UniProtKB - P0A9T0 (SERA_ECOLI)
Protein
D-3-phosphoglycerate dehydrogenase
Gene
serA
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.1 Publication
Catalytic activityi
Activity regulationi
Displays feedback inhibition by L-serine. Inhibited by glycine.1 Publication
Kineticsi
kcat is 0.55 sec(-1) for 3-phospho-D-glycerate oxidation. kcat is 27.8 sec(-1) for 3-phosphonooxypyruvate reduction. kcat is 33.3 sec(-1) for 2-oxoglutarate reduction. kcat is 0.71 sec(-1) for (R)-2-hydroxyglutarate oxidation. kcat is 0.25 sec(-1) for (S)-2-hydroxyglutarate oxidation.1 Publication
- KM=1.2 mM for 3-phospho-D-glycerate1 Publication
- KM=3.2 µM for 3-phosphonooxypyruvate1 Publication
- KM=88 µM for 2-oxoglutarate1 Publication
- KM=0.37 mM for (R)-2-hydroxyglutarate1 Publication
- KM=2.9 mM for (S)-2-hydroxyglutarate1 Publication
- Vmax=183 nmol/min/mg enzyme for 3-phospho-D-glycerate oxidation1 Publication
- Vmax=9.27 µmol/min/mg enzyme for 3-phosphonooxypyruvate reduction1 Publication
- Vmax=11.1 µmol/min/mg enzyme for 2-oxoglutarate reduction1 Publication
- Vmax=237 nmol/min/mg enzyme for (R)-2-hydroxyglutarate oxidation1 Publication
- Vmax=83.3 nmol/min/mg enzyme for (S)-2-hydroxyglutarate oxidation1 Publication
pH dependencei
Optimum pH is 8.5 for the reductase activities and 9.0 for the dehydrogenase activities.1 Publication
: L-serine biosynthesis Pathwayi
This protein is involved in step 1 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:
- 2-oxoglutarate reductase (FAZ83_05975), D-3-phosphoglycerate dehydrogenase (serA)
- Phosphoserine aminotransferase (serC), Phosphoserine aminotransferase (serC)
- O-phosphoserine phosphohydrolase (FAZ83_13125), Phosphoserine phosphatase (serB)
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.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 181 | NAD1 Publication | 1 | |
Active sitei | 240 | 1 | ||
Binding sitei | 264 | NAD1 Publication | 1 | |
Active sitei | 269 | 1 | ||
Active sitei | 292 | Proton donor | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 161 – 162 | NAD1 Publication | 2 | |
Nucleotide bindingi | 238 – 240 | NAD1 Publication | 3 | |
Nucleotide bindingi | 292 – 295 | NAD1 Publication | 4 |
GO - Molecular functioni
- 2-hydroxyglutarate dehydrogenase activity Source: EcoCyc
- glyoxylate reductase (NADP+) activity Source: GO_Central
- hydroxypyruvate reductase activity Source: GO_Central
- identical protein binding Source: EcoCyc
- NAD+ binding Source: EcoCyc
- NADH binding Source: EcoCyc
- phosphoglycerate dehydrogenase activity Source: EcoCyc
- serine binding Source: EcoCyc
GO - Biological processi
- L-serine biosynthetic process Source: EcoCyc
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Amino-acid biosynthesis, Serine biosynthesis |
Ligand | NAD |
Enzyme and pathway databases
BioCyci | EcoCyc:PGLYCDEHYDROG-MONOMER MetaCyc:PGLYCDEHYDROG-MONOMER |
BRENDAi | 1.1.1.95, 2026 |
SABIO-RKi | P0A9T0 |
UniPathwayi | UPA00135;UER00196 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:serA Ordered Locus Names:b2913, JW2880 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000075999 | 2 – 410 | D-3-phosphoglycerate dehydrogenaseAdd BLAST | 409 |
Proteomic databases
jPOSTi | P0A9T0 |
PaxDbi | P0A9T0 |
PRIDEi | P0A9T0 |
Interactioni
Subunit structurei
Homotetramer.
