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Human Metabolome Database Version 2.5

 

Showing metabocard for L-Dihydroorotic acid (HMDB03349)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-08-12 20:12:38
Update Date 2009-10-22 15:39:34
Accession Number HMDB03349
Secondary Accession Numbers Not Available
Common Name L-Dihydroorotic acid
Description L-Dihydroorotic acid is an intermediate in the metabolism of Pyrimidine. It is a substrate for Dihydroorotate dehydrogenase (mitochondrial).
Synonyms
  1. (S)-4,5-Dihydroorotate
  2. Dihydro-L-orotate
  3. Dihydro-L-orotic acid
  4. L-Dihydroorotate
  5. L-Dihydroorotic acid
  6. (S)-Dihydroorotate
Chemical IUPAC Name (4S)-2,6-dioxo-1,3-diazinane-4-carboxylic acid
Chemical Formula C5H6N2O4
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • carboxylic acid
  • carboxylic acid imide, N-unsubstituted
  • urea
  • heterocyclic compound
Biofunction
  • Component of Pyrimidine metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 158.112
Monoisotopic Molecular Weight 158.032761
Isomeric SMILES OC(=O)[C@@H]1CC(=O)NC(=O)N1
Canonical SMILES OC(=O)C1CC(=O)NC(=O)N1
KEGG Compound ID C00337 Link Image
BioCyc ID DI-H-OROTATE Link Image
BiGG ID 34662 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB03349 Link Image
Metagene Link HMDB03349 Link Image
METLIN ID 6899 Link Image
PubChem Compound 439216 Link Image
PubChem Substance 8144637 Link Image
ChEBI ID 17025 Link Image
CAS Registry Number 5988-19-2
InChI Identifier InChI=1/C5H6N2O4/c8-3-1-2(4(9)10)6-5(11)7-3/h2H,1H2,(H,9,10)(H2,6,7,8,11)/t2-/m0/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 12.7 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.70 [Predicted by ALOGPS]; -3.8 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Pyrimidine Metabolism SMP00046 Link Image map00240 Link Image
General References Not Available
Metabolic Enzymes
  1. Dihydroorotate dehydrogenase, mitochondrial
  2. CAD protein
Enzyme 1 [top]
Enzyme 1 ID 5416
Enzyme 1 Name Dihydroorotate dehydrogenase, mitochondrial
Enzyme 1 Synonyms
  1. DHOdehase
  2. Dihydroorotate oxidase
Enzyme 1 Gene Name DHODH
Enzyme 1 Protein Sequence >Dihydroorotate dehydrogenase, mitochondrial 
MAWRHLKKRAQDAVIILGGGGLLFASYLMATGDERFYAEHLMPTLQGLLDPESAHRLAVR
FTSLGLLPRARFQDSDMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSV
TPKPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAKLTEDGLPLGVN
LGKNKTSVDAAEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLTKVLQER
DGLRRVHRPAVLVKIAPDLTSQDKEDIASVVKELGIDGLIVTNTTVSRPAGLQGALRSET
GGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDALEKIRAGASLVQLYTALTF
WGPPVVGKVKRELEALLKEQGFGGVTDAIGADHRR
Enzyme 1 Number of Residues 395
Enzyme 1 Molecular Weight 42866.9
Enzyme 1 Theoretical pI 10.23
Enzyme 1 GO Classification
Function
  • catalytic activity
  • dihydroorotate dehydrogenase activity
  • dihydroorotate oxidase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • oxidoreductase activity, acting on the CH-CH group of donors, quinone or related compound as acceptor
Process
  • 'de novo' pyrimidine base biosynthetic process
  • UMP biosynthetic process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • oxidation reduction
  • pyrimidine base biosynthetic process
  • pyrimidine base metabolic process
  • pyrimidine nucleoside monophosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
  • pyrimidine ribonucleoside monophosphate biosynthetic process
Component
  • cell part
  • membrane
Enzyme 1 General Function Involved in catalytic activity
Enzyme 1 Specific Function (S)-dihydroorotate + a quinone = orotate + a quinol
Enzyme 1 Pathways
Enzyme 1 Reactions
  • (S)-dihydroorotate + a quinone = orotate + a quinol [RN:R01868]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 12-32
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 158258018 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q02127 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PYRD_HUMAN Link Image
Enzyme 1 PDB ID 1D3H Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1188 bp 
ATGGCGTGGAGACACCTGCAAAAGCGGGCCCAGGATGCTGTGATCATCCTGGGGGGAGGA
GGACTTCTCTTCGCCTCCTACCTGATGGCCACGGGAGATGAGCGTTTCTATGCTGAACAC
CTGATGCCGACTCTGCAGGGGCTGCTGGACCCGGAGTCAGCCCACAGACTGGCTGTTCGC
TTCACCTCCCTGGGGCTCCTTCCACGGGCCAGATTTCAAGACTCTGACATGCTGGAAGTG
AGAGTTCTGGGCCATAAATTCCGAAATCCAGTAGGAATTGCTGCAGGATTTGACAAGCAT
GGGGAAGCCGTGGACGGACTTTATAAGATGGGCTTTGGTTTTGTTGAGATAGGAAGTGTG
ACTCCAAAACCTCAGGAAGGAAACCCTAGACCCAGAGTCTTCCGCCTCCCTGAGGACCAA
GCTGTCATTAACAGGTATGGATTTAACAGTCACGGGCTTTCAGTGGTGGAACACAGGTTA
CGGGCCAGACAGCAGAAGCAGGCCAAGCTCACAGAAGATGGACTGCCTCTGGGGGTCAAC
TTGGGGAAGAACAAGACCTCAGTGGACGCCGCGGAGGACTACGCAGAAGGGGTGCGCGTA
CTGGGCCCCCTGGCCGACTACCTGGTGGTGAATGTGTCCAGCCCCAACACTGCCGGGCTG
CGGAGCCTTCAGGGAAAGGCCGAGCTGCGCCGCCTGCTGACCAAGGTGCTGCAGGAGAGG
