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Entry: A1SH63_NOCSJ
LinkDB: A1SH63_NOCSJ
Original site: A1SH63_NOCSJ 
ID   A1SH63_NOCSJ            Unreviewed;       467 AA.
AC   A1SH63;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Dihydropyrimidinase {ECO:0000313|EMBL:ABL81148.1};
DE            EC=3.5.2.2 {ECO:0000313|EMBL:ABL81148.1};
GN   OrderedLocusNames=Noca_1635 {ECO:0000313|EMBL:ABL81148.1};
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL81148.1, ECO:0000313|Proteomes:UP000000640};
RN   [1] {ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABL81148.1, ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RX   PubMed=21551312; DOI=10.1128/JB.05109-11;
RA   Coleman N.V., Wilson N.L., Barry K., Brettin T.S., Bruce D.C., Copeland A.,
RA   Dalin E., Detter J.C., Del Rio T.G., Goodwin L.A., Hammon N.M., Han S.,
RA   Hauser L.J., Israni S., Kim E., Kyrpides N., Land M.L., Lapidus A.,
RA   Larimer F.W., Lucas S., Pitluck S., Richardson P., Schmutz J., Tapia R.,
RA   Thompson S., Tice H.N., Spain J.C., Gossett J.G., Mattes T.E.;
RT   "Genome Sequence of the ethene- and vinyl chloride-oxidizing actinomycete
RT   Nocardioides sp. strain JS614.";
RL   J. Bacteriol. 193:3399-3400(2011).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two divalent
CC       metal cations. {ECO:0000256|PIRSR:PIRSR611778-50}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Hydantoinase/dihydropyrimidinase family.
CC       {ECO:0000256|ARBA:ARBA00008829}.
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DR   EMBL; CP000509; ABL81148.1; -; Genomic_DNA.
DR   RefSeq; WP_011755095.1; NC_008699.1.
DR   AlphaFoldDB; A1SH63; -.
DR   STRING; 196162.Noca_1635; -.
DR   KEGG; nca:Noca_1635; -.
DR   eggNOG; COG0044; Bacteria.
DR   HOGENOM; CLU_015572_2_0_11; -.
DR   OrthoDB; 9775759at2; -.
DR   Proteomes; UP000000640; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004157; F:dihydropyrimidinase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR02033; D-hydantoinase; 1.
DR   PANTHER; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1.
DR   PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:ABL81148.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000640}.
FT   DOMAIN          54..443
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
FT   MOD_RES         156
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611778-50"
SQ   SEQUENCE   467 AA;  48561 MW;  4F36840BE78FE674 CRC64;
     MSNDLVVRGG TVVDGAGTRR ADVLVRAGRI VAVEPEIALD SAAAADIVDA GGAYVVPGGI
     DVHTHFALPV GAVTSADDFE SGTLAAACGG TTCVVDFAGA GREPWQEALA TWHDRARDRA
     VVDYGFHLTV AELPEDPEAA VARFGEFVEH GVTSVKLYLA YPDRLMVDDD TLARALAAGR
     RTGVRVCVHA EDGATVESLV VEALAAGRKG PDAIPAVRPD SVEAEAIRRA AVLAAAADTS
     LYVVHLSSAA GLEAVRAARA VGADVHAETC PHYLYLDQAH LEAGEPDFVC APPLRGAADR
     AALWGAIAAG EVEVVATDHC PFTRADRRRG TGGDGWADFR QLPGGLSGVE TRLALAYQGV
     VSGRLTLGRW VEVTSGAPAR LFGLAGVKGS VRPGLDADLV VFDPGATRVL DAATLHSRCD
     HSPYEGLVVT GWPALTLSRG EVVAAAGEPV EPRPGRGRFV RRSPIVH
//
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