ID A0A1H9SFK0_9PSEU Unreviewed; 431 AA.
AC A0A1H9SFK0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN05216188_11677 {ECO:0000313|EMBL:SER83806.1};
OS Lentzea xinjiangensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=402600 {ECO:0000313|EMBL:SER83806.1, ECO:0000313|Proteomes:UP000199352};
RN [1] {ECO:0000313|Proteomes:UP000199352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3525 {ECO:0000313|Proteomes:UP000199352};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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_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}.
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DR EMBL; FOFR01000016; SER83806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9SFK0; -.
DR STRING; 402600.SAMN05216188_11677; -.
DR OrthoDB; 9803027at2; -.
DR UniPathway; UPA00070; UER00117.
DR Proteomes; UP000199352; 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; IPR006680; Amidohydro-rel.
DR InterPro; IPR004722; DHOase.
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; PF01979; Amidohydro_1; 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 Zinc {ECO:0000256|HAMAP-Rule:MF_00220}.
FT DOMAIN 49..422
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT ACT_SITE 305
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 60..62
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 309
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
FT BINDING 323..324
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00220"
SQ SEQUENCE 431 AA; 45483 MW; 3890D49FEDC40C80 CRC64;
MKPLLLKGVR PYGEGEPIDL LIRDGVIAGQ SDPTQHGADV EVIEGNGAVL LPGFVDLHTH
LREPGREDTE TIETGSRAAA LGGYTAVFAM ANTDPVADNA VIVEHVARRG QEVGLVDVHP
VGAVTVGLKG EKLAELGTMA KSKANVRVFS DDGHCVHDPL IMRRALEYSK SLGAVIAQHA
EEPRLTVGAQ AHEGENASRL GLQGWPAAAE ESIVARDCIL AKQVDARLHV CHVSTTGTAD
VLKWAKARGT EVSAEVTPHH LILTDDRLAT YDPVNKVNPP LRTQADVDAL RQALADGTID
CVATDHAPHA VQDKDCEWSA ARPGMLGLQT ALGIVVETMV RTGLLDWRGV ARVMSEKPAE
IAGLTDQGRP IAPGEPANLV LVDPDASWTV NGAELASIAG NTPFEGMELP AAVTATILRG
RVTALAGRIA E
//