GATGGCTTGCGGAGAGTGCACAGGCCGGCAGTCCTGGTGAAGATCGCTCCTGACCTCACC
AGCCAGGATAAGGAGGACATTGCCAGTGTGGTCAAAGAGTTGGGCATCGATGGGCTGATT
GTTACGAACACCACCGTGAGTCGCCCTGCGGGCCTCCAGGGTGCCCTGCGCTCTGAAACA
GGAGGGCTGAGTGGGAAGCCCCTCCGGGATTTATCAACTCAAACCATTCGGGAGATGTAT
GCACTCACCCAAGGCCGAGTTCCCATAATTGGGGTTGGTGGTGTGAGCAGCGGGCAGGAC
GCGCTGGAGAAGATCCGGGCAGGGGCCTCCCTGGTGCAGCTGTACACGGCCCTCACCTTC
TGGGGGCCACCCGTTGTGGGCAAAGTCAAGCGGGAACTGGAGGCCCTTCTGAAAGAGCAG
GGCTTTGGCGGAGTCACAGATGCCATTGGAGCAGATCATCGGAGGTGA
Enzyme 1 GenBank Gene ID AK292293 Link Image
Enzyme 1 GeneCard ID DHODH Link Image
Enzyme 1 GenAtlas ID DHODH Link Image
Enzyme 1 HGNC ID HGNC:2867 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 16q22
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Minet M, Dufour ME, Lacroute F: Cloning and sequencing of a human cDNA coding for dihydroorotate dehydrogenase by complementation of the corresponding yeast mutant. Gene. 1992 Nov 16;121(2):393-6. [PubMed Link Image]
  2. Copeland RA, Davis JP, Dowling RL, Lombardo D, Murphy KB, Patterson TA: Recombinant human dihydroorotate dehydrogenase: expression, purification, and characterization of a catalytically functional truncated enzyme. Arch Biochem Biophys. 1995 Oct 20;323(1):79-86. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Knecht W, Bergjohann U, Gonski S, Kirschbaum B, Loffler M: Functional expression of a fragment of human dihydroorotate dehydrogenase by means of the baculovirus expression vector system, and kinetic investigation of the purified recombinant enzyme. Eur J Biochem. 1996 Aug 15;240(1):292-301. [PubMed Link Image]
  6. Liu S, Neidhardt EA, Grossman TH, Ocain T, Clardy J: Structures of human dihydroorotate dehydrogenase in complex with antiproliferative agents. Structure. 2000 Jan 15;8(1):25-33. [PubMed Link Image]
  7. Ng SB, Buckingham KJ, Lee C, Bigham AW, Tabor HK, Dent KM, Huff CD, Shannon PT, Jabs EW, Nickerson DA, Shendure J, Bamshad MJ: Exome sequencing identifies the cause of a mendelian disorder. Nat Genet. 2010 Jan;42(1):30-5. Epub 2009 Nov 13. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 8876
Enzyme 2 Name CAD protein
Enzyme 2 Synonyms
  1. Glutamine-dependent carbamoyl-phosphate synthase
  2. Aspartate carbamoyltransferase
  3. Dihydroorotase
Enzyme 2 Gene Name CAD
Enzyme 2 Protein Sequence >CAD protein 
MAALVLEDGSVLRGQPFGAAVSTAGEVVFQTGMVGYPEALTDPSYKAQILVLTYPLIGNY
