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Protein

Phosphoserine aminotransferase

Gene

serC

Organism
Bacillus circulans
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.1 Publication

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'-phosphate2 PublicationsNote: Binds 1 pyridoxal phosphate per subunit.2 Publications

Kineticsi

  1. KM=1 mM for glutamate (at pH 7)1 Publication
  2. KM=0.2 mM for glutamate (at pH 9)1 Publication
  3. KM=0.1 mM for phosphohydroxypyruvate (at pH 7)1 Publication
  4. KM=0.09 mM for phosphohydroxypyruvate (at pH 9)1 Publication
  1. Vmax=6 nmol/min/mg enzyme for the reaction forming phosphoserine (at pH 7)1 Publication
  2. Vmax=10 nmol/min/mg enzyme for the reaction forming phosphoserine (at pH 9)1 Publication

pH dependencei

Optimum pH is 9.0. At pH 9.5, retains more 60% of its maximum activity. Inactive below pH 6.1 Publication

Temperature dependencei

Thermal denaturation midpoint (Tm) is 71 degrees Celsius at pH 6 and is lowered around 58 degrees Celsius at pH 8.5 and 10.1 Publication

Pathwayi: L-serine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-serine from 3-phospho-D-glycerate.
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), 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.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. Phosphoserine aminotransferase (serC)
  4. 4-hydroxythreonine-4-phosphate dehydrogenase (pdxA)
  5. no protein annotated in this organism
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 sitei43L-glutamateBy similarity1
Binding sitei103Pyridoxal phosphate1
Binding sitei153Pyridoxal phosphate1
Binding sitei173Pyridoxal phosphate1
Binding sitei196Pyridoxal phosphate1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Serine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi2.6.1.52. 649.
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
OrganismiBacillus circulans
Taxonomic identifieri1397 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001501472 – 362Phosphoserine aminotransferaseAdd BLAST361

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei197N6-(pyridoxal phosphate)lysine1

Interactioni

Subunit structurei

Homodimer.3 Publications

Structurei

Secondary structure

1362
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 12Combined sources3
Helixi17 – 25Combined sources9
Beta strandi27 – 30Combined sources4
Beta strandi33 – 35Combined sources3
Helixi37 – 39Combined sources3
Helixi45 – 61Combined sources17
Beta strandi66 – 75Combined sources10
Helixi76 – 88Combined sources13
Beta strandi94 – 99Combined sources6
Helixi102 – 114Combined sources13
Beta strandi117 – 122Combined sources6
Helixi124 – 126Combined sources3
Helixi134 – 136Combined sources3
Beta strandi143 – 152Combined sources10
Turni153 – 156Combined sources4
Beta strandi170 – 173Combined sources4
Turni175 – 179Combined sources5
Helixi185 – 187Combined sources3
Beta strandi189 – 194Combined sources6
Turni195 – 199Combined sources5
Beta strandi205 – 210Combined sources6
Helixi211 – 213Combined sources3
Beta strandi214 – 216Combined sources3
Helixi223 – 225Combined sources3
Helixi227 – 232Combined sources6
Turni233 – 235Combined sources3
Helixi242 – 257Combined sources16
Helixi260 – 280Combined sources21
Beta strandi285 – 290Combined sources6
Helixi292 – 294Combined sources3
Beta strandi297 – 303Combined sources7
Helixi307 – 319Combined sources13
Beta strandi322 – 324Combined sources3
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
1BT4X-ray2.30A4-362[»]
1W3UX-ray1.50A1-362[»]
2C0RX-ray1.20A/B2-362[»]
ProteinModelPortaliQ59196.
SMRiQ59196.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ59196.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni77 – 78Pyridoxal phosphate binding2
Regioni238 – 239Pyridoxal phosphate binding2

Sequence similaritiesi

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.

Q59196-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKRAYNFNA GPAALPLEVL ERAQAEFVDY QHTGMSIMEM SHRGAVYEAV
60 70 80 90 100
HNEAQARLLA LLGNPTGYKV LFIQGGASTQ FAMIPMNFLK EGQTANYVMT
110 120 130 140 150
GSWASKALKE AKLIGDTHVA ASSEASNYMT LPKLQEIQLQ DNAAYLHLTS
160 170 180 190 200
NETIEGAQFK AFPDTGSVPL IGDMSSDILS RPFDLNQFGL VYAGAQKNLG
210 220 230 240 250
PSGVTVVIVR EDLVAESPKH LPTMLRYDTY VKNNSLYNTP PSFGIYMVNE
260 270 280 290 300
VLKWIEERGG LEGVQQANRK KASLIYDAID QSGGFYRGCV DVDSRSDMNI
310 320 330 340 350
TFRLASEELE KEFVKASEQE GFVGLKGHRS VGGLRASIYN AVPYESCEAL
360
VQFMEHFKRS RG
Length:362
Mass (Da):39,924
Last modified:January 23, 2007 - v3
Checksum:i2D63C629C8DD269B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46432 Genomic DNA. Translation: CAA86558.2.
PIRiS71439.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46432 Genomic DNA. Translation: CAA86558.2.
PIRiS71439.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BT4X-ray2.30A4-362[»]
1W3UX-ray1.50A1-362[»]
2C0RX-ray1.20A/B2-362[»]
ProteinModelPortaliQ59196.
SMRiQ59196.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00135; UER00197.
UPA00244; UER00311.
BRENDAi2.6.1.52. 649.

Miscellaneous databases

EvolutionaryTraceiQ59196.

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_BACCI
AccessioniPrimary (citable) accession number: Q59196
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Significant conformational rearrangements are involved in response to pH changes.

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.