GO - Molecular functioni
- identical protein binding Source: EcoCyc
Protein-protein interaction databases
BioGRIDi | 4261173, 27 interactors |
DIPi | DIP-10851N |
IntActi | P0A9T0, 3 interactors |
STRINGi | 511145.b2913 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0A9T0 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0A9T0 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 339 – 410 | ACTPROSITE-ProRule annotationAdd BLAST | 72 |
Sequence similaritiesi
Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.Curated
Phylogenomic databases
eggNOGi | COG0111, Bacteria |
HOGENOMi | CLU_019796_9_2_6 |
InParanoidi | P0A9T0 |
PhylomeDBi | P0A9T0 |
Family and domain databases
InterProi | View protein in InterPro IPR002912, ACT_dom IPR006139, D-isomer_2_OHA_DH_cat_dom IPR029753, D-isomer_DH_CS IPR029752, D-isomer_DH_CS1 IPR006140, D-isomer_DH_NAD-bd IPR036291, NAD(P)-bd_dom_sf |
Pfami | View protein in Pfam PF00389, 2-Hacid_dh, 1 hit PF02826, 2-Hacid_dh_C, 1 hit PF01842, ACT, 1 hit |
SUPFAMi | SSF51735, SSF51735, 1 hit |
PROSITEi | View protein in PROSITE PS51671, ACT, 1 hit PS00065, D_2_HYDROXYACID_DH_1, 1 hit PS00670, D_2_HYDROXYACID_DH_2, 1 hit PS00671, D_2_HYDROXYACID_DH_3, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P0A9T0-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAKVSLEKDK IKFLLVEGVH QKALESLRAA GYTNIEFHKG ALDDEQLKES
60 70 80 90 100
IRDAHFIGLR SRTHLTEDVI NAAEKLVAIG CFCIGTNQVD LDAAAKRGIP
110 120 130 140 150
VFNAPFSNTR SVAELVIGEL LLLLRGVPEA NAKAHRGVWN KLAAGSFEAR
160 170 180 190 200
GKKLGIIGYG HIGTQLGILA ESLGMYVYFY DIENKLPLGN ATQVQHLSDL
210 220 230 240 250
LNMSDVVSLH VPENPSTKNM MGAKEISLMK PGSLLINASR GTVVDIPALC
260 270 280 290 300
DALASKHLAG AAIDVFPTEP ATNSDPFTSP LCEFDNVLLT PHIGGSTQEA
310 320 330 340 350
QENIGLEVAG KLIKYSDNGS TLSAVNFPEV SLPLHGGRRL MHIHENRPGV
360 370 380 390 400
LTALNKIFAE QGVNIAAQYL QTSAQMGYVV IDIEADEDVA EKALQAMKAI
410
PGTIRARLLY
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L29397 Genomic DNA Translation: AAA24625.1 U28377 Genomic DNA Translation: AAA69080.1 U00096 Genomic DNA Translation: AAC75950.1 AP009048 Genomic DNA Translation: BAE76977.1 X66836 Genomic DNA Translation: CAA47308.1 M64630 Genomic DNA Translation: AAA73016.1 |
PIRi | A25200, DEECPG |
RefSeqi | NP_417388.1, NC_000913.3 WP_001151604.1, NZ_STEB01000001.1 |
Genome annotation databases
EnsemblBacteriai | AAC75950; AAC75950; b2913 BAE76977; BAE76977; BAE76977 |
GeneIDi | 58460576 945258 |
KEGGi | ecj:JW2880 eco:b2913 |
PATRICi | fig|1411691.4.peg.3820 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L29397 Genomic DNA Translation: AAA24625.1 U28377 Genomic DNA Translation: AAA69080.1 U00096 Genomic DNA Translation: AAC75950.1 AP009048 Genomic DNA Translation: BAE76977.1 X66836 Genomic DNA Translation: CAA47308.1 M64630 Genomic DNA Translation: AAA73016.1 |
PIRi | A25200, DEECPG |
RefSeqi | NP_417388.1, NC_000913.3 WP_001151604.1, NZ_STEB01000001.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1PSD | X-ray | 2.75 | A/B | 2-410 | [»] | |
1SC6 | X-ray | 2.09 | A/B/C/D | 7-410 | [»] | |
1YBA | X-ray | 2.24 | A/B/C/D | 1-410 | [»] | |
2P9C | X-ray | 2.46 | A/B | 1-410 | [»] | |
2P9E | X-ray | 2.60 | A/B/C/D | 1-410 | [»] | |
2P9G | X-ray | 2.80 | A/B | 1-410 | [»] | |
2PA3 | X-ray | 2.74 | A | 1-410 | [»] | |
SMRi | P0A9T0 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4261173, 27 interactors |
DIPi | DIP-10851N |
IntActi | P0A9T0, 3 interactors |
STRINGi | 511145.b2913 |
Proteomic databases
jPOSTi | P0A9T0 |
PaxDbi | P0A9T0 |
PRIDEi | P0A9T0 |
Genome annotation databases
EnsemblBacteriai | AAC75950; AAC75950; b2913 BAE76977; BAE76977; BAE76977 |
GeneIDi | 58460576 945258 |
KEGGi | ecj:JW2880 eco:b2913 |
PATRICi | fig|1411691.4.peg.3820 |
Organism-specific databases
EchoBASEi | EB0937 |
Phylogenomic databases
eggNOGi | COG0111, Bacteria |
HOGENOMi | CLU_019796_9_2_6 |
InParanoidi | P0A9T0 |
PhylomeDBi | P0A9T0 |
Enzyme and pathway databases
UniPathwayi | UPA00135;UER00196 |
BioCyci | EcoCyc:PGLYCDEHYDROG-MONOMER MetaCyc:PGLYCDEHYDROG-MONOMER |
BRENDAi | 1.1.1.95, 2026 |
SABIO-RKi | P0A9T0 |
Miscellaneous databases
EvolutionaryTracei | P0A9T0 |
PROi | PR:P0A9T0 |
Family and domain databases
InterProi | View protein in InterPro IPR002912, ACT_dom IPR006139, D-isomer_2_OHA_DH_cat_dom IPR029753, D-isomer_DH_CS IPR029752, D-isomer_DH_CS1 IPR006140, D-isomer_DH_NAD-bd IPR036291, NAD(P)-bd_dom_sf |
Pfami | View protein in Pfam PF00389, 2-Hacid_dh, 1 hit PF02826, 2-Hacid_dh_C, 1 hit PF01842, ACT, 1 hit |
SUPFAMi | SSF51735, SSF51735, 1 hit |
PROSITEi | View protein in PROSITE PS51671, ACT, 1 hit PS00065, D_2_HYDROXYACID_DH_1, 1 hit PS00670, D_2_HYDROXYACID_DH_2, 1 hit PS00671, D_2_HYDROXYACID_DH_3, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | SERA_ECOLI | |
Accessioni | P0A9T0Primary (citable) accession number: P0A9T0 Secondary accession number(s): P08328, Q2M9S9, Q47633 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1988 |
Last sequence update: | January 23, 2007 | |
Last modified: | April 7, 2021 | |
This is version 138 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families