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Escherichia coli K-12 substr. MG1655 Polypeptide: sulfate adenylyltransferase, CysD subunit



Gene: cysD Accession Numbers: EG10186 (EcoCyc), b2752, ECK2747

Regulation Summary Diagram: ?

Component of: sulfate adenylyltransferase (summary available)

Summary:
CysD along with CysN are the two subunits which form sulfate adenylyltransferase [Leyh88]. This enzyme is involved in the assimilation of sulfate and catalyzes two reactions, GTP hydrolysis and activation of intracellular sulfate to adenosine 5'-phosphosulfate (APS) which generates a sulfate-phosphate anhydride linkage. This linkage facilitates an energetically-downhill entry into the subsequent metabolic fates of reduction and group transfer. The rate of APS formation is enhanced by both a protein activator and by GTP hydrolysis [Neuwald92].

Mutations in the cysD gene prevent the anabolic utilization of sulfate [Leyh88].

cysD, along with cysN and cysC, resides in the sulfate activation operon [Leyh92].

cysD shows differential codon adaptation, resulting in differential translation efficiency signatures, in aerotolerant compared to obligate anaerobic microbes. It was therefore predicted to play a role in the oxidative stress response. A cysD deletion mutant was shown to be more sensitive than wild-type specifically to hydrogen peroxide exposure, but not other stresses [Kri14].

Gene Citations: [Malo90]

Locations: cytosol

Map Position: [2,873,443 <- 2,874,351] (61.93 centisomes)
Length: 909 bp / 302 aa

Molecular Weight of Polypeptide: 35.188 kD (from nucleotide sequence), 27 kD (experimental) [Leyh88 ]

Unification Links: ASAP:ABE-0009029 , CGSC:895 , DIP:DIP-360N , DIP:DIP-9376N , EchoBASE:EB0183 , EcoGene:EG10186 , EcoliWiki:b2752 , ModBase:P21156 , OU-Microarray:b2752 , PortEco:cysD , PR:PRO_000022376 , Pride:P21156 , Protein Model Portal:P21156 , RefSeq:NP_417232 , RegulonDB:EG10186 , SMR:P21156 , String:511145.b2752 , Swiss-Model:P21156 , UniProt:P21156

Relationship Links: InterPro:IN-FAMILY:IPR002500 , InterPro:IN-FAMILY:IPR011784 , InterPro:IN-FAMILY:IPR014729 , Pfam:IN-FAMILY:PF01507

In Paralogous Gene Group: 452 (2 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006790 - sulfur compound metabolic process Inferred from experiment [Leyh88]
GO:0006979 - response to oxidative stress Inferred from experiment [Kri14]
GO:0000103 - sulfate assimilation Inferred by computational analysis [GOA06]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01]
GO:0019419 - sulfate reduction Inferred by computational analysis [GOA01]
GO:0070814 - hydrogen sulfide biosynthetic process Inferred by computational analysis [UniProtGOA12]
Molecular Function: GO:0004781 - sulfate adenylyltransferase (ATP) activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, GOA01, Leyh88]
GO:0005515 - protein binding Inferred from experiment [Leyh88]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11]
GO:0016779 - nucleotidyltransferase activity Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism metabolism of other compounds sulfur metabolism

Essentiality data for cysD knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 0.4% glucose No 37 Aerobic 7.2 0.27 No [Patrick07, Comment 3]
M9 medium with 1% glycerol No 37 Aerobic 7.2 0.35 No [Joyce06]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Credits:
Last-Curated ? 23-Aug-2013 by Kubo A , SRI International


Subunit of: sulfate adenylyltransferase

Subunit composition of sulfate adenylyltransferase = [CysD]4[CysN]4
         sulfate adenylyltransferase, CysD subunit = CysD (extended summary available)
         sulfate adenylyltransferase, CysN subunit = CysN (summary available)

Summary:
Sulfate adenylyltransferase is composed of two types of subunits, CysN (53 kDa) and CysD (35 kDa) [Leyh88]. The native (390 kDa) molecular weight suggests that the enzyme is a tetramer of CysD-CysN heterodimers .