GIPPDEMDEFGLCKWFESSGIHVAALVVGECCPTPSHWSATRTLHEWLQQHGIPGLQGVD
TRELTKKLREQGSLLGKLVQNGTEPSSLPFLDPNARPLVPEVSIKTPRVFNTGGAPRILA
LDCGLKYNQIRCLCQRGAEVTVVPWDHALDSQEYEGLFLSNGPGDPASYPSVVSTLSRVL
SEPNPRPVFGICLGHQLLALAIGAKTYKMRYGNRGHNQPCLLVGSGRCFLTSQNHGFAVE
TDSLPADWAPLFTNANDGSNEGIVHNSLPFFSVQFHPEHQAGPSDMELLFDIFLETVKEA
TAGNPGGQTVRERLTERLCPPGIPTPGSGLPPPRKVLILGSGGLSIGQAGEFDYSGSQAI
KALKEENIQTLLINPNIATVQTSQGLADKVYFLPITPHYVTQVIRNERPDGVLLTFGGQT
ALNCGVELTKAGVLARYGVRVLGTPVETIELTEDRRAFAARMAEIGEHVAPSEAANSLEQ
AQAAAERLGYPVLVRAAFALGGLGSGFASNREELSALVAPAFAHTSQVLVDKSLKGWKEI
EYEVVRDAYGNCVTVCNMENLDPLGIHTGESIVVAPSQTLNDREYQLLRQTAIKVTQHLG
IVGECNVQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLALGIPLPELRN
SVTGGTAAFEPSVDYCVVKIPRWDLSKFLRVSTKIGSCMKSVGEVMGIGRSFEEAFQKAL
RMVDENCVGFDHTVKPVSDMELETPTDKRIFVVAAALWAGYSVDRLYELTRIDRWFLHRM
KRIIAHAQLLEQHRGQPLPPDLLQQAKCLGFSDKQIALAVLSTELAVRKLRQELGICPAV
KQIDTVAAEWPAQTNYLYLTYWGTTHDLTFRTPHVLVLGSGVYRIGSSVEFDWCAVGCIQ
QLRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYELENPEGVILSMGGQLP
NNMAMALHRQQCRVLGTSPEAIDSAENRFKFSRLLDTIGISQPQWRELSDLESARQFCQT
VGYPCVVRPSYVLSGAAMNVAYTDGDLERFLSSAAAVSKEHPVVISKFIQEAKEIDVDAV
ASDGVVAAIAISEHVENAGVHSGDATLVTPPQDITAKTLERIKAIVHAVGQELQVTGPFN
LQLIAKDDQLKVIECNVRVSRSFPFVSKTLGVDLVALATRVIMGEEVEPVGLMTGSGVVG
VKVPQFSFSRLAGADVVLGVEMTSTGEVAGFGESRCEAYLKAMLSTGFKIPKKNILLTIG
SYKNKSELLPTVRLLESLGYSLYASLGTADFYTEHGVKVTAVDWHFEEAVDGECPPQRSI
LEQLAEKNFELVINLSMRGAGGRRLSSFVTKGYRTRRLAADFSVPLIIDIKCTKLFVEAL
GQIGPAPPLKVHVDCMTSQKLVRLPGLIDVHVHLREPGGTHKEDFASGTAAALAGGITMV
CAMPNTRPPIIDAPALALAQKLAEAGARCDFALFLGASSENAGTLGTVAGSAAGLKLYLN
ETFSELRLDSVVQWMEHFETWPSHLPIVAHAEQQTVAAVLMVAQLTQRSVHICHVARKEE
ILLIKAAKARGLPVTCEVAPHHLFLSHDDLERLGPGKGEVRPELGSRQDVEALWENMAVI
DCFASDHAPHTLEEKCGSRPPPGFPGLETMLPLLLTAVSEGRLSLDDLLQRLHHNPRRIF
HLPPQEDTYVEVDLEHEWTIPSHMPFSKAHWTPFEGQKVKGTVRRVVLRGEVAYIDGQVL
VPPGYGQDVRKWPQGAVPQLPPSAPATSEMTTTPERPRRGIPGLPDGRFHLPPRIHRASD
PGLPAEEPKEKSSRKVAEPELMGTPDGTCYPPPPVPRQASPQNLGTPGLLHPQTSPLLHS
LVGQHILSVQQFTKDQMSHLFNVAHTLRMMVQKERSLDILKGKVMASMFYEVSTRTSSSF
AAAMARLGGAVLSFSEATSSVQKGESLADSVQTMSCYADVVVLRHPQPGAVELAAKHCRR
PVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKHGRTVHSLACLLTQYRVS
LRYVAPPSLRMPPTVRAFVASRGTKQEEFESIEEALPDTDVLYMTRIQKERFGSTQEYEA
CFGQFILTPHIMTRAKKKMVVMHPMPRVNEISVEVDSDPRAAYFRQAENGMYIRMALLAT
VLGRF
Enzyme 2 Number of Residues 2225
Enzyme 2 Molecular Weight 242981.7
Enzyme 2 Theoretical pI 6.42
