RegulonDB RegulonDB 11.1: Gene Form
   

serC gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

aroA serC ycaP CRP Lrp anti-terminator anti-anti-terminator terminator anti-terminator anti-anti-terminator TSS_1177 (cluster) TSS_1177 (cluster) TSS_1176 TSS_1176 TSS_1175 TSS_1175 TSS_1174 TSS_1174 TSS_1173 TSS_1173 TSS_1172 TSS_1172 serCp1 serCp1 TSS_1171 TSS_1171 serCp2 serCp2

Gene      
Name: serC    Texpresso search in the literature
Synonym(s): ECK0898, EG10946, b0907, pdxC, pdxF
Genome position(nucleotides): 957653 --> 958741
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 50.14
External database links:  
ASAP:
 ABE-0003093
CGSC:
 171
ECHOBASE:
 EB0939
ECOLIHUB:
 serC
MIM:
 610992
MIM:
 616038
OU-MICROARRAY:
 b0907
STRING:
 511145.b0907
COLOMBOS: serC


Product      
Name: phosphoserine/phosphohydroxythreonine aminotransferase
Synonym(s): PdxC, PdxF, SerC
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 39.783
Isoelectric point: 5.258
Motif(s):
 
Type Positions Sequence Comment
2 -> 362 AQIFNFSSGPAMLPAEVLKQAQQELRDWNGLGTSVMEVSHRGKEFIQVAEEAEKDFRDLLNVPSNYKVLFCHGGGRGQFAAVPLNILGDKTTADYVDAGYWAASAIKEAKKYCTPNVFDAKVTVDGLRAVKPMREWQLSDNAAYMHYCPNETIDGIAIDETPDFGADVVVAADFSSTILSRPIDVSRYGVIYAGAQKNIGPAGLTIVIVREDLLGKANIACPSILDYSILNDNGSMFNTPPTFAWYLSGLVFKWLKANGGVAEMDKINQQKAELLYGVIDNSDFYRNDVAKANRSRMNVPFQLADSALDKLFLEESFAAGLHALKGHRVVGGMRASIYNAMPLEGVKALTDFMVEFERRHG UniProt: Phosphoserine aminotransferase.
4 -> 350 IFNFSSGPAMLPAEVLKQAQQELRDWNGLGTSVMEVSHRGKEFIQVAEEAEKDFRDLLNVPSNYKVLFCHGGGRGQFAAVPLNILGDKTTADYVDAGYWAASAIKEAKKYCTPNVFDAKVTVDGLRAVKPMREWQLSDNAAYMHYCPNETIDGIAIDETPDFGADVVVAADFSSTILSRPIDVSRYGVIYAGAQKNIGPAGLTIVIVREDLLGKANIACPSILDYSILNDNGSMFNTPPTFAWYLSGLVFKWLKANGGVAEMDKINQQKAELLYGVIDNSDFYRNDVAKANRSRMNVPFQLADSALDKLFLEESFAAGLHALKGHRVVGGMRASIYNAMPLEGVKAL
76 -> 77 GR UniProt: Pyridoxal phosphate binding; Sequence Annotation Type: region of interest.
239 -> 240 NT UniProt: Pyridoxal phosphate binding; Sequence Annotation Type: region of interest.
293 -> 293 A UniProt: In Ref. 1; no nucleotide entry..

