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Database: UniProt
Entry: J0U394_9BURK
LinkDB: J0U394_9BURK
Original site: J0U394_9BURK 
ID   J0U394_9BURK            Unreviewed;       405 AA.
AC   J0U394;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:EJE50587.1};
GN   ORFNames=PMI14_04764 {ECO:0000313|EMBL:EJE50587.1};
OS   Acidovorax sp. CF316.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1144317 {ECO:0000313|EMBL:EJE50587.1, ECO:0000313|Proteomes:UP000004811};
RN   [1] {ECO:0000313|EMBL:EJE50587.1, ECO:0000313|Proteomes:UP000004811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF316 {ECO:0000313|EMBL:EJE50587.1,
RC   ECO:0000313|Proteomes:UP000004811};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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:EJE50587.1}.
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DR   EMBL; AKJX01000173; EJE50587.1; -; Genomic_DNA.
DR   RefSeq; WP_007857655.1; NZ_AKJX01000173.1.
DR   AlphaFoldDB; J0U394; -.
DR   PATRIC; fig|1144317.3.peg.4428; -.
DR   Proteomes; UP000004811; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd05666; M20_Acy1-like; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR   PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EJE50587.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004811}.
FT   DOMAIN          204..298
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   405 AA;  42633 MW;  7F36C29602E43A89 CRC64;
     MGAALPVESS QDVARVEEGI AAFIGEFKAL RQDLHRHPEL SFQEHRTAAI VAERLAAWGY
     EVTTGIAGTG VVGRLVRGSG RGNGSGNSLG IRADMDALPI TEATGLPYAS ENAGVMHACG
     HDGHTTVLLA TARFLAESGR FDGTLNLIFQ PAEENGGGAN RMIAEGLFER FPCDAVFGLH
     NWPCVGEGHF GCVTGPAMAS VDQITITVRG KGGHGAAPHE TVDPVVASAH IITALQTVVS
     RNVDPLDMGV VTVGSIHGGA APNVIPESVE LKLTARAFKP EVRAILKERI PAIARAQAES
     FGATAEVQYR PGYPAVLNHD AETALARSVA VDTFGAARVD AGFRPRTASE DFAFMLLKRP
     GSYVFVGNGD GASLHSPYYD FNDAILAPSA TYWVRLAERF LAPAA
//
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