ID A0A1N7SAB0_9BURK Unreviewed; 353 AA.
AC A0A1N7SAB0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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:SIT44292.1};
GN ORFNames=BN2475_470093 {ECO:0000313|EMBL:SIT44292.1};
OS Paraburkholderia ribeironis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1247936 {ECO:0000313|EMBL:SIT44292.1, ECO:0000313|Proteomes:UP000187012};
RN [1] {ECO:0000313|EMBL:SIT44292.1, ECO:0000313|Proteomes:UP000187012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM7296 {ECO:0000313|EMBL:SIT44292.1,
RC ECO:0000313|Proteomes:UP000187012};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-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}.
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DR EMBL; CYGX02000047; SIT44292.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7SAB0; -.
DR STRING; 1247936.BN2475_470093; -.
DR OrthoDB; 9808095at2; -.
DR UniPathway; UPA00070; UER00117.
DR Proteomes; UP000187012; 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:UP000187012};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00219}.
FT DOMAIN 18..320
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT ACT_SITE 257
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 22..24
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 106
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 106
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 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
FT MOD_RES 106
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00219"
SQ SEQUENCE 353 AA; 38624 MW; 148B691D4D68EB91 CRC64;
MTASNVSLDS LTLTRPDDWH LHVRDGAMLA AVLPDTARQF GRAIIMPNLK PPVTTTAMAQ
AYRERIVAAI PAGAKFEPLM TLYLTDNTPP DEIRRARESG FVHGVKLYPA GATTNSDAGV
TDIMKCAKTL ETMQETGMPL LVHGEVTDSS IDLFDREKVF IDRVMTPLRR AFPALKVVFE
HITTKDAADY VREAGVAPEL LGATITAHHL LYNRNAIFQG GIRPHYYCLP VLKRETHRVA
LVEAATSGNP RFFLGTDSAP HPKGLKEHAC GCAGCYTALH ALELYTEAFD QAGALDKLEG
FASFFGADFY GLPRNVGKVT LRREEWTLPA ELPAGDTPVV PLRGGESIGW RLV
//