 
Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.5 - biosynthesis of building blocks --> 1.5.1 - amino acids --> 1.5.1.11 - serine
Gene Ontology Terms (GO)  
cellular_component GO:0005737 - cytoplasm
GO:0005829 - cytosol
molecular_function GO:0003824 - catalytic activity
GO:0005515 - protein binding
GO:0016740 - transferase activity
GO:0008483 - transaminase activity
GO:0004648 - O-phospho-L-serine:2-oxoglutarate aminotransferase activity
GO:0030170 - pyridoxal phosphate binding
GO:0042803 - protein homodimerization activity
biological_process GO:0006563 - L-serine metabolic process
GO:0006564 - L-serine biosynthetic process
GO:0008615 - pyridoxine biosynthetic process
GO:0008652 - cellular amino acid biosynthetic process
GO:0042823 - pyridoxal phosphate biosynthetic process
GO:0033359 - lysine biosynthetic process via diaminopimelate and N-succinyl-2-amino-6-ketopimelate
Note(s): Note(s): ...[more].
Reference(s): [1] Grant GA. 2018
[2] Gu P., et al., 2014
[3] Ivancic T., et al., 2013
[4] Mundhada H., et al., 2016
[5] Rohweder B., et al., 2019
[6] Smallbone K., et al., 2013
[7] Wintermute EH., et al., 2010
[8] Zhang Y., et al., 2019
External database links:  
ALPHAFOLD:
 P23721
DIP:
 DIP-2896N
ECOCYC:
 PSERTRANSAM-MONOMER
ECOLIWIKI:
 b0907
INTERPRO:
 IPR022278
INTERPRO:
 IPR015424
INTERPRO:
 IPR020578
INTERPRO:
 IPR015422
INTERPRO:
 IPR000192
INTERPRO:
 IPR015421
MODBASE:
 P23721
PANTHER:
 PTHR43247
PDB:
 1BJN
PDB:
 1BJO
PFAM:
 PF00266
PRIDE:
 P23721
PROSITE:
 PS00595
REFSEQ:
 NP_415427
SMR:
 P23721
UNIPROT:
 P23721


Operon      
Name: serC-aroA         
Operon arrangement:
Transcription unit        Promoter
serC
serC
serC-aroA


Transcriptional Regulation      
Display Regulation             
Activated by: Lrp
Repressed by: CRP


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter TSS_1171 957585 forward nd [RS-EPT-CBR] [9]
  promoter TSS_1172 957945 forward nd [RS-EPT-CBR] [9]
  promoter TSS_1173 958104 forward nd [RS-EPT-CBR] [9]
  promoter TSS_1174 958585 forward nd [RS-EPT-CBR] [9]
  promoter TSS_1175 958602 forward nd [RS-EPT-CBR] [9]
  promoter TSS_1176 958749 forward nd [RS-EPT-CBR] [9]
  promoter TSS_1177 (cluster) 958751 forward nd [RS-EPT-CBR] [9]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates


Reference(s)    

 [1] Grant GA., 2018, Elucidation of a Self-Sustaining Cycle in Escherichia coli l-Serine Biosynthesis That Results in the Conservation of the Coenzyme, NAD+., Biochemistry 57(11):1798-1806

 [2] Gu P., Yang F., Su T., Li F., Li Y., Qi Q., 2014, Construction of an L-serine producing Escherichia coli via metabolic engineering., J Ind Microbiol Biotechnol 41(9):1443-50

 [3] Ivancic T., Jamnik P., Stopar D., 2013, Cold shock CspA and CspB protein production during periodic temperature cycling in Escherichia coli., BMC Res Notes 6:248

 [4] Mundhada H., Schneider K., Christensen HB., Nielsen AT., 2016, Engineering of high yield production of L-serine in Escherichia coli., Biotechnol Bioeng 113(4):807-16

 [5] Rohweder B., Lehmann G., Eichner N., Polen T., Rajendran C., Ruperti F., Linde M., Treiber T., Jung O., Dettmer K., Meister G., Bott M., Gronwald W., Sterner R., 2019, Library Selection with a Randomized Repertoire of (βα)8 -Barrel Enzymes Results in Unexpected Induction of Gene Expression., Biochemistry 58(41):4207-4217

 [6] Smallbone K., Stanford NJ., 2013, Kinetic modeling of metabolic pathways: application to serine biosynthesis., Methods Mol Biol 985:113-21

 [7] Wintermute EH., Silver PA., 2010, Emergent cooperation in microbial metabolism., Mol Syst Biol 6:407

 [8] Zhang Y., Ma C., Dischert W., Soucaille P., Zeng AP., 2019, Engineering of Phosphoserine Aminotransferase Increases the Conversion of l-Homoserine to 4-Hydroxy-2-ketobutyrate in a Glycerol-Independent Pathway of 1,3-Propanediol Production from Glucose., Biotechnol J 14(9):e1900003

 [9] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.

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