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Database: UniProt
Entry: A0A1C3CX47_9GAMM
LinkDB: A0A1C3CX47_9GAMM
Original site: A0A1C3CX47_9GAMM 
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
//
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