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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei43 – 431L-glutamateBy similarity
Binding sitei103 – 1031Pyridoxal phosphate
Binding sitei153 – 1531Pyridoxal phosphate
Binding sitei173 – 1731Pyridoxal phosphate
Binding sitei196 – 1961Pyridoxal phosphate

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 362361Phosphoserine aminotransferasePRO_0000150147Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei197 – 1971N6-(pyridoxal phosphate)lysine

Interactioni

Subunit structurei

Homodimer.3 Publications

Structurei

Secondary structure

1
362
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 123Combined sources
Helixi17 – 259Combined sources
Beta strandi27 – 304Combined sources
Beta strandi33 – 353Combined sources
Helixi37 – 393Combined sources
Helixi45 – 6117Combined sources
Beta strandi66 – 7510Combined sources
Helixi76 – 8813Combined sources
Beta strandi94 – 996Combined sources
Helixi102 – 11413Combined sources
Beta strandi117 – 1226Combined sources
Helixi124 – 1263Combined sources
Helixi134 – 1363Combined sources
Beta strandi143 – 15210Combined sources
Turni153 – 1564Combined sources
Beta strandi170 – 1734Combined sources
Turni175 – 1795Combined sources
Helixi185 – 1873Combined sources
Beta strandi189 – 1946Combined sources
Turni195 – 1995Combined sources
Beta strandi205 – 2106Combined sources
Helixi211 – 2133Combined sources
Beta strandi214 – 2163Combined sources
Helixi223 – 2253Combined sources
Helixi227 – 2326Combined sources
Turni233 – 2353Combined sources
Helixi242 – 25716Combined sources
Helixi260 – 28021Combined sources
Beta strandi285 – 2906Combined sources
Helixi292 – 2943Combined sources
Beta strandi297 – 3037Combined sources
Helixi307 – 31913Combined sources
Beta strandi322 – 3243Combined 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
1BT4X-ray2.30A4-362[»]
1W3UX-ray1.50A1-362[»]
2C0RX-ray1.20A/B2-362[»]
ProteinModelPortaliQ59196.
SMRiQ59196. Positions 2-362.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ59196.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni77 – 782Pyridoxal phosphate binding
Regioni238 – 2392Pyridoxal phosphate binding

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00160. SerC_aminotrans_5.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1BT4X-ray2.30A4-362[»]
1W3UX-ray1.50A1-362[»]
2C0RX-ray1.20A/B2-362[»]
ProteinModelPortaliQ59196.
SMRiQ59196. Positions 2-362.
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

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00160. SerC_aminotrans_5.
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...

Publicationsi

  1. "Phosphoserine aminotransferase from Bacillus circulans var. alkalophilus: purification, gene cloning and sequencing."
    Battchikova N., Holopainen M., Himanen J.-P., Korpela T.
    (In) Sannia G. (eds.); Proceedings of 9th meeting on vitamin B6 and carbonyl catalysis, pp.207-207, Dipt. Chimica Organica e Biologica, Napoli (1994)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 21783 / subsp. Alkalophilus.
  2. "Phosphoserine aminotransferase from Bacillus circulans subsp. alkalophilus: purification, gene cloning and sequencing."
    Battchikova N., Himanen J.-P., Ahjolahti M., Korpela T.
    Biochim. Biophys. Acta 1295:187-194(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, SUBUNIT, CATALYTIC ACTIVITY.
    Strain: ATCC 21783 / subsp. Alkalophilus.
  3. "Crystallization and preliminary X-ray analysis of phosphoserine aminotransferase from Bacillus circulans subsp. alkalophilus."
    Moser M., Mueller R., Battchikova N., Koivulehto M., Korpela T., Jansonius J.N.
    Protein Sci. 5:1426-1428(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
    Strain: ATCC 21783 / subsp. Alkalophilus.
  4. Hester G., Luong T.N., Moser M., Jansonius J.N.
    Submitted (SEP-1998) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT GLU-3 IN COMPLEX WITH PLP, COFACTOR.
    Strain: ATCC 21783 / subsp. Alkalophilus.
  5. "Effect of pH on the structure and stability of Bacillus circulans ssp. alkalophilus phosphoserine aminotransferase: thermodynamic and crystallographic studies."
    Kapetaniou E.G., Thanassoulas A., Dubnovitsky A.P., Nounesis G., Papageorgiou A.C.
    Proteins 63:742-753(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF MUTANT GLU-3 IN COMPLEX WITH PLP, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
    Strain: ATCC 21783 / subsp. Alkalophilus.

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: October 14, 2015
This is version 108 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.