ECMDB

Identification

Name:

Phosphoserine aminotransferase

Synonyms:

Phosphohydroxythreonine aminotransferase
PSAT

Gene Name:

serC

Enzyme Class:

2.6.1.52

Biological Properties

General Function:

Involved in metabolic process

Specific Function:

Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine. Is involved in both pyridoxine and serine biosynthesis

Cellular Location:

Cytoplasm

SMPDB Pathways:

Secondary Metabolites: cysteine biosynthesis from serine PW000977
Vitamin B6 1430936196 PW000891
cysteine biosynthesis PW000800
serine biosynthesis and metabolism PW000809

KEGG Pathways:

Glycine, serine and threonine metabolism ec00260
Metabolic pathways eco01100
Methane metabolism ec00680
Microbial metabolism in diverse environments ec01120
Vitamin B6 metabolism ec00750

KEGG Reactions:

1.0

↔

1.0

1.0L-Glutamate + 1.02-Oxo-3-hydroxy-4-phosphobutanoic acid ↔ 1.0alpha-Ketoglutarate + 1.0O-Phospho-4-hydroxy-L-threonine
ReactionCard

1.0

→

1.0

1.0Phosphohydroxypyruvic acid + 1.0L-Glutamate → 1.0alpha-Ketoglutarate + 1.0Phosphoserine
ReactionCard

1.0

↔

1.0

1.0Phosphoserine + 1.0alpha-Ketoglutarate ↔ 1.0Phosphohydroxypyruvic acid + 1.0L-Glutamate
ReactionCard

1.0

↔

1.0

1.0O-Phospho-4-hydroxy-L-threonine + 1.0alpha-Ketoglutarate ↔ 1.02-Oxo-3-hydroxy-4-phosphobutanoic acid + 1.0L-Glutamate
ReactionCard

1.0

↔

1.0

1.0Phosphoserine + 1.0alpha-Ketoglutarate + 1.0O-Phospho-4-hydroxy-L-threonine ↔ 1.0Phosphohydroxypyruvic acid + 1.0L-Glutamate + 1.02-Oxo-3-hydroxy-4-phosphobutanoic acid
ReactionCard

SMPDB Reactions:

1.0

1.0L-Glutamic acid

1.0

→

1.0

1.0Phosphohydroxypyruvic acid + 1.0L-Glutamic acid + 1.0L-Glutamate → 1.0Oxoglutaric acid + 1.0DL-O-Phosphoserine
ReactionCard

1.0

1.0L-Glutamic acid

1.0

↔

1.0A-Ketoglutaric acid oxime

1.0

1.02-Oxo-3-hydroxy-4-phosphobutanoic acid + 1.0L-Glutamic acid + 1.0L-Glutamate ↔ 1.0A-Ketoglutaric acid oxime + 1.0O-Phospho-4-hydroxy-L-threonine
ReactionCard

1.0L-Glutamic acid

1.0

↔

1.0

1.0L-Glutamic acid + 1.0L-Glutamate ↔ 1.0O-Phospho-4-hydroxy-L-threonine
ReactionCard

1.0L-Glutamic acid

1.0

↔

1.0

1.0L-Glutamic acid + 1.0L-Glutamate ↔ 1.0Oxoglutaric acid + 1.0O-Phospho-4-hydroxy-L-threonine
ReactionCard

1.0L-Glutamic acid

1.0

↔

1.0

1.0A-Ketoglutaric acid oxime

1.0L-Glutamic acid + 1.0L-Glutamate ↔ 1.0O-Phospho-4-hydroxy-L-threonine + 1.0A-Ketoglutaric acid oxime
ReactionCard

1.0

1.0L-Glutamic acid

1.0

↔

1.0

1.02-Oxo-3-hydroxy-4-phosphobutanoic acid + 1.0L-Glutamic acid + 1.0L-Glutamate ↔ 1.0O-Phospho-4-hydroxy-L-threonine + 1.0Oxoglutaric acid
ReactionCard

EcoCyc Reactions:

1.0

→

1.0

1.0Phosphoserine + 1.0Oxoglutaric acid → 1.0Phosphohydroxypyruvic acid + 1.0L-Glutamate
ReactionCard

1.0

→

1.0

1.0O-Phospho-4-hydroxy-L-threonine + 1.0Oxoglutaric acid → 1.02-Oxo-3-hydroxy-4-phosphobutanoic acid + 1.0L-Glutamate
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB06801	2-Oxo-3-hydroxy-4-phosphobutanoic acid	MetaboCard
ECMDB02812	alpha-Ketoglutarate	MetaboCard
ECMDB24073	DL-O-Phosphoserine	MetaboCard
ECMDB00148	L-Glutamate	MetaboCard
ECMDB06802	O-Phospho-4-hydroxy-L-threonine	MetaboCard
ECMDB04123	Oxoglutaric acid	MetaboCard
ECMDB01024	Phosphohydroxypyruvic acid	MetaboCard
ECMDB00272	Phosphoserine	MetaboCard

GO Classification:

Function
binding
catalytic activity
cofactor binding
pyridoxal phosphate binding
Process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
L-serine biosynthetic process
L-serine metabolic process
metabolic process
serine family amino acid metabolic process

Gene Properties

Blattner:

b0907

Gene Orientation

Clockwise

Centisome Percentage:

20.62

Left Sequence End

956876

Right Sequence End

957964

Gene Sequence:

