Pyridoxamine kinase (P77150)

Identification
Name:Pyridoxamine kinase
Synonyms:
  • PM kinase
Gene Name:pdxY
Enzyme Class:
Biological Properties
General Function:Involved in pyridoxal kinase activity
Specific Function:Phosphorylates B6 vitamers; functions in a salvage pathway. Uses pyridoxamine, but has negligible activity toward pyridoxal and pyridoxine as substrates
Cellular Location:Not Available
SMPDB Pathways:Not Available
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Pyridoxal ↔ 1.0ADP + 1.0Hydrogen ion + 1.0Pyridoxal 5'-phosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Pyridoxine → 1.0ADP + 1.0Hydrogen ion + 1.0Pyridoxine 5'-phosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Pyridoxamine → 1.0ADP + 1.0Hydrogen ion + 1.0Pyridoxamine 5'-phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Pyridoxal ↔ 1.0ADP + 1.0Pyridoxal 5'-phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Pyridoxine ↔ 1.0ADP + 1.0Pyridoxine 5'-phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Pyridoxamine ↔ 1.0ADP + 1.0Pyridoxamine 5'-phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Pyridoxal ↔ 1.0ADP + 1.0Hydrogen ion + 1.0Pyridoxal 5'-phosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Pyridoxine → 1.0ADP + 1.0Hydrogen ion + 1.0Pyridoxine 5'-phosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Pyridoxamine → 1.0ADP + 1.0Hydrogen ion + 1.0Pyridoxamine 5'-phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Pyridoxamine ↔ 1.0ADP + 1.0Pyridoxamine 5'-phosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Pyridoxal → 1.0Hydrogen ion + 1.0ADP + 1.0Pyridoxal 5'-phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB01545PyridoxalMetaboCard
ECMDB01491Pyridoxal 5'-phosphateMetaboCard
ECMDB01431PyridoxamineMetaboCard
ECMDB01555Pyridoxamine 5'-phosphateMetaboCard
ECMDB00239PyridoxineMetaboCard
ECMDB01319Pyridoxine 5'-phosphateMetaboCard
GO Classification:
Function
catalytic activity
kinase activity
pyridoxal kinase activity
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
metabolic process
pyridoxine biosynthetic process
pyridoxine metabolic process
small molecule metabolic process
vitamin B6 metabolic process
vitamin metabolic process
water-soluble vitamin metabolic process
Gene Properties
Blattner:b1636
Gene OrientationCounterclockwise
Centisome Percentage:36.92
Left Sequence End1713050
Right Sequence End1713913
Gene Sequence:
>864 bp
GTGTGGGCGCTAACTGCGGATGCGGATTTTCTGGCGCAGCGGGGGCAAGGACAGGTTGAA
CAGGTCTTTGCCAGAGCGGTAAATATCGCACTCCCGGCTCGCCAGCAGTTGCTGACGCTG
CTTTGTGAAGAGTACGACAATGCGCCAAACAGTTGTCGGTTGGCACTCACTCACTTTGAT
GATCTGTTCCGGCATGGTGATAAGGTTCAGTTTGACGATCAAGGTATTACGGTTGGTCAA
CATCTTCATATAGAGATGAGTCGTTGTCGGCGTTGGCTGTCCCCAACCTTGCAAATGACC
GCTGTGAATTTTCACCTTATCGCCTGGCTACAGTGGCACGACATTATTCATCAGCACCTG
GGGGAAAATGAAACCCTGTTTAATTATCGCGGCGATAATCCGTTTTATCAGGCGTTAAAT
AAAGAATTACATATTAAACGACGGGCAGTTATTCAGGCCGTAAACGATAAACAAAATATC
GCCTCAGCGGTCGCCAGTATGATGGGGTTAGGGATTGGCCTTACGCCATCAGCCGACGAT
TATTTAACAGGTCTGGCGCTTATTTTATTTATTCCCGGGCATCCGGCGGAAAAATACAAA
GAGGAATTTTATCTCGGTCTGCAACGCGGCAAAAATAATACCACATTATTAAGTGCCATA
ACGCTGGAAGCCGCATTACAACAACGCTGCCGGGAAAATATTCATCGTTTTATTCACAAC
ATTATTTATGACATCCCTGGGAACGCAACTCAGGCAATAGAAAAAATTAAACATATTGGC
TCCAGTTCCGGCTGCGACATGCTGTATGGCATGGCCGATGGTTGTGCGCTGAGCCAAACC
TACGGAGGGAATTATGTCAGTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:287
Protein Molecular Weight:31322
Protein Theoretical pI:7
PDB File:1TD2
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Pyridoxamine kinase
MMKNILAIQSHVVYGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPSHL
TEIVQGIAAIDKLHTCDAVLSGYLGSAEQGEHILGIVRQVKAANPQAKYFCDPVMGHPEK
GCIVAPGVAEFHVRHGLPASDIIAPNLVELEILCEHAVNNVEEAVLAARELIAQGPQIVL
VKHLARAGYSRDRFEMLLVTADEAWHISRPLVDFGMRQPVGVGDVTSGLLLVKLLQGATL
QEALEHVTAAVYEIMVTTKAMQEYELQVVAAQDRIAKPEHYFSATKL
References
External Links:
ResourceLink
Uniprot ID:P77150
Uniprot Name:PDXY_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674462
PDB ID:1TD2
Ecogene ID:EG13940
Ecocyc:EG13940
ColiBase:b1636
Kegg Gene:b1636
EchoBASE ID:EB3699
CCDB:PDXY_ECOLI
BacMap:16129594
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., 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., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • 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
  • 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
  • Safo, M. K., Musayev, F. N., Hunt, S., di Salvo, M. L., Scarsdale, N., Schirch, V. (2004). "Crystal structure of the PdxY Protein from Escherichia coli." J Bacteriol 186:8074-8082. Pubmed: 15547280
  • Yang, Y., Tsui, H. C., Man, T. K., Winkler, M. E. (1998). "Identification and function of the pdxY gene, which encodes a novel pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate biosynthesis in Escherichia coli K-12." J Bacteriol 180:1814-1821. Pubmed: 9537380