHRMAYQG EAFVQRYGVQ AARHTPPVRR
MLAAGVPVGA GTDATRVASY NPWVALSWLV TGRTVGGLAL YGDENLLERE QALRLWTQGS
AWFSGDEDKK GTLAPGQLAD FIVLSDDYFR VDDAAIADIT SVLTVLGGTV VHGDGDFAAL
APSLPPAMPE WSPVNRFGGY HVGGAVSGLA SVAHAHGPGC RTHGTHGHAA HHAAPSDDLR
GFWGALGCAC FAF
//