Enzyme 2 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • amino acid binding
  • aspartate carbamoyltransferase activity
  • binding
  • carbamoyl-phosphate synthase activity
  • carboxyl- or carbamoyltransferase activity
  • carboxylic acid binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleoside binding
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring one-carbon groups
Process
  • 'de novo' pyrimidine base biosynthetic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • glutamine family amino acid metabolic process
  • glutamine metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase metabolic process
  • pyrimidine base biosynthetic process
  • pyrimidine base metabolic process
Component
—
Enzyme 2 General Function Involved in hydrolase activity
Enzyme 2 Specific Function This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase)
Enzyme 2 Pathways
Enzyme 2 Reactions
  • (1) 2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate [RN:R00575]
  • (2) L-glutamine + H2O = L-glutamate + NH3 [RN:R00256]
  • (3) 2 ATP + HCO3- = 2 ADP + phosphate + carbamoyl phosphate [RN:R07641]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 1228049 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P27708 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PYR1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >6678 bp 
ATGGCGGCCCTAGTGTTGGAGGACGGGTCGGTCCTGCGGGGCCAGCCCTTTGGGGCCGCC
GTGTCGACTGCCGGGGAAGTGGTGTTTCAAACCGGCATGGTCGGCTACCCCGAGGCCCTC
ACTGATCCCTCCTACAAGGCACAGATCTTAGTGCTCACCTATCCTCTGATCGGCAACTAT
GGCATCCCCCCAGATGAAATGGATGAGTTCGGTCTCTGCAAGTGGTTTGAATCCTCGGGC
ATCCACGTAGCAGCACTGGTAGTGGGAGAGTGCTGTCCTACTCCCAGCCACTGGAGTGCC
ACCCGCACCCTGCATGAGTGGCTGCAGCAGCATGGCATCCCTGGCTTGCAAGGAGTAGAC
ACTCGGGAGCTGACCAAGAAGTTGCGGGAACAGGGGTCTCTGCTGGGGAAGCTGGTCCAG
AATGGAACAGAACCTTCATCCCTGCCATTCTTGGACCCCAATGCCCGCCCCCTGGTACCA
GAGGTCTCCATTAAGACTCCACGGGTATTCAATACAGGGGGTGCCCCTCGGATCCTTGCT
TTGGACTGTGGCCTCAAGTATAATCAGATCCGATGCCTCTGCCAGCGTGGGGCTGAGGTC
ACTGTGGTACCCTGGGACCATGCACTAGACAGCCAAGAGTATGAGGGTCTCTTCTTAAGT
AATGGGCCTGGTGACCCTGCCTCCTATCCCAGTGTCGTATCCACACTGAGCCGTGTTTTA
TCTGAGCCTAATCCCCGACCTGTCTTTGGGATCTGCCTGGGACACCAGCTATTGGCCTTA
GCCATTGGGGCCAAGACTTACAAGATGAGATATGGGAACCGAGGCCATAACCAGCCCTGC
TTGTTGGTGGGCTCTGGGCGCTGCTTTCTGACATCCCAGAACCATGGGTTTGCTGTGGAG
ACAGACTCACTGCCAGCAGACTGGGCTCCTCTCTTCACCAACGCCAATGATGGTTCCAAT
GAAGGCATTGTGCACAACAGCTTGCCTTTCTTCAGTGTCCAGTTTCACCCAGAGCACCAA
