ID   C5CZ11_VARPS            Unreviewed;       531 AA.
AC   C5CZ11;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=N-acyl-D-amino-acid deacylase {ECO:0000313|EMBL:ACS20972.1};
DE            EC=3.5.1.81 {ECO:0000313|EMBL:ACS20972.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Vapar_4361 {ECO:0000313|EMBL:ACS20972.1};
OS   Variovorax paradoxus (strain S110).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=543728 {ECO:0000313|EMBL:ACS20972.1};
RN   [1] {ECO:0000313|EMBL:ACS20972.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S110 {ECO:0000313|EMBL:ACS20972.1};
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; ACS20972.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5CZ11; -.
DR   STRING; 543728.Vapar_4361; -.
DR   KEGG; vap:Vapar_4361; -.
DR   eggNOG; COG3653; Bacteria.
DR   HOGENOM; CLU_016107_2_1_4; -.
DR   OrthoDB; 9766983at2; -.
DR   GO; GO:0047420; F:N-acyl-D-amino-acid deacylase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
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   PANTHER; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1.
DR   PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 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:ACS20972.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..531
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002950112"
FT   DOMAIN          75..505
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   531 AA;  56579 MW;  5C80CFE4F17159F7 CRC64;
     MQKPVVVLAI SAALAGLSSA APATTDAPVE LDLLLRGGTV YTGDSDQPVV GDVGIVGDRI
     VFAGRKAPPQ FSARRTIDAA GLVVAPGFID AHTHADADLH STDPRKRLNI PFLTQGVTTA
     VIGNDGFGGF DIAAQTQRLR SAPVGTNVAM YVGFGPVRID QLGEANRTPT PEQLDAMRRH
     LSRAICDGAL GLSTGLFYPP QNFSKTEEVI ELAKVAAGHG GLYDSHIRDE SMYNIGLKGS
     IEEVIRIGRE ARLPVHVAHI KALGVDVQGQ SGDIIRRIEK ERAAGLDITA DHYPWTASST
     RFSAALVPLW AVDGGRAAML KRFDDPAVQE RLRTGMRENL RLRGGPETIL FSAGSTKYVG
     KTLADVAKAS GADPVDAAIA VLRDGDLMIA SFNQSDDDVR AFMKRPWVMT SSDSSLGHPR
     AYGTFARKYD QYVVKEHTIS LGQFIRSSSS LTADTLGLEQ RGHLRPGYYA DVVVFDPARY
     AAKATYTQPT LLSEGVVTVV VNGRLAVDAG KPTGVGAGQP LLRTPKTGSC T
//