Histidinol-phosphate aminotransferase (P06986)

Identification
Name:Histidinol-phosphate aminotransferase
Synonyms:
  • Imidazole acetol-phosphate transaminase
  • HPAT
  • HspAT
Gene Name:hisC
Enzyme Class:
Biological Properties
General Function:Involved in transferase activity
Specific Function:L-histidinol phosphate + 2-oxoglutarate = 3- (imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0alpha-Ketoglutarate + 1.0L-Phenylalanine ↔ 1.0L-Glutamate + 1.0Phenylpyruvic acid
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0alpha-Ketoglutarate + 1.0L-Tyrosine ↔ 1.04-Hydroxyphenylpyruvic acid + 1.0L-Glutamate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0L-Glutamate + 1.0Imidazole acetol-phosphate ↔ 1.0alpha-Ketoglutarate + 1.0Histidinol phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Histidinol phosphate + 1.0alpha-Ketoglutarate ↔ 1.0Imidazole acetol-phosphate + 1.0L-Glutamate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0L-Glutamic acid+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Imidazole acetol-phosphate + 1.0L-Glutamic acid + 1.0L-Glutamate → 1.0Oxoglutaric acid + 1.0L-histidinol-phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Histidinol phosphate + 1.0Oxoglutaric acid → 1.0Imidazole acetol-phosphate + 1.0L-Glutamate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB007074-Hydroxyphenylpyruvic acidMetaboCard
ECMDB02812alpha-KetoglutarateMetaboCard
ECMDB03287Histidinol phosphateMetaboCard
ECMDB12236Imidazole acetol-phosphateMetaboCard
ECMDB00148L-GlutamateMetaboCard
ECMDB24197L-histidinol-phosphateMetaboCard
ECMDB00159L-PhenylalanineMetaboCard
ECMDB00158L-TyrosineMetaboCard
ECMDB04123Oxoglutaric acidMetaboCard
ECMDB00205Phenylpyruvic acidMetaboCard
GO Classification:
Function
binding
catalytic activity
cofactor binding
histidinol-phosphate transaminase activity
pyridoxal phosphate binding
transaminase activity
transferase activity
transferase activity, transferring nitrogenous groups
Process
biosynthetic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
histidine biosynthetic process
histidine family amino acid metabolic process
histidine metabolic process
metabolic process
Gene Properties
Blattner:b2021
Gene OrientationClockwise
Centisome Percentage:45.06
Left Sequence End2090422
Right Sequence End2091492
Gene Sequence:
>1071 bp
ATGCGCGTTACCGATTTCTCCTTTGAATTGCCCGAATCCCTGATTGCCCACTATCCCATG
CCTGAACGCAGTAGCTGTCGTTTACTGTCGCTGGACGGGCCGACGGGCGCGCTGACGCAC
GGTACTTTCACCGATTTACTTGATAAGCTCAACCCCGGCGATCTTCTGGTTTTTAATAAT
ACCCGCGTGATCCCGGCGCGCCTGTTTGGGCGTAAAGCCAGCGGCGGCAAGATTGAAGTG
CTGGTTGAACGGATGCTCGACGACAAACGCATTCTTGCGCATATTCGCGCCTCGAAAGCG
CCAAAACCTGGCGCAGAACTGCTGCTGGGCGATGACGAAAGTATTAACGCAACAATGACC
GCGCGCCACGGCGCACTGTTTGAAGTCGAATTTAATGATGAACGCTCGGTGCTGGATATT
CTCAACAGCATCGGCCATATGCCGCTGCCGCCGTATATCGACCGTCCGGACGAAGACGCT
GACCGCGAACTTTATCAAACCGTTTATAGCGAAAAACCGGGCGCGGTTGCAGCCCCGACC