>1089 bp
ATGAATTCATGTGATTTTCGTGTTTTTCTGCAAGAGTTCGGTACAACGGTTCATTTGTCA
TTGCCTGGTAGCGTATCCGAGAAAGAACGACTGCTACTCAAGCTGCTGATGCAGGGAATG
TCTGTAACAGAAATATCACAGTACAGAAATCGCAGTGCAAAGACAATTTCACATCAAAAG
AAACAGCTCTTTGAGAAACTGGGGATTCAGAGCGATATTACTTTCTGGCGCGATATTTTC
TTTCAGTACAATCCGGAGATCATATCCGCCACGGGGAGTAATAGTCACAGATATATTAAT
GATAATCACTATCACCATATCGTCACGCCTGAAGCCATCAGTCTGGCGTTGGAAAACCAC
GAATTCAAACCGTGGATCCAACCGGTTTTCTGCGCGCAGACTGGCGTACTGACGGGCTGT
GAGGTGCTTGTCCGCTGGGAACATCCACAAACGGGAATTATCCCACCGGATCAGTTTATT
CCTCTGGCGGAGTCATCCGGTCTTATTGTCATAATGACCCGCCAACTGATGAAACAGACT
GCGGATATTCTGATGCCGGTAAAACATTTGCTGCCGGACAATTTCCATATTGGCATCAAC
GTCTCGGCGGGTTGTTTTTTGGCAGCGGGATTTGAAAAAGAGTGTCTGAACCTGGTTAAT
AAATTAGGTAACGATAAAATCAAGCTGGTTCTCGAGCTAACGGAACGTAACCCTATTCCG
GTAACGCCAGAAGCCAGAGCGATATTTGACAGCCTTCATCAGCACAACATTACCTTTGCG
CTGGATGACTTTGGTACGGGTTATGCGACCTATCGTTACTTGCAGGCGTTCCCGGTCGAT
TTTATTAAGATCGATAAGTCATTTGTGCAAATGGCGAGTGTCGACGAAATCTCCGGTCAT
ATTGTGGACAATATTGTCGAACTAGCGCGTAAGCCTGGTCTGAGTATCGTGGCGGAAGGG
GTAGAAACCCAGGAGCAGGCGGATTTAATGATCGGTAAAGGCGTTCACTTTTTGCAGGGC
TATTTGTACTCTCCGCCAGTACCGGGTAATAAATTTATCTCTGAATGGGTAATGAAAGCA
GGTGGTTGA

Protein Properties

Pfam Domain Function:

Aminotran_5 (PF00266 )

Protein Residues:

362

Protein Molecular Weight:

39783

Protein Theoretical pI:

PDB File:

1BJO

Signaling Regions:

None

Transmembrane Regions:

None

Protein Sequence:

>Phosphoserine aminotransferase
MAQIFNFSSGPAMLPAEVLKQAQQELRDWNGLGTSVMEVSHRGKEFIQVAEEAEKDFRDL
LNVPSNYKVLFCHGGGRGQFAAVPLNILGDKTTADYVDAGYWAASAIKEAKKYCTPNVFD
AKVTVDGLRAVKPMREWQLSDNAAYMHYCPNETIDGIAIDETPDFGADVVVAADFSSTIL
SRPIDVSRYGVIYAGAQKNIGPAGLTIVIVREDLLGKANIACPSILDYSILNDNGSMFNT
PPTFAWYLSGLVFKWLKANGGVAEMDKINQQKAELLYGVIDNSDFYRNDVAKANRSRMNV
PFQLADSALDKLFLEESFAAGLHALKGHRVVGGMRASIYNAMPLEGVKALTDFMVEFERR
HG

References

External Links:

Resource	Link
Uniprot ID:	P23721
Uniprot Name:	SERC_ECOLI
GenBank Gene ID:	AP009048
Genebank Protein ID:	85674458
PDB ID:	1BJO
Ecogene ID:	EG10946
Ecocyc:	EG10946
ColiBase:	b0907
Kegg Gene:	b0907
EchoBASE ID:	EB0939
CCDB:	SERC_ECOLI
BacMap:	16128874

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
Drewke, C., Klein, M., Clade, D., Arenz, A., Muller, R., Leistner, E. (1996). "4-O-phosphoryl-L-threonine, a substrate of the pdxC(serC) gene product involved in vitamin B6 biosynthesis." FEBS Lett 390:179-182. Pubmed: 8706854
Duncan, K., Coggins, J. R. (1986). "The serC-aro A operon of Escherichia coli. A mixed function operon encoding enzymes from two different amino acid biosynthetic pathways." Biochem J 234:49-57. Pubmed: 3518706
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
Hester, G., Stark, W., Moser, M., Kallen, J., Markovic-Housley, Z., Jansonius, J. N. (1999). "Crystal structure of phosphoserine aminotransferase from Escherichia coli at 2.3 A resolution: comparison of the unligated enzyme and a complex with alpha-methyl-l-glutamate." J Mol Biol 286:829-850. Pubmed: 10024454
Lam, H. M., Winkler, M. E. (1990). "Metabolic relationships between pyridoxine (vitamin B6) and serine biosynthesis in Escherichia coli K-12." J Bacteriol 172:6518-6528. Pubmed: 2121717
Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
van der Zel, A., Lam, H. M., Winkler, M. E. (1989). "Extensive homology between the Escherichia coli K-12 SerC(PdxF) aminotransferase and a protein encoded by a progesterone-induced mRNA in rabbit and human endometria." Nucleic Acids Res 17:8379. Pubmed: 2682527

Phosphoserine aminotransferase (P23721)