Cysteine synthase A (P0ABK5)

Identification
Name:Cysteine synthase A
Synonyms:
  • CSase A
  • O-acetylserine (thiol)-lyase A
  • OAS-TL A
  • O-acetylserine sulfhydrylase A
  • Sulfate starvation-induced protein 5
  • SSI5
Gene Name:cysK
Enzyme Class:
Biological Properties
General Function:Involved in cysteine biosynthetic process from serine
Specific Function:O(3)-acetyl-L-serine + H(2)S = L-cysteine + acetate
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0O-Acetylserine + 1.0Hydrogen sulfide ↔ 1.0Acetic acid + 1.0L-Cysteine + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0O-Acetylserine + 1.0Hydrogen sulfide ↔ 1.0L-Cysteine + 1.0Acetic acid
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0O-Acetylserine + 1.0Hydrogen selenide ↔ 1.0Selenocysteine + 1.0Acetic acid
ReactionCard
1.0Thumb+1.0Thumb+1.0Thioredoxin+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thioredoxin disulfide+1.0Thumb
1.0O-Acetylserine + 1.0Thiosulfate + 1.0Thioredoxin + 1.0Hydrogen ion ↔ 1.0L-Cysteine + 1.0Sulfite + 1.0Thioredoxin disulfide + 1.0Acetic acid
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0O-Acetylserine + 1.0Hydrogen sulfide → 1.0Hydrogen ion + 1.0Acetic acid + 1.0L-Cysteine
ReactionCard
1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Cysteine → 1.0Hydrogen ion + 1.0Hydrogen sulfide + 1.02-Aminoacrylic acid
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0O-Acetylserine + 1.0Hydrogen sulfide ↔ 1.0Acetic acid + 1.0L-Cysteine + 1.0Hydrogen ion
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0O-Acetylserine + 1.0Hydrogen sulfide → 1.0L-Cysteine + 1.0Acetic acid
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB036092-Aminoacrylic acidMetaboCard
ECMDB00042Acetic acidMetaboCard
ECMDB04037ChlorideMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB11110Hydrogen selenideMetaboCard
ECMDB03276Hydrogen sulfideMetaboCard
ECMDB00574L-CysteineMetaboCard
ECMDB03011O-AcetylserineMetaboCard
ECMDB23102S-Carboxymethyl-L-cysteineMetaboCard
ECMDB03288SelenocysteineMetaboCard
ECMDB00240SulfiteMetaboCard
ECMDB21573ThioglycolateMetaboCard
ECMDB23749ThioredoxinMetaboCard
ECMDB00257ThiosulfateMetaboCard
GO Classification:
Function
binding
carbon-oxygen lyase activity
catalytic activity
cofactor binding
cysteine synthase activity
lyase activity
pyridoxal phosphate binding
Process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
cysteine biosynthetic process from serine
L-serine metabolic process
metabolic process
serine family amino acid metabolic process
Gene Properties
Blattner:b2414
Gene OrientationClockwise
Centisome Percentage:54.54
Left Sequence End2530431
Right Sequence End2531402
Gene Sequence:
>972 bp
GTGGCACAGGAATATACTGTTGAACAACTAAACCACGGCCGTAAAGTCTATGACTTTATG
CGCTGGGACTACTGGGCTTTCGGCATCTCTGGTCTGCTGTTAATCGCTGCTATCGTTATT
ATGGGCGTGCGCGGCTTTAACTGGGGGCTGGATTTCACCGGTGGTACGGTTATTGAAATT
ACGCTCGAAAAACCGGCTGAAATTGACGTAATGCGTGATGCATTGCAAAAAGCCGGTTTT
