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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)DescriptionActionsGraphical viewLength
Binding sitei9L-glutamate1
Binding sitei42L-glutamate1
Binding sitei102Pyridoxal phosphate1
Binding sitei153Pyridoxal phosphate1
Binding sitei174Pyridoxal phosphate1
Binding sitei197Pyridoxal phosphate1

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001501672 – 362Phosphoserine aminotransferaseAdd BLAST361

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei198N6-(pyridoxal phosphate)lysine1

Proteomic databases

EPDiP23721.
PaxDbiP23721.
PRIDEiP23721.

2D gel databases

SWISS-2DPAGEP23721.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

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

Structurei

Secondary structure

1362
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 11Combined sources3
Helixi16 – 24Combined sources9
Beta strandi26 – 28Combined sources3
Helixi29 – 31Combined sources3
Beta strandi32 – 34Combined sources3
Helixi36 – 38Combined sources3
Helixi44 – 61Combined sources18
Beta strandi67 – 74Combined sources8
Helixi75 – 87Combined sources13
Beta strandi93 – 100Combined sources8
Helixi101 – 110Combined sources10
Turni111 – 113Combined sources3
Beta strandi114 – 120Combined sources7
Beta strandi122 – 125Combined sources4
Beta strandi128 – 131Combined sources4
Helixi134 – 136Combined sources3
Beta strandi146 – 148Combined sources3
Beta strandi150 – 152Combined sources3
Turni153 – 156Combined sources4
Beta strandi171 – 174Combined sources4
Turni176 – 180Combined sources5
Helixi186 – 188Combined sources3
Beta strandi190 – 195Combined sources6
Turni196 – 200Combined sources5
Beta strandi206 – 211Combined sources6
Helixi212 – 214Combined sources3
Helixi224 – 226Combined sources3
Helixi228 – 233Combined sources6
Turni234 – 236Combined sources3
Helixi243 – 258Combined sources16
Helixi261 – 282Combined sources22
Beta strandi284 – 287Combined sources4
Helixi292 – 294Combined sources3
Beta strandi297 – 306Combined sources10
Helixi307 – 309Combined sources3
Helixi310 – 319Combined sources10
Turni329 – 331Combined sources3
Beta strandi333 – 337Combined sources5
Helixi344 – 361Combined sources18

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP23721.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni76 – 77Pyridoxal phosphate binding2
Regioni239 – 240Pyridoxal phosphate binding2

Sequence similaritiesi

Phylogenomic databases

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

Family and domain databases

CDDicd00611. PSAT_like. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti293A → R no nucleotide entry (PubMed:3518706).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BJNX-ray2.30A/B3-362[»]
1BJOX-ray2.80A/B3-362[»]
ProteinModelPortaliP23721.
SMRiP23721.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260006. 18 interactors.
DIPiDIP-2896N.
IntActiP23721. 9 interactors.
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

CDDicd00611. PSAT_like. 1 hit.
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: November 30, 2016
This is version 159 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.