ID A0A3M0G742_9ACTN Unreviewed; 441 AA.
AC A0A3M0G742;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Dihydroorotase {ECO:0000256|HAMAP-Rule:MF_00220};
DE Short=DHOase {ECO:0000256|HAMAP-Rule:MF_00220};
DE EC=3.5.2.3 {ECO:0000256|HAMAP-Rule:MF_00220};
GN Name=pyrC {ECO:0000256|HAMAP-Rule:MF_00220};
GN ORFNames=EAX62_15830 {ECO:0000313|EMBL:RMB57503.1};
OS Tessaracoccus antarcticus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=2479848 {ECO:0000313|EMBL:RMB57503.1, ECO:0000313|Proteomes:UP000275256};
RN [1] {ECO:0000313|EMBL:RMB57503.1, ECO:0000313|Proteomes:UP000275256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JDX10 {ECO:0000313|EMBL:RMB57503.1,
RC ECO:0000313|Proteomes:UP000275256};
RA Zhou L.Y., Du Z.J.;
RT "Tessaracoccus antarcticuss sp. nov., isolated from sediment.";
RL Submitted (OCT-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_00220}.
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_00220};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00220};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00220};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000256|HAMAP-
CC Rule:MF_00220}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC DHOase family. Class I DHOase subfamily.
CC {ECO:0000256|ARBA:ARBA00010286, ECO:0000256|HAMAP-Rule:MF_00220}.
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:RMB57503.1}.
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DR EMBL; REFW01000006; RMB57503.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M0G742; -.
DR OrthoDB; 9803027at2; -.
DR UniPathway; UPA00070; UER00117.
DR Proteomes; UP000275256; 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 CDD; cd01317; DHOase_IIa; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR HAMAP; MF_00220_B; PyrC_classI_B; 1.
DR InterPro; IPR004722; DHOase.
DR InterPro; IPR024403; DHOase-like_bac.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR00857; pyrC_multi; 1.
DR PANTHER; PTHR43668; ALLANTOINASE; 1.
DR PANTHER; PTHR43668:SF2; ALLANTOINASE; 1.
DR Pfam; PF12890; DHOase; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00220};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00220}; Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00220};
KW Reference proteome {ECO:0000313|Proteomes:UP000275256};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_00220}.
FT ACT_SITE 320
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 74..76
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 338..339
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
SQ SEQUENCE 441 AA; 46648 MW; 94218E62FDB7562A CRC64;
MTSPRFLSSP ATKEPGVSTD TSAFVITGAQ LPDGTRTDLF ISDGVLVGER PDNAEAIDAD
GLIALPGLVD LHTHLREPGR EDAETVASGS LAAARGGFTC IHAMANTTPV TDTAENAEHI
ADLGREAGHA QVVPIGAITK GLGGKELAEL GLMHQSRAGV RVFSDDGNCV MDPGLMRRAF
EWVRPFDGVL AQHAQDSGLA GPGACCHEGE LSGRLGLAGW PPVAESVIIA RDVQLAEATG
SRLHVCHVTS AEGVDVIRWA KARGINVTAE ATPHHLYLTT AEVVGYDTLY KVNPPLRTDE
HVEAIRAALA DGTIDIVGTD HAPHAPQDKD HAFADARPGM LGLEQALAVV METMVHTGRL
DWAGVVDRMS AAPARIGRVA EQGRPLAVGE PATLVLVDPA RRATVDRDDS ASLSRNNPYH
GRDLPDPVEL TMWAGRITHR R
//
