ID A0A1C1CBF0_9EURO Unreviewed; 572 AA.
AC A0A1C1CBF0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=dihydropyrimidinase {ECO:0000256|ARBA:ARBA00039113};
DE EC=3.5.2.2 {ECO:0000256|ARBA:ARBA00039113};
GN Name=PYD2 {ECO:0000313|EMBL:OCT45798.1};
GN ORFNames=CLCR_01481 {ECO:0000313|EMBL:OCT45798.1};
OS Cladophialophora carrionii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT45798.1, ECO:0000313|Proteomes:UP000094526};
RN [1] {ECO:0000313|Proteomes:UP000094526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouracil + H2O = 3-(carbamoylamino)propanoate + H(+);
CC Xref=Rhea:RHEA:16121, ChEBI:CHEBI:11892, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15901; EC=3.5.2.2;
CC Evidence={ECO:0000256|ARBA:ARBA00036696};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Hydantoinase/dihydropyrimidinase family.
CC {ECO:0000256|ARBA:ARBA00008829}.
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:OCT45798.1}.
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DR EMBL; LGRB01000019; OCT45798.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C1CBF0; -.
DR STRING; 86049.A0A1C1CBF0; -.
DR VEuPathDB; FungiDB:CLCR_01481; -.
DR VEuPathDB; FungiDB:G647_03689; -.
DR eggNOG; KOG2584; Eukaryota.
DR Proteomes; UP000094526; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11647:SF1; COLLAPSIN RESPONSE MEDIATOR PROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000094526}.
FT DOMAIN 54..518
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT REGION 381..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 572 AA; 62250 MW; BB6669E2D9A68042 CRC64;
MDLDLIIKNA TIVTATEVLP PGLSIGIHGG KIVAIALSLP CTPSTRVIDA EGAYVTPGGV
DSHVHLHQDN APTGDKWLSG SRSALCGGNT TILAFATQKR TDESLFPVVR DYHTRAAGQS
FVDYGFHLIV SRPGPEILGG PAMTAKMGKE ADVNDRKDEN EGELKIMVEQ EGITSVKLYM
TYPAYRLGDR EMLDVMMRCR EVGMTVMVHA ENADMIDMIT TRLLSSSHTQ PKYHAVARPQ
IAETEATYRA ISLSTLTATP ILIVHMSSPA ALSHARKAQS KQMLPIHAET CPHYMFLKSE
RLGATSHPFE GEDHSHAHLD GKLGEEVDEW AGARHICAPP LRHDDKDLQS VWDAVTNGTI
TVISSDHAPS QYHNPLGKKK PVHEYESGKT TIPPSFANTP NGLPGIETRL PLLFSAATDA
SVTASAARTL TLPKFVALTS TNPARMYGLA GRKGSIAPGY DADLVVWYPH SPRADDASRD
KPTITITNDM LHHSIDYTPF EGFPVTNWPR YVLLRGQVKW DRDLELAEGP GKGILGRPGD
GLFLKRAKGE VLVGRTGGEP EGMRLGETKS WM
//