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Protein

Phosphoserine aminotransferase

Gene

serC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate.1 Publication
4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate.1 Publication

Cofactori

pyridoxal 5'-phosphate1 PublicationNote: Binds 1 pyridoxal phosphate per subunit.1 Publication

Kineticsi

No activity could be observed with non-phosphorylated substrates.

  1. KM=15 µM for 3-phosphonooxypyruvate1 Publication
  2. KM=17 µM for O(3)-phospho-L-serine1 Publication
  3. KM=110 µM for 4-phosphonooxy-L-threonine1 Publication
  1. Vmax=45 nmol/sec/mg enzyme with 3-phosphonooxypyruvate as substrate1 Publication
  2. Vmax=9.9 nmol/sec/mg enzyme with O(3)-phospho-L-serine as substrate1 Publication
  3. Vmax=3.8 nmol/sec/mg enzyme with 4-phosphonooxy-L-threonine as substrate1 Publication

pH dependencei

Optimum pH is 7.5-8.8.1 Publication

Pathwayi: L-serine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-serine from 3-phospho-D-glycerate.1 Publication
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. D-3-phosphoglycerate dehydrogenase (serA)
  2. Phosphoserine aminotransferase (serC)
  3. Phosphoserine phosphatase (serB)
This subpathway is part of the pathway L-serine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-serine from 3-phospho-D-glycerate, the pathway L-serine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: pyridoxine 5'-phosphate biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes pyridoxine 5'-phosphate from D-erythrose 4-phosphate.1 Publication
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. D-erythrose-4-phosphate dehydrogenase (epd)
  2. Erythronate-4-phosphate dehydrogenase (pdxB)
  3. Phosphoserine aminotransferase (serC)
  4. 4-hydroxythreonine-4-phosphate dehydrogenase (pdxA)
  5. Pyridoxine 5'-phosphate synthase (pdxJ)
This subpathway is part of the pathway pyridoxine 5'-phosphate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyridoxine 5'-phosphate from D-erythrose 4-phosphate, the pathway pyridoxine 5'-phosphate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91L-glutamate
Binding sitei42 – 421L-glutamate
Binding sitei102 – 1021Pyridoxal phosphate
Binding sitei153 – 1531Pyridoxal phosphate
Binding sitei174 – 1741Pyridoxal phosphate
Binding sitei197 – 1971Pyridoxal phosphate

GO - Molecular functioni

  • O-phospho-L-serine:2-oxoglutarate aminotransferase activity Source: EcoCyc
  • pyridoxal phosphate binding Source: EcoCyc

GO - Biological processi

  • L-serine biosynthetic process Source: EcoCyc
  • L-serine metabolic process Source: UniProtKB
  • lysine biosynthetic process via diaminopimelate and N-succinyl-2-amino-6-ketopimelate Source: EcoCyc
  • pyridoxal phosphate biosynthetic process Source: EcoCyc
  • pyridoxine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Pyridoxine biosynthesis, Serine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:PSERTRANSAM-MONOMER.
ECOL316407:JW0890-MONOMER.
MetaCyc:PSERTRANSAM-MONOMER.
SABIO-RKP23721.
UniPathwayiUPA00135; UER00197.
UPA00244; UER00311.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoserine aminotransferase (EC:2.6.1.52)
Alternative name(s):
Phosphohydroxythreonine aminotransferase
Short name:
PSAT
Gene namesi
Name:serC
Synonyms:pdxC, pdxF
Ordered Locus Names:b0907, JW0890
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10946. serC.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 362361Phosphoserine aminotransferasePRO_0000150167Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei198 – 1981N6-(pyridoxal phosphate)lysine

Proteomic databases

EPDiP23721.
PaxDbiP23721.
PRIDEiP23721.

2D gel databases

SWISS-2DPAGEP23721.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4260006. 18 interactions.
DIPiDIP-2896N.
IntActiP23721. 9 interactions.
MINTiMINT-1249760.
STRINGi511145.b0907.

