ID A0A1C3CX47_9GAMM Unreviewed; 344 AA.
AC A0A1C3CX47;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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 ORFNames=BBP83_07770 {ECO:0000313|EMBL:ODA13324.1};
OS Acinetobacter celticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1891224 {ECO:0000313|EMBL:ODA13324.1, ECO:0000313|Proteomes:UP000186553};
RN [1] {ECO:0000313|EMBL:ODA13324.1, ECO:0000313|Proteomes:UP000186553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 4603 {ECO:0000313|EMBL:ODA13324.1,
RC ECO:0000313|Proteomes:UP000186553};
RA Radolfova-Krizova L., Nemec A.;
RT "Acinetobacter sp. ANC 4603.";
RL Submitted (JUL-2016) 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}.
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:ODA13324.1}.
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DR EMBL; MBDL01000009; ODA13324.1; -; Genomic_DNA.
DR RefSeq; WP_068887572.1; NZ_MBDL01000009.1.
DR AlphaFoldDB; A0A1C3CX47; -.
DR STRING; 1891224.BBP83_07770; -.
DR OrthoDB; 9808095at2; -.
DR UniPathway; UPA00070; UER00117.
DR Proteomes; UP000186553; 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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00219}.
FT DOMAIN 11..309
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT ACT_SITE 247
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 15..17
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 41
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 344 AA; 38516 MW; C0B235A1D706249D CRC64;
MNTITLLQPD DWHAHLRDGP ALQRTVPDLA NQFARAICMP NLVPPVKTVE EANAYRERIL
AHVPEGVHFD PRMVLYLTNN TAPSEVLKIK QSDYVNAIKL YPAGATTNSD SGVSDISKVY
GVIEQLEEHQ VPLLLHGEVT HNHVDIFDRE KRFLDEVLSP LLRQFPKLKL VLEHITTSEA
AHFVLEHDRH VAATITPQHL LFNRNDMLVG GIKPHFYCLP ILKRQTHQQT LLEVATSGSP
KFFLGTDSAP HSKDAKENAC GCAGCYSAPT AIELYAQAFD QVGKIERLEG FASHFGADFY
GLPRNTNTIT LVKEDQVIPE SLDYLDGEKI IPLHAGKTIQ WRKV
//