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Information on EC 3.5.2.3 - dihydroorotase and Organism(s) Yersinia pestis and UniProt Accession Q8ZFU4

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.2 In cyclic amides
                3.5.2.3 dihydroorotase
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This record set is specific for:
Yersinia pestis
UNIPROT: Q8ZFU4 not found.
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The taxonomic range for the selected organisms is: Yersinia pestis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
dihydroorotase, dho, dhoase, dihydroorotase domain, hudhoase, type i dhoase, human dhoase domain, type ii dho, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
type II DHO
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carbamoylaspartic dehydrase
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-
-
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DHOase
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-
-
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dihydroorotate dehydrolase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of cyclic amides
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-
-
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formation of cyclic amides
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-
-
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PATHWAY SOURCE
PATHWAYS
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-, -, -
SYSTEMATIC NAME
IUBMB Comments
(S)-dihydroorotate amidohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9024-93-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-dihydroorotate + H2O
N-carbamoyl-L-aspartate
show the reaction diagram
-
-
-
r
N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O
show the reaction diagram
-
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(S)-dihydroorotate + H2O
N-carbamoyl-L-aspartate
show the reaction diagram
-
-
-
r
N-carbamoyl-L-aspartate
(S)-dihydroorotate + H2O
show the reaction diagram
-
-
-
r
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
the active site of YpDHO contains two zinc ions: Znalpha in trigonal bipyramidal coordination and Znbeta in tetrahedral coordination. Each zinc ion is coordinated by two histidine residues, His17 and His19 for Znalpha, and His140 and His178 for Znbeta in YpDHO, structure analysis, overview
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxo-1,2,3,6-tetrahydropyrimidine4,6-dicarboxylate
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L-6-thiodihydroorotate
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additional information
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the structure of YpDHO has essentially the same conformation as the structure of DHO from Escherichia coli (EcDHO), the most thoroughly studied bacterial type II DHO. The enzyme belongs to the amidohydrolase superfamily
metabolism
the de novo pyrimidine biosynthesis pathway is essential for the proliferation of many pathogens. One of the pathway enzymes, dihydroorotase (DHO), catalyzes the reversible interconversion of N-carbamoyl-L-aspartate to 4,5-dihydroorotate. De novo pyrimidine biosynthesis pathway, overview
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PYRC_YERPE
348
0
38542
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme, sitting drop vapor diffusion technique, mixing of 400 nl of 10 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 150 mM NaCl, 10% glycerol, 0.1% sodium azide, and 0.5 mM TCEP, with 400 nl of crystallization solution containing 0.15 M DL-malic acid, pH 7.0, and 20% w/v PEG 3350, equilibration against 0.034 ml of reservoir solution of 1.3 M NaCl, 4-7 days, 16°C, X-ray diffraction structure determination and analysis at 2.4 A resolution, molecular replacement, modelling
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, desalting gel filtration, and ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene pyrC, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the substantial difference between bacterial and mammalian DHOs makes the bacterial enzyme a promising drug target for disrupting bacterial growth and thus an important candidate to evaluate as a response to antimicrobial resistance on a molecular level
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lipowska, J.; Miks, C.D.; Kwon, K.; Shuvalova, L.; Zheng, H.; Lewinski, K.; Cooper, D.R.; Shabalin, I.G.; Minor, W.
Pyrimidine biosynthesis in pathogens - structures and analysis of dihydroorotases from Yersinia pestis and Vibrio cholerae
Int. J. Biol. Macromol.
136
1176-1187
2019
Yersinia pestis (Q8ZFU4), Yersinia pestis, Vibrio cholerae serotype O1 (Q9KL24), Vibrio cholerae serotype O1 El Tor Inaba N16961 (Q9KL24), Vibrio cholerae serotype O1 ATCC 39315 (Q9KL24)
Manually annotated by BRENDA team