GAAGAGCCGATGCTGCAAAACTTTGGTAGCAGCCATGACATCATGGTCCGTATGCCGCCT
GCTGAAGGCGAAACCGGCGGTCAGGTGTTGGGCAGCCAGGTTCTGAAGGTGATTAACGAA
TCCACCAATCAGAATGCAGCAGTGAAGCGTATTGAGTTCGTCGGTCCGAGCGTGGGGGCA
GACCTTGCGCAAACCGGTGCGATGGCGTTGATGGCAGCGCTGCTGTCTATCCTCGTGTAC
GTAGGTTTCCGCTTTGAGTGGCGACTGGCGGCAGGGGTGGTTATTGCGCTGGCGCACGAC
GTTATCATTACGCTGGGTATTTTGTCGTTATTCCATATCGAGATTGACCTGACCATTGTG
GCATCGTTGATGTCGGTTATCGGTTACTCGCTTAACGACAGTATCGTGGTATCGGACCGT
ATTCGTGAAAACTTCCGCAAGATCCGTCGCGGTACGCCTTACGAAATCTTTAACGTGTCC
TTGACCCAGACGCTGCACCGTACCTTGATCACATCCGGTACTACCTTGATGGTTATCCTG
ATGCTGTACCTCTTCGGTGGTCCGGTACTGGAAGGCTTCTCGCTGACCATGCTTATCGGT
GTTTCCATCGGTACTGCATCTTCCATCTATGTGGCATCTGCGTTGGCTCTGAAACTGGGT
ATGAAGCGCGAACACATGTTGCAGCAGAAAGTGGAAAAAGAAGGGGCGGATCAGCCGTCA
ATTCTGCCGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:323
Protein Molecular Weight:34489
Protein Theoretical pI:6
PDB File:1FCJ
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Cysteine synthase A
MSKIFEDNSLTIGHTPLVRLNRIGNGRILAKVESRNPSFSVKCRIGANMIWDAEKRGVLK
PGVELVEPTSGNTGIALAYVAAARGYKLTLTMPETMSIERRKLLKALGANLVLTEGAKGM
KGAIQKAEEIVASNPEKYLLLQQFSNPANPEIHEKTTGPEIWEDTDGQVDVFIAGVGTGG
TLTGVSRYIKGTKGKTDLISVAVEPTDSPVIAQALAGEEIKPGPHKIQGIGAGFIPANLD
LKLVDKVIGITNEEAISTARRLMEEEGILAGISSGAAVAAALKLQEDESFTNKNIVVILP
SSGERYLSTALFADLFTEKELQQ
References
External Links:
ResourceLink
Uniprot ID:P0ABK5
Uniprot Name:CYSK_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674549
PDB ID:1FCJ
Ecogene ID:EG10192
Ecocyc:EG10192
ColiBase:b2414
Kegg Gene:b2414
EchoBASE ID:EB0189
CCDB:CYSK_ECOLI
BacMap:16130340
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Byrne, C. R., Monroe, R. S., Ward, K. A., Kredich, N. M. (1988). "DNA sequences of the cysK regions of Salmonella typhimurium and Escherichia coli and linkage of the cysK regions to ptsH." J Bacteriol 170:3150-3157. Pubmed: 3290198
  • De Reuse, H., Danchin, A. (1988). "The ptsH, ptsI, and crr genes of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system: a complex operon with several modes of transcription." J Bacteriol 170:3827-3837. Pubmed: 2457575
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Henzel, W. J., Billeci, T. M., Stults, J. T., Wong, S. C., Grimley, C., Watanabe, C. (1993). "Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases." Proc Natl Acad Sci U S A 90:5011-5015. Pubmed: 8506346
  • Levy, S., Danchin, A. (1988). "Phylogeny of metabolic pathways: O-acetylserine sulphydrylase A is homologous to the tryptophan synthase beta subunit." Mol Microbiol 2:777-783. Pubmed: 3062311
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Quadroni, M., Staudenmann, W., Kertesz, M., James, P. (1996). "Analysis of global responses by protein and peptide fingerprinting of proteins isolated by two-dimensional gel electrophoresis. Application to the sulfate-starvation response of Escherichia coli." Eur J Biochem 239:773-781. Pubmed: 8774726
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837