Histidine biosynthesis trifunctional protein (P00815)

Identification
NameHistidine biosynthesis trifunctional protein
Synonyms
  • Phosphoribosyl-AMP cyclohydrolase
  • Phosphoribosyl-ATP pyrophosphohydrolase
  • Histidinol dehydrogenase
  • HDH
Gene NameHIS4
Enzyme Class
Biological Properties
General FunctionInvolved in oxidoreductase activity
Specific Function1-(5-phosphoribosyl)-AMP + H(2)O = 1-(5- phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino)imidazole-4-carboxamide
Cellular LocationCytoplasmic
SMPDB Pathways
Histidine BiosynthesisPW002418 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Histidine metabolismec00340 Map00340
SMPDB Reactions
1-(5-phosphoribosyl)-ATP + water → hydron + Pyrophosphate + Phosphoribosyl-AMP
Phosphoribosyl-AMP → water + PhosphoribosylformiminoAICAR-phosphate
water + 1-(5-phosphoribosyl)-ATP → Phosphoribosyl-AMP + hydron + Pyrophosphate
L-histidinol + NAD → hydron + NADH + Histidinal
Histidinal + water + NAD → hydron + NADH + L-Histidine
KEGG Reactions
water + NAD + L-histidinol → NADH + L-Histidine + hydron
1-(5-phosphoribosyl)-5'-AMP + water → 1-(5-phospho-D-ribosyl)-5-[(5-phospho-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
water + 5-phosphoribosyl-ATP → Pyrophosphate + 1-(5-phosphoribosyl)-5'-AMP + hydron
Metabolites
YMDB IDNameView
YMDB00110NADShow
YMDB00143NADHShow
YMDB00165Phosphoribosyl-ATPShow
YMDB00219PyrophosphateShow
YMDB00317Phosphoribosyl-AMPShow
YMDB00369L-HistidineShow
YMDB00412NAD(+)Show
YMDB004171-(5-phospho-D-ribosyl)-5-[(5-phospho-D-ribosylamino)methylideneamino]imidazole-4-carboxamideShow
YMDB00702L-histidinolShow
YMDB00862hydronShow
YMDB008681-(5-phosphoribosyl)-5'-AMPShow
YMDB00890waterShow
YMDB16235HistidinalShow
YMDB16238PhosphoribosylformiminoAICAR-phosphateShow
YMDB162741-(5-phosphoribosyl)-ATPShow
GO Classification
Component
Not Available
Function
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
cyclohydrolase activity
ion binding
pyrophosphatase activity
cation binding
phosphoribosyl-ATP diphosphatase activity
metal ion binding
phosphoribosyl-AMP cyclohydrolase activity
transition metal ion binding
histidinol dehydrogenase activity
oxidoreductase activity
catalytic activity
zinc ion binding
hydrolase activity
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
oxidoreductase activity, acting on CH-OH group of donors
hydrolase activity, acting on acid anhydrides
binding
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
nucleotide binding
NAD or NADH binding
