{"ymdb_id":"YMDB00668","created_at":"2011-05-29T18:41:57.000Z","updated_at":"2016-09-08T18:35:45.000Z","name":"7,8-dihydroneopterin 3'-phosphate","cas":null,"state":null,"melting_point":null,"description":"7,8-Dihydroneopterin 3'-phosphate is the precursor to 7,8-dihydroneopterin in the 6-hydroxymethyl-dihydropterin diphosphate biosynthesis pathway. 6-Hydroxymethyl-dihydropterin diphosphate is the pterin precursor for the biosynthesis of several important cofactors, including tetrahydrofolate, methanopterin and sarcinapterin. [Biocyc PWY-6147]","experimental_water_solubility":null,"experimental_logp_hydrophobicity":null,"location":"cytoplasm","synthesis_reference":null,"chebi_id":"48954","hmdb_id":null,"kegg_id":"C05925","pubchem_id":"25245170","cs_id":"21865614","foodb_id":null,"wikipedia_link":null,"biocyc_id":null,"iupac":"[(2R,3S)-3-(2-amino-4-oxo-1,4,7,8-tetrahydropteridin-6-yl)-2,3-dihydroxypropoxy]phosphonic acid","traditional_iupac":"(2R,3S)-3-(2-amino-4-oxo-7,8-dihydro-1H-pteridin-6-yl)-2,3-dihydroxypropoxyphosphonic acid","logp":"-3.645897293721321","pka":"6.508991148749795","alogps_solubility":"5.26e+00 g/l","alogps_logp":"-2.30","alogps_logs":"-1.80","acceptor_count":"11","donor_count":"7","rotatable_bond_count":"5","polar_surface_area":"199.09","refractivity":"80.5299","polarizability":"28.708219078730725","formal_charge":"0","physiological_charge":"-2","pka_strongest_basic":"0.18347444009312497","pka_strongest_acidic":"1.506217875759555","bioavailability":"0","number_of_rings":"2","rule_of_five":"0","ghose_filter":"0","veber_rule":"0","mddr_like_rule":"0","synonyms":["2-amino-4-hydroxy-6-(erythro-1,2,3-trihydroxypropyl)dihydropteridine phosphate","Dihydroneopterin phosphate"],"pathways":[{"name":"Folate biosynthesis","kegg_map_id":"00790"},{"name":"tetrahydrofolate biosynthesis","kegg_map_id":null}],"growth_conditions":[],"references":[{"pubmed_id":18846089,"citation":"Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). \"A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology.\" Nat Biotechnol 26:1155-1160."}],"proteins":[{"created_at":"2011-05-27T09:05:09.000Z","updated_at":"2011-07-22T17:54:37.000Z","name":"ATPase GET3","uniprot_id":"Q12154","uniprot_name":"GET3_YEAST","enzyme":true,"transporter":false,"gene_name":"GET3","num_residues":354,"molecular_weight":"39353.39844","theoretical_pi":"4.61","general_function":"Inorganic ion transport and metabolism","specific_function":"ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors GET1 and GET2, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the GET1-GET2 receptor, and returning it to the cytosol to initiate a new round of targeting. Cooperates with the HDEL receptor ERD2 to mediate the ATP-dependent retrieval of resident ER proteins that contain a C-terminal H-D-E-L retention signal from the Golgi to the ER. Involved in low-level resistance to the oxyanions arsenite and arsenate, and in heat