The enzyme catalyzes the activation of intracellular sulfate to adenosine 5'-phosphosulfate (APS), a reaction that generates a sulfate-phosphate anhydride linkage. This linkage facilitates an energetically-downhill entry into the subsequent metabolic fates of reduction and group transfer. The rate of APS formation is enhanced by both a protein activator and by GTP hydrolysis [Neuwald92]. The intrinsic GTPase Is believed to be the CysN subunit [Leyh92a].

Credits:
Created 20-Sep-2006 by Caspi R , SRI International


Enzymatic reaction of: sulfate adenylyltransferase

Synonyms: sulfate adenylate transferase, ATP-sulfurylase, sulfurylase, ATP:sulfate adenylyltransferase, adenylylsulfate pyrophosphorylase

EC Number: 2.7.7.4

sulfate + ATP + H+ <=> adenosine 5'-phosphosulfate + diphosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: superpathway of sulfate assimilation and cysteine biosynthesis , sulfate reduction I (assimilatory) , sulfate activation for sulfonation

Summary:
Studies using the hydrolysis-resistant nucleotide analogues AMPCPP and GMPPNP demonstrated that GTP hydrolysis precedes scision of the α-β bond of ATP. Product inhibition studies indicate that PPi release occurs prior to the addition of sulfate and APS formation [Liu94c].


Sequence Features

Feature Class Location Citations Comment
Sequence-Conflict 180
[Leyh92, UniProt10]
Alternate sequence: S → T; UniProt: (in Ref. 1; AAA23645);


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b2752 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10186; confirmed by SwissProt match.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kri14: Krisko A, Copi T, Gabaldon T, Lehner B, Supek F (2014). "Inferring gene function from evolutionary change in signatures of translation efficiency." Genome Biol 15(3);R44. PMID: 24580753

Leyh88: Leyh TS, Taylor JC, Markham GD (1988). "The sulfate activation locus of Escherichia coli K12: cloning, genetic, and enzymatic characterization." J Biol Chem 263(5);2409-16. PMID: 2828368

Leyh92: Leyh TS, Vogt TF, Suo Y (1992). "The DNA sequence of the sulfate activation locus from Escherichia coli K-12." J Biol Chem 1992;267(15);10405-10. PMID: 1316900

Leyh92a: Leyh TS, Suo Y (1992). "GTPase-mediated activation of ATP sulfurylase." J Biol Chem 1992;267(1);542-5. PMID: 1730615

Liu94c: Liu C, Martin E, Leyh TS (1994). "GTPase activation of ATP sulfurylase: the mechanism." Biochemistry 33(8);2042-7. PMID: 8117661

Malo90: Malo MS, Loughlin RE (1990). "Promoter elements and regulation of expression of the cysD gene of Escherichia coli K-12." Gene 1990;87(1);127-31. PMID: 2185135

Neuwald92: Neuwald AF, Krishnan BR, Brikun I, Kulakauskas S, Suziedelis K, Tomcsanyi T, Leyh TS, Berg DE (1992). "cysQ, a gene needed for cysteine synthesis in Escherichia coli K-12 only during aerobic growth." J Bacteriol 1992;174(2);415-25. PMID: 1729235

Patrick07: Patrick WM, Quandt EM, Swartzlander DB, Matsumura I (2007). "Multicopy suppression underpins metabolic evolvability." Mol Biol Evol 24(12);2716-22. PMID: 17884825

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Other References Related to Gene Regulation

Kredich92: Kredich NM (1992). "The molecular basis for positive regulation of cys promoters in Salmonella typhimurium and Escherichia coli." Mol Microbiol 6(19);2747-53. PMID: 1435253


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Thu Nov 27, 2014, BIOCYC13A.