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
Process
histidine metabolic process
histidine biosynthetic process
oxidation reduction
metabolic process
cellular metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
histidine family amino acid metabolic process
Gene Properties
Chromosome Locationchromosome 3
LocusYCL030C
Gene Sequence>2400 bp ATGGTTTTGCCGATTCTACCGTTAATTGATGATCTGGCCTCATGGAATAGTAAGAAGGAA TACGTTTCACTTGTTGGTCAGGTACTTTTGGATGGCTCGAGCCTGAGTAATGAAGAGATT CTCCAGTTCTCCAAAGAGGAAGAAGTTCCATTGGTGCGTTTGTCCTTGCCAAGTGGTAAA TTCAGCGATGATGAAATCATTGCCTTCTTGAACAACGGAGTTTCTTCTCTGTTCATTGCT AGCCAAGATGCTAAAACAGCCGAACACTTGGTTGAACAATTGAATGTACCAAAGGAGCGT GTTGTTGTGGAAGAGAACGGTGTTTTCTCCAATCAATTCATGGTAAAACAAAAATTCTCG CAAGATAAAATTGTGTCCATAAAGAAATTAAGCAAGGATATGTTGACCAAAGAAGTGCTT GGTGAAGTACGTACAGACCGTCCTGACGGTTTATATACCACCCTAGTTGTCGACCAATAT GAGCGTTGTCTAGGGTTGGTGTATTCTTCGAAGAAATCTATAGCAAAGGCCATCGATTTG GGTCGTGGCGTTTATTATTCTCGTTCTAGGAATGAAATCTGGATCAAGGGTGAAACTTCT GGCAATGGCCAAAAGCTTTTACAAATCTCTACTGACTGTGATTCGGATGCCTTAAAGTTT ATCGTTGAACAAGAAAACGTTGGATTTTGCCACTTGGAGACCATGTCTTGCTTTGGTGAA TTCAAGCATGGTTTGGTGGGGCTAGAATCTTTACTAAAACAAAGGCTACAGGACGCTCCA GAGGAATCTTATACTAGAAGACTATTCAACGACTCTGCATTGTTAGATGCCAAGATCAAG GAAGAAGCTGAAGAACTGACTGAGGCAAAGGGTAAGAAGGAGCTTTCTTGGGAGGCTGCC GATTTGTTCTACTTTGCACTGGCCAAATTAGTGGCCAACGATGTTTCATTGAAGGACGTC GAGAATAATCTGAATATGAAGCATCTGAAGGTTACAAGACGGAAAGGTGATGCTAAGCCA AAGTTTGTTGGACAACCAAAGGCTGAAGAAGAAAAACTGACCGGTCCAATTCACTTGGAC GTGGTGAAGGCTTCCGACAAAGTTGGTGTGCAGAAGGCTTTGAGCAGACCAATCCAAAAG ACTTCTGAAATTATGTATTTAGTCAATCCGATCATCGAAAATGTTAGAGACAAAGGTAAC TCTGTTTTTTTGGAGTACACAGAAAAGTTTGATGGTGTAAAATTATCCAATCCTGTTCTT AATGCTCCATTCCCAGAAGAATACTTTGAAGGTTTAACCGAGGAAATGAAGGAAGCTTTG AACCTTTCAATTGAAAACGTCCGCAAATTCCATGCTGCTCAATTGCCAACAGAGACTCTT GAAGTTGAAACCCAACCTGGTGTCTTGTGTTCCAGATTCCCTCGTCCTATTGAAAAAGTT GGTTTGTATATCCCTGGTGGCACTGCCATTTTACCAAGTACTGCATTAATGCTTGGTGTT CCAGCACAAGTTGCCCAATGTAAGGAGATTGTGTTTGCATCTCCACCAAGAAAATCTGAT GGTAAAGTTTCACCCGAAGTTGTTTATGTCGCAGAAAAAGTTGGCGCTTCCAAGATTGTT CTAGCTGGTGGTGCCCAAGCCGTTGCTGCTATGGCTTACGGGACAGAAACTATTCCTAAA GTGGATAAGATCTTGGGTCCAGGTAATCAATTTGTGACTGCCGCCAAAATGTATGTTCAA AATGACACTCAAGCTCTATGTTCCATTGATATGCCAGCTGGCCCAAGTGAAGTTTTGGTT ATTGCCGATGAAGATGCCGATGTGGATTTTGTTGCAAGTGATTTGCTATCGCAAGCTGAA CACGGTATTGACTCCCAAGTTATCCTTGTTGGTGTTAACTTGAGCGAAAAGAAAATTCAA GAGATTCAAGATGCTGTTCACAATCAAGCTTTACAACTGCCACGTGTGGATATTGTTCGT AAATGTATTGCTCACAGTACGATCGTTCTTTGTGACGGTTACGAAGAAGCCCTTGAAATG TCCAACCAATATGCACCAGAACATTTGATTCTACAAATCGCCAATGCTAACGATTATGTT AAATTGGTTGACAATGCAGGGTCCGTATTTGTGGGTGCTTACACTCCAGAATCGTGCGGT GACTATTCAAGTGGTACTAACCATACATTACCAACCTATGGTTACGCTAGGCAGTACAGT GGTGCCAACACTGCAACCTTCCAAAAGTTTATCACTGCCCAAAACATTACCCCTGAAGGT TTAGAAAACATCGGTAGAGCTGTTATGTGCGTTGCCAAGAAGGAGGGTCTAGACGGTCAC AGAAACGCTGTGAAAATCAGAATGAGTAAGCTTGGGTTGTTCCCAAAGGATTTCCAGTAG