GCAGGTCTGCATTTTGACGAGCCTTTGCTGGAAAAATTGCGCGCCAAAGGCGTGGAGATG
GCGTTTGTGACGTTGCACGTTGGTGCGGGCACCTTCCAGCCGGTGCGCGTCGACACCATT
GAAGATCACATCATGCACTCGGAATACGCTGAAGTACCGCAGGATGTGGTAGACGCGGTA
CTGGCGGCGAAAGCGCGCGGTAACCGGGTGATTGCGGTTGGCACCACTTCAGTACGTTCG
CTGGAAAGCGCGGCTCAGGCAGCGAAAAACGATCTCATTGAACCGTTCTTCGACGATACC
CAAATCTTTATCTATCCGGGCTTCCAGTACAAAGTGGTCGATGCGCTGGTGACGAACTTC
CACTTGCCAGAGTCGACGCTGATTATGCTGGTTTCGGCCTTTGCCGGTTATCAACACACC
ATGAACGCCTATAAAGCAGCGGTAGAAGAGAAATATCGCTTTTTTAGTTACGGTGATGCG
ATGTTTATCACGTACAATCCGCAGGCAATTAATGAGCGCGTCGGGGAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:356
Protein Molecular Weight:39360
Protein Theoretical pI:5
PDB File:1GEY
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Histidinol-phosphate aminotransferase
MSTVTITDLARENVRNLTPYQSARRLGGNGDVWLNANEYPTAVEFQLTQQTLNRYPECQP
KAVIENYAQYAGVKPEQVLVSRGADEGIELLIRAFCEPGKDAILYCPPTYGMYSVSAETI
GVECRTVPTLDNWQLDLQGISDKLDGVKVVYVCSPNNPTGQLINPQDFRTLLELTRGKAI
VVADEAYIEFCPQASLAGWLAEYPHLAILRTLSKAFALAGLRCGFTLANEEVINLLMKVI
APYPLSTPVADIAAQALSPQGIVAMRERVAQIIAEREYLIAALKEIPCVEQVFDSETNYI
LARFKASSAVFKSLWDQGIILRDQNKQPSLSGCLRITVGTREESQRVIDALRAEQV
References
External Links:
ResourceLink
Uniprot ID:P06986
Uniprot Name:HIS8_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674545
PDB ID:1GEY
Ecogene ID:EG10446
Ecocyc:EG10446
ColiBase:b2021
Kegg Gene:b2021
EchoBASE ID:EB0441
CCDB:HIS8_ECOLI
BacMap:16129962
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Carlomagno, M. S., Chiariotti, L., Alifano, P., Nappo, A. G., Bruni, C. B. (1988). "Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons." J Mol Biol 203:585-606. Pubmed: 3062174
  • Grisolia, V., Carlomagno, M. S., Nappo, A. G., Bruni, C. B. (1985). "Cloning, structure, and expression of the Escherichia coli K-12 hisC gene." J Bacteriol 164:1317-1323. Pubmed: 2999081
  • Haruyama, K., Nakai, T., Miyahara, I., Hirotsu, K., Mizuguchi, H., Hayashi, H., Kagamiyama, H. (2001). "Structures of Escherichia coli histidinol-phosphate aminotransferase and its complexes with histidinol-phosphate and N-(5'-phosphopyridoxyl)-L-glutamate: double substrate recognition of the enzyme." Biochemistry 40:4633-4644. Pubmed: 11294630
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Itoh, T., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Kasai, H., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Seki, Y., Horiuchi, T., et, a. l. .. (1996). "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." DNA Res 3:379-392. Pubmed: 9097040
  • Jovanovic, G., Kostic, T., Jankovic, M., Savic, D. J. (1994). "Nucleotide sequence of the Escherichia coli K12 histidine operon revisited." J Mol Biol 239:433-435. Pubmed: 8201624
  • Sivaraman, J., Li, Y., Larocque, R., Schrag, J. D., Cygler, M., Matte, A. (2001). "Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and l-histidinol phosphate." J Mol Biol 311:761-776. Pubmed: 11518529