GCTGGCCCTTCAGATATGGAACTGCTTTTCGATATCTTTCTGGAAACTGTGAAAGAGGCC
ACAGCTGGGAACCCTGGGGGCCAGACAGTTAGAGAGCGGCTGACTGAGCGCCTCTGTCCC
CCTGGGATTCCCACTCCCGGCTCTGGACTTCCACCACCACGAAAGGTTCTGATCCTGGGC
TCAGGGGGCCTCTCCATTGGCCAAGCTGGAGAATTTGACTACTCGGGCTCTCAGGCAATT
AAGGCCCTGAAGGAGGAAAACATCCAGACGTTGCTGATCAACCCCAATATTGCCACAGTG
CAGACCTCCCAGGGGCTGGCCGACAAGGTCTATTTTCTTCCCATAACACCTCATTATGTA
ACCCAGGTGATACGTAATGAACGCCCCGATGGTGTGTTACTGACTTTTGGGGGCCAGACT
GCTCTGAACTGTGGTGTGGAGCTGACCAAGGCCGGGGTGCTGGCTCGGTATGGGGTCCGG
GTCCTGGGCACAACAGTGGAGACCATTGAGCTGACCGAGGATCGACGGGCCTTTGCTGCC
AGAATGGCAGAGATCGGAGAGCATGTGGCCCCGAGCGAGGCAGGAAATTCTCTTGAACAG
GCCCAGGCAGCCGCTGAACGGCTGGGGTACCCTGTGCTAGTGCGTGCAGCCTTTGCCGTG
GGTGGCCTGGGCTCTGGCTTTGCCTCTAACAGGGAGGAGCTCTCTGCTCTCGTGGCCCCA
GCTTTTGCCCATACCAGCCAAGTGCTAGTAGACAAGTCTCTGAAGGGATGGAAGGAGATT
GAGTACGAGGTGGTGAGAGACGCCTATGGCAACTGTGTCACGGTGTGTAACATGGAGAAC
TTGGACCCACTGGGCATCCACACTGGTGAGTCCATAGTGGTGGCCCCTAGCCAGACACTG
AATGACAGGGAGTATCAGCTCCTGAGGCAGACAGCTATCAAGGTGACCCAGCACCTGGGA
ATTGTTGGGGAGTGCAATGTGCAGTATGCCTTGAACCCTGAGTCTGAGCAGTATTACATC
ATTGAAGTGAATGCCAGGCTCTCTCGCAGCTCTGCCCTGGCCAGTAAGGCCACAGGTTAT
CCACTGGCTTATGTGGCAGCCAAGCTAGCATTGGGCATCCCTTTGCCTGAGCTCAGGAAC
TCTGTGACAGGGGGTACAGCAGCCTTTGAACCCAGCGTGGATTATTGTGTGGTGAAGATT
CCTCGATGGGACCTTAGCAAGTTCCTGCGAGTCAGCACAAAGATTGGGAGCTGCATGAAG
AGCGTTGGTGAAGTCATGGGCATTGGGCGTTCATTTGAGGAGGCCTTCCAGAAGGCCCTG
CGCATGGTGGATGAGAACTGTGTGGGCTTTGATCACACAGTGAAACCAGTCAGCGATATG
GAGTTGGAGACTCCAACAGATAAGCGGATTTTTGTGGTGGCAGCTGCTTTGTGGGCTGGT
TATTCAGTGGACCGCCTGTATGAGCTCACACGCATCGACCGCTGGTTCCTGCACCGAATG
AAGCGTATCATCGCACATGCCCAGCTGCTAGAACAACACCGTGGACAGCCTTTGCCGCCA
GACCTGCTGCAACAGGCCAAGTGTCTTGGCTTCTCAGACAAACAGATTGCCCTTGCAGTT
CTGAGCACAGAGCTGGCTGTTCGCAAGCTGCGTCAGGAACTGGGGATCTGTCCAGCAGTG
AAACAGATTGACACAGTTGCAGCTGAGTGGCCAGCCCAGACAAATTACCTATACCTAACG
TATTGGGGCACCACCCATGACCTCACCTTTCGAACACCTCATGTCCTAGTCCTTGGCTCT
GGCGTCTACCGTATTGGCTCCAGTGTTGAGTTTGACTGGTGTGCTGTAGGCTGCATCCAG
CAGCTCCGAAAGATGGGATATAAGACCATCATGGTGAACTATAACCCAGAGACAGTCAGC
ACCGACTATGACATGTGTGATCGACTCTACTTTGATGAGATCTCTTTTGAGGTGGTGATG
GACATCTATGAGCTCGAGAACCCTGAAGGTGTGATCCTATCCATGGGTGGACAGCTGCCC
AACAACATGGCCATGGCGTTGCATCGGCAGCAGTGCCGGGTGCTGGGCACCTCCCCTGAA
GCCATTGACTCGGCTGAGAACCGTTTCAAGTTTTCCCGGCTCCTTGACACCATTGGTATC
AGCCAGCCTCAGTGGAGGGAGCTCAGTGACCTCGAGTCTGCTCGCCAATTCTGCCAGACC
GTGGGGTACCCCTGTGTGGTGCGCCCCTCCTATGTGCTGAGCGGTGCTGCTATGAATGTG
GCCTACGCGGATGGAGACCTGGAGCGCTTCCTGAGCAGCGCAGCAGCCGTCTCCAAAGAG