tolerance","reactions":[{"id":1458,"direction":"\u003e","locations":"cytoplasm","altext":null,"export":true,"pw_reaction_id":null,"source":null}],"signal_regions":"None","transmembrane_regions":"None","pdb_id":null,"cellular_location":"Cytoplasm. Endoplasmic reticulum. Golgi apparatus.","genbank_gene_id":"AY693164","genbank_protein_id":"51013779","gene_card_id":"GET3","chromosome_location":"chromosome 4","locus":"YDL100C","synonyms":["Arsenical pump-driving ATPase","Arsenite-stimulated ATPase","Golgi to ER traffic protein 3","Guided entry of tail-anchored proteins 3"],"enzyme_classes":["3.6.-.-"],"go_classes":[{"category":"Component","description":" Not Available"},{"category":"Function","description":" binding"},{"category":"Function","description":" nucleoside binding"},{"category":"Function","description":" purine nucleoside binding"},{"category":"Function","description":" adenyl nucleotide binding"},{"category":"Function","description":" adenyl ribonucleotide binding"},{"category":"Function","description":" ATP binding"},{"category":"Process","description":" chemical homeostasis"},{"category":"Process","description":" ion homeostasis"},{"category":"Process","description":" cellular ion homeostasis"},{"category":"Process","description":" cellular cation homeostasis"},{"category":"Process","description":" cellular metal ion homeostasis"},{"category":"Process","description":" biological regulation"},{"category":"Process","description":" regulation of biological quality"},{"category":"Process","description":" homeostatic process"}],"pfams":[],"pathways":[],"gene_sequence":"ATGGATTTAACCGTGGAACCTAATTTGCACTCTTTAATTACCTCTACCACTCATAAGTGGATTTTCGTTGGTGGTAAAGGTGGTGTTGGTAAGACTACTTCATCATGTTCCATTGCTATCCAAATGACTTTGAGTCAACCAAACAAACAGTTCCTACTGATCTCTACTGATCCTGCCCATAACTTAAGTGATGCATTCGGTGAGAAATTTGGTAAAGACGCCAGAAAGGTGACAGGCATGAATAATCTATCATGTATGGAAATCGATCCATCCGCTGCTTTGAAGGATATGAACGACATGGCAGTTTCACGCGCTAACAATAACGGAAGTGACGGTCAAGGTGACGATCTAGGAAGCTTGCTTCAAGGTGGTGCTCTTGCTGATTTGACCGGTTCCATCCCTGGTATCGACGAAGCTTTATCCTTCATGGAAGTCATGAAGCACATTAAAAGGCAAGAACAGGGCGAAGGTGAAACCTTCGATACTGTTATTTTTGACACTGCTCCAACTGGCCACACATTAAGATTTCTACAACTACCAAATACTTTATCCAAGCTTTTGGAAAAGTTCGGTGAAATTACCAACAAATTGGGCCCAATGCTAAACTCTTTTATGGGCGCAGGTAATGTCGATATCTCTGGAAAATTGAACGAGTTAAAGGCTAATGTCGAGACCATCAGACAACAATTCACGGATCCTGACCTAACGACTTTTGTTTGCGTTTGTATCAGTGAATTCTTATCCTTATATGAAACTGAAAGACTAATTCAGGAATTGATTTCCTACGATATGGACGTTAATTCCATCATTGTCAACCAATTATTATTTGCTGAAAACGATCAAGAGCACAACTGTAAGAGATGTCAGGCAAGATGGAAGATGCAAAAGAAGTACTTGGACCAAATCGACGAATTGTACGAAGATTTCCATGTCGTTAAAATGCCATTATGTGCTGGAGAAATCAGAGGCTTAAATAACTTAACAAAGTTCTCACAGTTCCTAAACAAAGAATATAACCCTATTACTGATGGCAAAGTCATTTATGAGTTAGAAGATAAGGAATAG","protein_sequence":"MDLTVEPNLHSLITSTTHKWIFVGGKGGVGKTTSSCSIAIQMALSQPNKQFLLISTDPAHNLSDAFGEKFGKDARKVTGMNNLSCMEIDPSAALKDMNDMAVSRANNNGSDGQGDDLGSLLQGGALADLTGSIPGIDEALSFMEVMKHIKRQEQGEGETFDTVIFDTAPTGHTLRFLQLPNTLSKLLEKFGEITNKLGPMLNSFMGAGNVDISGKLNELKANVETIRQQFTDPDLTTFVCVCISEFLSLYETERLIQELISYDMDVNSIIVNQLLFAENDQEHNCKRCQARWKMQKKYLDQIDELYEDFHVVKMPLCAGEIRGLNNLTKFSQFLNKEYNPITDGKVIYELEDKE"}]}