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Database: UniProt
Entry: C5CW89_VARPS
LinkDB: C5CW89_VARPS
Original site: C5CW89_VARPS 
ID   C5CW89_VARPS            Unreviewed;       557 AA.
AC   C5CW89;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Amidohydrolase 3 {ECO:0000313|EMBL:ACS16787.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Vapar_0124 {ECO:0000313|EMBL:ACS16787.1};
OS   Variovorax paradoxus (strain S110).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=543728 {ECO:0000313|EMBL:ACS16787.1};
RN   [1] {ECO:0000313|EMBL:ACS16787.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S110 {ECO:0000313|EMBL:ACS16787.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Orwin P.,
RA   Leadbetter J.R., Spain J.C., Han J.I.;
RT   "Complete sequence of chromosome 1 of Variovorax paradoxus S110.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001635; ACS16787.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5CW89; -.
DR   STRING; 543728.Vapar_0124; -.
DR   KEGG; vap:Vapar_0124; -.
DR   eggNOG; COG1574; Bacteria.
DR   HOGENOM; CLU_009942_4_3_4; -.
DR   OrthoDB; 9031471at2; -.
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   Hydrolase {ECO:0000313|EMBL:ACS16787.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..557
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002949848"
FT   DOMAIN          72..541
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   557 AA;  59865 MW;  140D3009B477B21A CRC64;
     MRTLLMAAGA AALLLRPPAA QAQPADLIVT NAKIATLDAA ATTAQALAVR DGRIVAVGNA
     AQVRALSGPI TRTVDAGGRT VVPGLIDSHM HAVRAALSYS TEVNWIGAGS IGEAMERIRA
     AAARARPGGW LIVAGGWTEQ QFVERRRPTA AELQEAAPNH PVYVQLFYEA VVMTPKALEA
     LGVPAGTLPA GMKPAADGAP GWMTGDIVGI SALFDKLPKP TYDDNLAGTR AFFRELNRLG
     VTGLVDPGGF SIAPSQYAAL FELWREKALT LRVAYSVFAQ KPGAELQEFR ELTQMLPMGF
     GDDMLKFNGL GERVTLAMYN NNFPDAAAKE KFYELIKWAA MRRLAVTIHW QENGSVDHLL
     GLYEKLNAEV PIKELRWSIA HLDDASPETL ARMKALGIGW TMQDAMYFQG DRALATRGEA
     ARRMPPIGSA LRTGVNVGAG TDAHRVASYN PFVALQWMLD GRTVSGKAMR GADETPTREQ
     ALRLYTVGSA WFSFDEARRG TLEVGKLADF AILDQDFFSV PLERIGKTVS LMTVVGGRVV
     YAARPFDGAG TSVAAAP
//
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