ID V5EW27_KALBG Unreviewed; 390 AA.
AC V5EW27;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=dihydroorotase {ECO:0000256|ARBA:ARBA00012860};
DE EC=3.5.2.3 {ECO:0000256|ARBA:ARBA00012860};
GN ORFNames=PSEUBRA_SCAF2g02615 {ECO:0000313|EMBL:EST07503.1};
OS Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST07503.1, ECO:0000313|Proteomes:UP000019377};
RN [1] {ECO:0000313|Proteomes:UP000019377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA Goldman G.H.;
RT "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT high producer of endo-1,4-xylanase isolated from an insect pest of
RT sugarcane.";
RL Genome Announc. 1:E0092013-E0092013(2013).
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00004880}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC DHOase family. Class II DHOase subfamily.
CC {ECO:0000256|ARBA:ARBA00005631}.
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DR EMBL; KI545862; EST07503.1; -; Genomic_DNA.
DR RefSeq; XP_016292492.1; XM_016437012.1.
DR AlphaFoldDB; V5EW27; -.
DR STRING; 1365824.V5EW27; -.
DR GeneID; 27419684; -.
DR eggNOG; KOG2902; Eukaryota.
DR HOGENOM; CLU_041558_0_0_1; -.
DR OMA; TLHHISM; -.
DR OrthoDB; 275861at2759; -.
DR UniPathway; UPA00070; UER00117.
DR Proteomes; UP000019377; Unassembled WGS sequence.
DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR CDD; cd01294; DHOase; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR HAMAP; MF_00219; PyrC_classII; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR004721; DHOdimr.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43137; DIHYDROOROTASE; 1.
DR PANTHER; PTHR43137:SF1; DIHYDROOROTASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR PIRSF; PIRSF001237; DHOdimr; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000019377};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 8..263
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 390 AA; 42104 MW; 084B3D2F4E4A3299 CRC64;
MSAQEITVPA PADFHVHLRQ GPMSQLVTPH VAEGGISLAY VMPNLVPPIT SAQQAAGYLQ
SLRNLAPQTK FIGTLYLSSA LTPAEIAEAA KEGVRGVKSY PRGVTTNSDS GIEDYETYYP
IFEEMQKHDM VLNLHGEVPS NADAGICVLN AEEKFLTHLF KIHKRFPKLK IVLEHATTRK
AVEAVKECGE TVGCTITPHH LELIVDDWAG KPLNFCKPVA KYPDDRQALR DVIREGHPRF
FLGSDSAPHP LANKYPSAVT HGAPGTKASA SGGDDLEPTG VVSCGCAAGV YTSSILVPLC
ATLLEGFGAL DQLANYVSLN GRRFYGYDDE QELSQGSIKL RRAGGGSSAA TVPAVYVHPE
FRDVPDSDAS KVQVVPFWAG KRLGWEIVRS
//
