|Gene:||cysD||Accession Numbers: EG10186 (EcoCyc), b2752, ECK2747|
Component of: sulfate adenylyltransferase (summary available)
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 [Leyh92a].
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]
|Map Position: [2,873,443 <- 2,874,351] (61.93 centisomes, 223°)||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 , 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
In Paralogous Gene Group: 452 (2 members)
|Biological Process:||GO:0006790 - sulfur compound metabolic process
GO:0006979 - response to oxidative stress [Kri14]
GO:0000103 - sulfate assimilation [GOA06]
GO:0008152 - metabolic process [GOA01a]
GO:0019419 - sulfate reduction [GOA01a]
GO:0070814 - hydrogen sulfide biosynthetic process [UniProtGOA12]
|Molecular Function:||GO:0004781 - sulfate adenylyltransferase (ATP) activity
[GOA06, GOA01, GOA01a, Leyh88]
GO:0005515 - protein binding [Leyh88]
GO:0000166 - nucleotide binding [UniProtGOA11a]
GO:0003824 - catalytic activity [GOA01a]
GO:0005524 - ATP binding [UniProtGOA11a]
GO:0016740 - transferase activity [UniProtGOA11a]
GO:0016779 - nucleotidyltransferase activity [UniProtGOA11a]
|Cellular Component:||GO:0005829 - cytosol [DiazMejia09]|
|MultiFun Terms:||metabolism → metabolism of other compounds → sulfur metabolism|
|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]
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)
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 [Leyh92].
Enzymatic reaction of: sulfate adenylyltransferase
Synonyms: sulfate adenylate transferase, ATP-sulfurylase, sulfurylase, ATP:sulfate adenylyltransferase, adenylylsulfate pyrophosphorylase
EC Number: 220.127.116.11
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.
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 [Liu94b].
10/20/97 Gene b2752 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10186; confirmed by SwissProt match.
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
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
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
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