Structurei

Secondary structure

1
362
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 113Combined sources
Helixi16 – 249Combined sources
Beta strandi26 – 283Combined sources
Helixi29 – 313Combined sources
Beta strandi32 – 343Combined sources
Helixi36 – 383Combined sources
Helixi44 – 6118Combined sources
Beta strandi67 – 748Combined sources
Helixi75 – 8713Combined sources
Beta strandi93 – 1008Combined sources
Helixi101 – 11010Combined sources
Turni111 – 1133Combined sources
Beta strandi114 – 1207Combined sources
Beta strandi122 – 1254Combined sources
Beta strandi128 – 1314Combined sources
Helixi134 – 1363Combined sources
Beta strandi146 – 1483Combined sources
Beta strandi150 – 1523Combined sources
Turni153 – 1564Combined sources
Beta strandi171 – 1744Combined sources
Turni176 – 1805Combined sources
Helixi186 – 1883Combined sources
Beta strandi190 – 1956Combined sources
Turni196 – 2005Combined sources
Beta strandi206 – 2116Combined sources
Helixi212 – 2143Combined sources
Helixi224 – 2263Combined sources
Helixi228 – 2336Combined sources
Turni234 – 2363Combined sources
Helixi243 – 25816Combined sources
Helixi261 – 28222Combined sources
Beta strandi284 – 2874Combined sources
Helixi292 – 2943Combined sources
Beta strandi297 – 30610Combined sources
Helixi307 – 3093Combined sources
Helixi310 – 31910Combined sources
Turni329 – 3313Combined sources
Beta strandi333 – 3375Combined sources
Helixi344 – 36118Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BJNX-ray2.30A/B3-362[»]
1BJOX-ray2.80A/B3-362[»]
ProteinModelPortaliP23721.
SMRiP23721. Positions 3-362.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23721.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni76 – 772Pyridoxal phosphate binding
Regioni239 – 2402Pyridoxal phosphate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107QM1. Bacteria.
COG1932. LUCA.
HOGENOMiHOG000088965.
InParanoidiP23721.
KOiK00831.
OMAiGAQKNMG.
PhylomeDBiP23721.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00160. SerC_aminotrans_5. 1 hit.
InterProiIPR000192. Aminotrans_V_dom.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR022278. Pser_aminoTfrase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF000525. SerC. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01364. serC_1. 1 hit.
PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23721-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQIFNFSSG PAMLPAEVLK QAQQELRDWN GLGTSVMEVS HRGKEFIQVA
60 70 80 90 100
EEAEKDFRDL LNVPSNYKVL FCHGGGRGQF AAVPLNILGD KTTADYVDAG
110 120 130 140 150
YWAASAIKEA KKYCTPNVFD AKVTVDGLRA VKPMREWQLS DNAAYMHYCP
160 170 180 190 200
NETIDGIAID ETPDFGADVV VAADFSSTIL SRPIDVSRYG VIYAGAQKNI
210 220 230 240 250
GPAGLTIVIV REDLLGKANI ACPSILDYSI LNDNGSMFNT PPTFAWYLSG
260 270 280 290 300
LVFKWLKANG GVAEMDKINQ QKAELLYGVI DNSDFYRNDV AKANRSRMNV
310 320 330 340 350
PFQLADSALD KLFLEESFAA GLHALKGHRV VGGMRASIYN AMPLEGVKAL
360
TDFMVEFERR HG
Length:362
Mass (Da):39,783
Last modified:January 23, 2007 - v4
Checksum:iF6A58CBF9FA22BC9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti293 – 2931A → R no nucleotide entry (PubMed:3518706).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC73993.1.
AP009048 Genomic DNA. Translation: BAA35642.1.
PIRiB64830.
RefSeqiNP_415427.1. NC_000913.3.
WP_000057138.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73993; AAC73993; b0907.
BAA35642; BAA35642; BAA35642.
GeneIDi945527.
KEGGiecj:JW0890.
eco:b0907.
PATRICi32117027. VBIEscCol129921_0938.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC73993.1.
AP009048 Genomic DNA. Translation: BAA35642.1.
PIRiB64830.
RefSeqiNP_415427.1. NC_000913.3.
WP_000057138.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BJNX-ray2.30A/B3-362[»]
1BJOX-ray2.80A/B3-362[»]
ProteinModelPortaliP23721.
SMRiP23721. Positions 3-362.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260006. 18 interactions.
DIPiDIP-2896N.
IntActiP23721. 9 interactions.
MINTiMINT-1249760.
STRINGi511145.b0907.

2D gel databases

SWISS-2DPAGEP23721.

Proteomic databases

EPDiP23721.
PaxDbiP23721.
PRIDEiP23721.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73993; AAC73993; b0907.
BAA35642; BAA35642; BAA35642.
GeneIDi945527.
KEGGiecj:JW0890.
eco:b0907.
PATRICi32117027. VBIEscCol129921_0938.

Organism-specific databases

EchoBASEiEB0939.
EcoGeneiEG10946. serC.

Phylogenomic databases

eggNOGiENOG4107QM1. Bacteria.
COG1932. LUCA.
HOGENOMiHOG000088965.
InParanoidiP23721.
KOiK00831.
OMAiGAQKNMG.
PhylomeDBiP23721.

Enzyme and pathway databases

UniPathwayiUPA00135; UER00197.
UPA00244; UER00311.
BioCyciEcoCyc:PSERTRANSAM-MONOMER.
ECOL316407:JW0890-MONOMER.
MetaCyc:PSERTRANSAM-MONOMER.
SABIO-RKP23721.

Miscellaneous databases

EvolutionaryTraceiP23721.
PROiP23721.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00160. SerC_aminotrans_5. 1 hit.
InterProiIPR000192. Aminotrans_V_dom.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR022278. Pser_aminoTfrase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF000525. SerC. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01364. serC_1. 1 hit.
PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSERC_ECOLI
AccessioniPrimary (citable) accession number: P23721
Secondary accession number(s): P78266
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 157 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.