CATCCCGTGGTCATCTCCAAGTTCATCCAGGAGGCTAAGGAGATTGACGTGGATGCCGTG
GCCTCTGATGGTGTGGTGGCAGCCATCGCCATCTCTGAGCATGTGGAGAATGCAGGTGTG
CATTCAGGTGATGCGACGCTGGTGACCCCCCCACAAGATATCACTGCCAAAACCCTGGAG
CGGATCAAAGCCATTGTGCATGCTGTGGGCCAGGAGCTACAGGTCACAGGACCCTTCAAT
CTGCAGCTCATTGCCAAGGATGACCAGCTGAAAGTTATTGAATGCAACGTACGTGTCTCT
CGCTCCTTCCCCTTCGTTTCCAAGACACTGGGTGTGGACCTAGTAGCCTTGGCCACGCGG
GTCATCATGGGGGAAGAAGTGGAACCTGTGGGGCTAATGACTGGTTCTGGAGTCGTGGGA
GTAAAGGTGCCTCAGTTCTCCTTCTCCCGCTTGGCGGGTGCTGACGTGGTGTTGGGTGTG
GAAATGACCAGTACTGGGGAGGTGGCCGGCTTTGGGGAGAGCCGCTGTGAGGCATACCTC
AAGGCCATGCTAAGCACTGGCTTTAAGATCCCCAAGAAGAATATCCTGCTGACCATTGGC
AGCTATAAGAACAAAAGCGAGCTGCTCCCAACTGTGCGGCTACTGGAGAGCCTGGGCTAC
AGCCTCTATGCCAGTCTCGGCACAGCTGACTTCTACACTGAGCATGGCGTCAAGGTAACA
GCTGTGGACTGGCACTTTGAGGAGGCTGTGGATGGTGAGTGCCCACCACAGCGGAGCATC
CTGGAGCAGCTAGCTGAGAAAAACTTTGAGCTGGTGATTAACCTGTCAATGCGTGGAGCT
GGGGGCCGGCGTCTCTCCTCCTTTGTCACCAAGGGCTACCGCACCCGACGCTTGGCCGCT
GACTTCTCCGTGCCCCTAATCATCGATATCAAGTGCACCAAACTCTTTGTGGAGGCCCTA
GGCCAGATCGGGCCAGCCCCTCCTTTGAAGGTGCATGTTGACTGTATGACCTCCCAAAAG
CTTGTGCGACTGCCGGGATTGATTGATGTCCATGTGCACCTGCGGGAACCAGGTGGGACA
CATAAGGAGGACTTTGCTTCAGGCACAGCCGCTGCCCTGGCTGGGGGTATCACCATGGTG
TGTGCCATGCCTAATACCCGGCCCCCCATCATTGACGGCCCTGCTCTGGCCCTGGCCCAG
AAGCTGGCAGAGGCTGGCGCCCGGTGCGACTTTGCGCTATTCCTTGGGGCCTCGTCTGAA
AATGCAGGAACCTTGGGCACCGTGGCCGGGTCTGCAGCCGGGCTGAAGCTTTACCTCAAT
GAGACCTTCTCTGAGCTGCGGCTGGACAGCGTGGTCCAGTGGATGGAGCATTTCGAGACA
TGGCCCTCCCACCTCCCCATTGTGGCTCACGCAGAGCAGCAAACCGTGGCTGCTGTCCTC
ATGGTGGCTCAGCTCACTCAGCGCTCAGTGCACATATGTCACGTGGCACGGAAGGAGGAG
ATCCTGCTAATTAAAGCTGCAAAGGCACGGGGCTTGCCAGTGACCTGCGAGGTGGCTCCC
CACCACCTGTTCCTAAGCCATGATGACCTGGAGCGCCTGGGGCCTGGGAAGGGGGAGGTC
CGGCCTGAGCTTGGCTCCCGCCAGGATGTGGAAGCCCTGTGGGAGGACATGGCTGTCATC
GACTGCTTTGCCTCAGACCATGCTCCCCATACCTTGGAGGAGAAGTGTGGGTCCAGGCCC
CCACCTGGGTTCCCAGGGTTAGAGACCATGCTGCCACTACTCCTGACGGCTGTAAGCGAG
GGCCGGCTCAGCCTGGACGACCTGCTGCAGCGATTGCACCACAATCCTCGGCGCATCTTT
CACCTGCCCCCGCAGGAGGACACCTATGTGGAGGTGGATCTGGAGCATGAGTGGACAATT
CCCAGCCACATGCCCTTCTCCAAGGCCCACTGGACACCTTTTGAAGGGCAGAAAGTGAAG
GGCACCGTCCGCCGTGTGGTCCTGCGAGGGGAGGTTGCCTATATCGATGGGCAGGTTCTG
GTACCCCCGGGCTATGGACAGGATGTACGGAAGTGGCCACAGGGGGCTGTTCCTCAGCTC
CCACCCTCAGCCCCTGCCACTAGTGAGATGACCACGACACCTGAAAGACCCCGCCGTGGC
ATCCCAGGGCTTCCTGATGGCCGCTTCCATCTGCCGCCCCGAATCCATCGAGCCTCCGAC
CCAGGTTTGCCAGCTGAGGAGCCAAAGGAGAAGTCCTCTCGGAAGGTAGCCGAGCCAGAG
CTGATGGGAACCCCTGATGGCACCTGCTACCCTCCACCACCAGTACCGAGACAGGCATCT
