ID A0A380N0Z8_9GAMM Unreviewed; 345 AA.
AC A0A380N0Z8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Dihydroorotase {ECO:0000256|ARBA:ARBA00012860, ECO:0000256|HAMAP-Rule:MF_00219};
DE Short=DHOase {ECO:0000256|HAMAP-Rule:MF_00219};
DE EC=3.5.2.3 {ECO:0000256|ARBA:ARBA00012860, ECO:0000256|HAMAP-Rule:MF_00219};
GN Name=pyrC {ECO:0000256|HAMAP-Rule:MF_00219,
GN ECO:0000313|EMBL:SUO98469.1};
GN ORFNames=NCTC10717_02221 {ECO:0000313|EMBL:SUO98469.1};
OS Suttonella indologenes.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC Cardiobacteriaceae; Suttonella.
OX NCBI_TaxID=13276 {ECO:0000313|EMBL:SUO98469.1, ECO:0000313|Proteomes:UP000254575};
RN [1] {ECO:0000313|EMBL:SUO98469.1, ECO:0000313|Proteomes:UP000254575}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10717 {ECO:0000313|EMBL:SUO98469.1,
RC ECO:0000313|Proteomes:UP000254575};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate
CC to dihydroorotate. {ECO:0000256|ARBA:ARBA00002368, ECO:0000256|HAMAP-
CC Rule:MF_00219}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate;
CC Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00219,
CC ECO:0000256|RuleBase:RU003440};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00219,
CC ECO:0000256|RuleBase:RU003440};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-Rule:MF_00219,
CC ECO:0000256|RuleBase:RU003440};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00004880, ECO:0000256|HAMAP-Rule:MF_00219,
CC ECO:0000256|RuleBase:RU003440}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00219}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC DHOase family. Class II DHOase subfamily.
CC {ECO:0000256|ARBA:ARBA00005631, ECO:0000256|HAMAP-Rule:MF_00219,
CC ECO:0000256|RuleBase:RU003440}.
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DR EMBL; UHIA01000004; SUO98469.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A380N0Z8; -.
DR OrthoDB; 9808095at2; -.
DR UniPathway; UPA00070; UER00117.
DR Proteomes; UP000254575; Unassembled WGS sequence.
DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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 NCBIfam; TIGR00856; pyrC_dimer; 1.
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, ECO:0000256|HAMAP-Rule:MF_00219};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00219};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW Rule:MF_00219}; Reference proteome {ECO:0000313|Proteomes:UP000254575};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00219}.
FT DOMAIN 8..315
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT ACT_SITE 247
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 16..18
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT MOD_RES 99
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
SQ SEQUENCE 345 AA; 38446 MW; CBF65F606DF4B81B CRC64;
MTTSITLPRF DDMHVHFRDG AALKRTVADT SRWCARALIM PNLVPAVDSI AAVQSYRERI
IAHIPPEHDF TPLMSLYLSE HLSPDTVRQA KAAGVVAIKW YSKGATTNST QGVANVDSLA
PVLEAMQKEG LLLLIHGEVT DADIDIFDRE SRFIERILMP LRRNFPALKI VMEHITTAQA
VQYIRSQSEH LAATITPQHL LFNRNRLLVG GVKPHYYCLP ILKTESDRLA LIDAATSGDP
RFFLGTDSAP HAKHTKENAC GCAGCYTAWH APALYAQVFD SVGKLDKLKD FACRFGADYY
GLPYNSGEIV LKKQAMRIPE HLPYLEDSTV VALEGGSEWQ WSMEI
//
