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Database: UniProt
Entry: A0A1H9SFK0_9PSEU
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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
//
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