CCCCAGAACCTGGGGACCCCTGGCTTGCTGCACCCCCAGACCTCACCCCTGCTGCACTCA
TTAGTGGGCCAACATATCCTGTCCGTCCAGCAGTTCACCAAGGATCAGATGTCTCACCTG
TTCAATGTGGCACACACACTGCGTATGATGGTGCAGAAGGAGCGGAGCCTCGACATCCTG
AAGGGGAAGGTCATGGCCTCCATGTTCTATGAAGTGAGCACACGGACCAGCAGCTCCTTT
GCAGCAGCCATGGCCCGGCTGGGAGGTGCTGTGCTCAGCTTCTCGGAAGCCACATCGTCC
GTCCAGAAGGGCGAATCCCTGGCTGACTCCGTGCAGACCATGAGCTGCTATGCCGACGTC
GTCGTGCTCCGGCACCCCCAGCCTGGAGCAGTGGAGCTGGCCGCCAAGCACTGCCGGAGG
CCAGTGATCAATGCTGGGGATGGGGTCGGAGAGCACCCCACCCAGGCCCTGCTGGACATC
TTCACCATCCGTGAGGAGCTGGGAACTGTCAATGGCATGACGATCACGATGGTGGGTGAC
CTGAAGCACGGACGCACAGTACATTCCCTGGCCTGCCTGCTCACCCAGTATCGTGTCAGC
CTGCGCTACGTGGCACCTCCCAGCCTGCGCATGCCACCCACTGTGCGGGCCTTCGTGGCC
TCCCGCGGCACCAAGCAGGAGGAATTCGAGAGCATTGAGGAGGCGCTGCCTGACACTGAT
GTGCTCTACATGACTCGAATCCAGAAGGAACGATTTGGCTCTACCCAGGAGTACGAAGCT
TGCTTTGGTCAGTTCATCCTCACTCCCCACATCATGACCCGGGCCAAGAAGAAGATGGTG
GTGATGCACCCGATGCCCCGTGTCAACGAGATAAGCGTGGAAGTGGACTCGGATCCCCGC
GCAGCCTACTTCCGCCAGGCTGAGAACGGCATGTACATCCGCATGGCTCTGTTAGCCACC
GTGCTGGGCCGTTTCTAG
Enzyme 2 GenBank Gene ID D78586 Link Image
Enzyme 2 GeneCard ID CAD Link Image
Enzyme 2 GenAtlas ID CAD Link Image
Enzyme 2 HGNC ID HGNC:1424 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 2p22-p21
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Iwahana H, Fujimura M, Ii S, Kondo M, Moritani M, Takahashi Y, Yamaoka T, Yoshimoto K, Itakura M: Molecular cloning of a human cDNA encoding a trifunctional enzyme of carbamoyl-phosphate synthetase-aspartate transcarbamoylase-dihydroorotase in de Novo pyrimidine synthesis. Biochem Biophys Res Commun. 1996 Feb 6;219(1):249-55. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Davidson JN, Rao GN, Niswander L, Andreano C, Tamer C, Chen KC: Organization and nucleotide sequence of the 3' end of the human CAD gene. DNA Cell Biol. 1990 Nov;9(9):667-76. [PubMed Link Image]
  4. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  5. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  6. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  7. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  9. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  10. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  11. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  12. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  13. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available