Protein Properties
Pfam Domain Function
Protein Residues799
Protein Molecular Weight87720.5
Protein Theoretical pI4.94
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Histidine biosynthesis trifunctional protein MVLPILPLIDDLASWNSKKEYVSLVGQVLLDGSSLSNEEILQFSKEEEVPLVALSLPSGK FSDDEIIAFLNNGVSSLFIASQDAKTAEHLVEQLNVPKERVVVEENGVFSNQFMVKQKFS QDKIVSIKKLSKDMLTKEVLGEVRTDRPDGLYTTLVVDQYERCLGLVYSSKKSIAKAIDL GRGVYYSRSRNEIWIKGETSGNGQKLLQISTDCDSDALKFIVEQENVGFCHLETMSCFGE FKHGLVGLESLLKQRLQDAPEESYTRRLFNDSALLDAKIKEEAEELTEAKGKKELSWEAA DLFYFALAKLVANDVSLKDVENNLNMKHLKVTRRKGDAKPKFVGQPKAEEEKLTGPIHLD VVKASDKVGVQKALSRPIQKTSEIMHLVNPIIENVRDKGNSALLEYTEKFDGVKLSNPVL NAPFPEEYFEGLTEEMKEALDLSIENVRKFHAAQLPTETLEVETQPGVLCSRFPRPIEKV GLYIPGGTAILPSTALMLGVPAQVAQCKEIVFASPPRKSDGKVSPEVVYVAEKVGASKIV LAGGAQAVAAMAYGTETIPKVDKILGPGNQFVTAAKMYVQNDTQALCSIDMPAGPSEVLV IADEDADVDFVASDLLSQAEHGIDSQVILVGVNLSEKKIQEIQDAVHNQALQLPRVDIVR KCIAHSTIVLCDGYEEALEMSNQYAPEHLILQIANANDYVKLVDNAGSVFVGAYTPESCG DYSSGTNHTLPTYGYARQYSGANTATFQKFITAQNITPEGLENIGRAVMCVAKKEGLDGH RNAVKIRMSKLGLIPKDFQ
References
External Links
ResourceLink
Saccharomyces Genome Database HIS4
Uniprot IDP00815
Uniprot NameHIS2_YEAST
GenBank Gene IDV01310
Genebank Protein ID3785
General Reference
  • Donahue, T. F., Farabaugh, P. J., Fink, G. R. (1982). "The nucleotide sequence of the HIS4 region of yeast." Gene 18:47-59.7049842
  • Rad, M. R., Lutzenkirchen, K., Xu, G., Kleinhans, U., Hollenberg, C. P. (1991). "The complete sequence of a 11,953 bp fragment from C1G on chromosome III encompasses four new open reading frames." Yeast 7:533-538.1897318
  • Oliver, S. G., van der Aart, Q. J., Agostoni-Carbone, M. L., Aigle, M., Alberghina, L., Alexandraki, D., Antoine, G., Anwar, R., Ballesta, J. P., Benit, P., et, a. l. .. (1992). "The complete DNA sequence of yeast chromosome III." Nature 357:38-46.1574125
  • Farabaugh, P. J., Fink, G. R. (1980). "Insertion of the eukaryotic transposable element Ty1 creates a 5-base pair duplication." Nature 286:352-356.6250062
  • Roeder, G. S., Rose, A. B., Pearlman, R. E. (1985). "Transposable element sequences involved in the enhancement of yeast gene expression." Proc Natl Acad Sci U S A 82:5428-5432.2991923
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956