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Protein

Phosphoserine aminotransferase

Gene

serC

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 3 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.UniRule annotation

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphateUniRule annotationNote: Binds 1 pyridoxal phosphate per subunit.UniRule annotation

Pathwayi: L-serine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-serine from 3-phospho-D-glycerate.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Phosphoserine aminotransferase (serC)
  3. no protein annotated in this organism
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.UniRule annotation
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 1 (pdxA1), 4-hydroxythreonine-4-phosphate dehydrogenase 2 (pdxA2)
  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-glutamateUniRule annotation1
Binding sitei42L-glutamateUniRule annotation1
Binding sitei102Pyridoxal phosphateUniRule annotation1
Binding sitei153Pyridoxal phosphateUniRule annotation1
Binding sitei174Pyridoxal phosphateUniRule annotation1
Binding sitei197Pyridoxal phosphateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

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

UniPathwayiUPA00135; UER00197.
UPA00244; UER00311.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoserine aminotransferaseUniRule annotation (EC:2.6.1.52UniRule annotation)
Alternative name(s):
Phosphohydroxythreonine aminotransferaseUniRule annotation
Short name:
PSATUniRule annotation
Gene namesi
Name:serCUniRule annotation
Ordered Locus Names:STM0977
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001502071 – 362Phosphoserine aminotransferaseAdd BLAST362

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei198N6-(pyridoxal phosphate)lysineUniRule annotation1

Proteomic databases

PaxDbiP55900.
PRIDEiP55900.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi99287.STM0977.

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 – 22Combined sources7
Helixi51 – 61Combined sources11
Beta strandi67 – 74Combined sources8
Helixi78 – 87Combined sources10
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 strandi205 – 211Combined sources7
Helixi212 – 214Combined sources3
Helixi224 – 226Combined sources3
Helixi228 – 233Combined sources6
Helixi245 – 258Combined sources14
Helixi261 – 281Combined sources21
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
3QM2X-ray2.25A/B1-362[»]
ProteinModelPortaliP55900.
SMRiP55900.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55900.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni76 – 77Pyridoxal phosphate bindingUniRule annotation2
Regioni239 – 240Pyridoxal phosphate bindingUniRule annotation2

Sequence similaritiesi

Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107QM1. Bacteria.
COG1932. LUCA.
HOGENOMiHOG000088965.
KOiK00831.
OMAiGAQKNMG.
PhylomeDBiP55900.

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.

P55900-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQVFNFSSG PAMLPAEVLK LAQQELCDWH GLGTSVMEIS HRGKEFIQVA
60 70 80 90 100
EEAEQDFRDL LNIPSNYKVL FCHGGGRGQF AGVPLNLLGD KTTADYVDAG
110 120 130 140 150
YWAASAIKEA KKYCAPQIID AKITVDGKRA VKPMREWQLS DNAAYLHYCP
160 170 180 190 200
NETIDGIAID ETPDFGPEVV VTADFSSTIL SAPLDVSRYG VIYAGAQKNI
210 220 230 240 250
GPAGLTLVIV REDLLGKAHE SCPSILDYTV LNDNDSMFNT PPTFAWYLSG
260 270 280 290 300
LVFKWLKAQG GVAAMHKINQ QKAELLYGVI DNSDFYRNDV AQANRSRMNV
310 320 330 340 350
PFQLADNTLD KVFLEESFAA GLHALKGHRV VGGMRASIYN AMPIEGVKAL
360
TDFMIDFERR HG
Length:362
Mass (Da):39,832
Last modified:January 23, 2002 - v2
Checksum:i802C026A8B4CE2C3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti47I → M in CAA71381 (Ref. 1) Curated1
Sequence conflicti79Q → T in CAA71381 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10355 Genomic DNA. Translation: CAA71381.1.
AE006468 Genomic DNA. Translation: AAL19911.1.
RefSeqiNP_459952.1. NC_003197.1.
WP_000079584.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL19911; AAL19911; STM0977.
GeneIDi1252495.
KEGGistm:STM0977.
PATRICi32380367. VBISalEnt20916_1030.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10355 Genomic DNA. Translation: CAA71381.1.
AE006468 Genomic DNA. Translation: AAL19911.1.
RefSeqiNP_459952.1. NC_003197.1.
WP_000079584.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QM2X-ray2.25A/B1-362[»]
ProteinModelPortaliP55900.
SMRiP55900.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM0977.

Proteomic databases

PaxDbiP55900.
PRIDEiP55900.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL19911; AAL19911; STM0977.
GeneIDi1252495.
KEGGistm:STM0977.
PATRICi32380367. VBISalEnt20916_1030.

Phylogenomic databases

eggNOGiENOG4107QM1. Bacteria.
COG1932. LUCA.
HOGENOMiHOG000088965.
KOiK00831.
OMAiGAQKNMG.
PhylomeDBiP55900.

Enzyme and pathway databases

UniPathwayiUPA00135; UER00197.
UPA00244; UER00311.

Miscellaneous databases

EvolutionaryTraceiP55900.

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_SALTY
AccessioniPrimary (citable) accession number: P55900
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2002
Last modified: November 30, 2016
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.