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Database: UniProt
Entry: G8PW24_PSEUV
LinkDB: G8PW24_PSEUV
Original site: G8PW24_PSEUV 
ID   G8PW24_PSEUV            Unreviewed;       573 AA.
AC   G8PW24;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   08-MAY-2019, entry version 31.
DE   SubName: Full=Amidohydrolase 3 {ECO:0000313|EMBL:AEV39962.1};
GN   OrderedLocusNames=PSE_p0380 {ECO:0000313|EMBL:AEV39962.1};
OS   Pseudovibrio sp. (strain FO-BEG1).
OG   Plasmid FO-BEG1 {ECO:0000313|Proteomes:UP000005634}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Pseudovibrio.
OX   NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV39962.1, ECO:0000313|Proteomes:UP000005634};
RN   [1] {ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RC   PLASMID=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA   Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile and
RT   symbiotically interacting bacteria.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEV39962.1, ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV39962.1,
RC   ECO:0000313|Proteomes:UP000005634};
RC   PLASMID=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RX   PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA   Bondarev V., Richter M., Romano S., Piel J., Schwedt A.,
RA   Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile bacteria
RT   adapted for symbiosis.";
RL   Environ. Microbiol. 15:2095-2113(2013).
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DR   EMBL; CP003148; AEV39962.1; -; Genomic_DNA.
DR   RefSeq; WP_014290478.1; NC_016646.1.
DR   STRING; 911045.PSE_p0380; -.
DR   EnsemblBacteria; AEV39962; AEV39962; PSE_p0380.
DR   KEGG; psf:PSE_p0380; -.
DR   OMA; AVHECGG; -.
DR   BioCyc; PSP911045:GJTQ-5538-MONOMER; -.
DR   Proteomes; UP000005634; Plasmid FO-BEG1.
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; 2.30.40.10; -; 1.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR033932; YtcJ-like.
DR   Pfam; PF07969; Amidohydro_3; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005634};
KW   Hydrolase {ECO:0000313|EMBL:AEV39962.1};
KW   Plasmid {ECO:0000313|EMBL:AEV39962.1}.
FT   DOMAIN       80    542       Amidohydro_3. {ECO:0000259|Pfam:PF07969}.
SQ   SEQUENCE   573 AA;  63160 MW;  49C2766A61C9784C CRC64;
     MRWIAGLVIV IVGAAAGYYW YSLPPEYPTK YIITADRILT MDPERPQVQA ILVDGNEIMA
     LGDVRQLENQ DKAKLIRLKG TLIPGLIEPH THPIAAALLG AATDISAFKY DSRSQIMKAL
     EESADEYSLT PWVLAYGWDP IAIKDLSPPT LAELDAISPD KPMLVLTQMM HEAYANSAAL
     KEAGVDPSRG PMLRELEEIN RVVSAIPAPS DEAVELLVRK KYTDYAKAGY TSIGVTGAVG
     RHPNPVGLLQ RIGLEDNPPV RTYLYLTEDQ LPNWRFGGDD RFTILGAKFW LDGSPFTGAA
     ATYHPYETSE LVLERLGLSS GHHGELNMSD ADLVEKLREV HKKSGQVAMH VQGERAIDQA
     LMAIATIQAE DPRDDIQHRL EHNALITREQ IQWATDLGVS LGFFVDHITF YGDQLEDLFG
     NNRMNRYMPV RDAKDAGAVV TFHGDHPATP MNPMGTVETA MSRTSQSGNT VVGADHAVTL
     EEALQAMTVD AARQLGQEDT LGMIAVGMKA DFTLLNGNPQ VMRPEGLRLI RPTLTIRNGQ
     PVDTRFVSWF DPELAIKAVW KMLMGDETEP TST
//
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