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Escherichia coli K-12 substr. MG1655 Enzyme: cysteine sulfinate desulfinase



Gene: csdA Accession Numbers: G7454 (EcoCyc), b2810, ECK2806

Synonyms: ygdJ

Regulation Summary Diagram: ?

Subunit composition of cysteine sulfinate desulfinase = [CsdA]2
         cysteine sulfinate desulfinase = CsdA

Summary:
CsdA is a desulfinase which can utilize L-cysteine sulfinate, L-cysteine or L-selenocysteine as substrates [Mihara97]. The mechanism of L-cysteine desulfurization is different from that of L-selenocysteine degradation [Mihara00]. CsdA and CsdE combine to form the CSD sulfur transfer system. CsdA activity doubles in the presence of CsdE, which contains a cysteine residue (C61) that acts to accept sulfur liberated via the desulfinase activity of CsdA [Loiseau05]. CsdA can also transfer sulfur directly to CsdL in vitro [Trotter09].

Utilizing L-cysteine, the enzyme can provide sulfur to molybdopterin synthase in vitro; the sulfur appears to be transferred as a protein-bound persulfide [Leimkuhler01]. It is also able to provide sulfur for the ferredoxin iron-sulfur cluster assembly in vitro [Kurihara03]. With L-selenocysteine as substrate [Mihara97], CsdA can provide selenide to selenophosphate synthetase [Lacourciere00].

Unlike other cysteine desulfurases, none of the Cys residues of CsdA was reported to be essential for enzymatic activity [Mihara97]. In a later report, a C358A mutant was shown to be catalytically inactive towards L-cysteine, but showed activity with L-cysteine sulfinate and L-selenocysteine [Mihara00].

Overexpression of csdA suppresses the growth defect of an iscS sufS double mutant due to interaction of CsdA with the SufBCDE system [Trotter09]. In growth competition experiments, a csdA mutant is outcompeted by wild type after 48 h of co-culture. A csdA mutant is unable to swim [Trotter09].

CsdA: "cysteine sulfinate desulfinase"

Locations: cytosol

Map Position: [2,941,359 -> 2,942,564] (63.4 centisomes)
Length: 1206 bp / 401 aa

Molecular Weight of Polypeptide: 43.234 kD (from nucleotide sequence), 43.0 kD (experimental) [Mihara97 ]

Molecular Weight of Multimer: 97.0 kD (experimental) [Mihara97]

Unification Links: ASAP:ABE-0009218 , DIP:DIP-9323N , EchoBASE:EB2891 , EcoGene:EG13082 , EcoliWiki:b2810 , ModBase:Q46925 , OU-Microarray:b2810 , PortEco:csdA , PR:PRO_000022335 , Pride:Q46925 , Protein Model Portal:Q46925 , RefSeq:NP_417290 , RegulonDB:G7454 , SMR:Q46925 , String:511145.b2810 , Swiss-Model:Q46925 , UniProt:Q46925

Relationship Links: InterPro:IN-FAMILY:IPR000192 , InterPro:IN-FAMILY:IPR015421 , InterPro:IN-FAMILY:IPR015422 , InterPro:IN-FAMILY:IPR015424 , InterPro:IN-FAMILY:IPR020578 , InterPro:IN-FAMILY:IPR022471 , PDB:Structure:4LW2 , PDB:Structure:4LW4 , Pfam:IN-FAMILY:PF00266 , Prosite:IN-FAMILY:PS00595

In Paralogous Gene Group: 428 (3 members)

In Reactions of unknown directionality:

Not in pathways:
an [L-cysteine desulfurase] + L-cysteine = an S-sulfanyl-[L-cysteine desulfurase] + L-alanine

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0000096 - sulfur amino acid metabolic process Inferred from experiment [Mihara97]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
GO:0016226 - iron-sulfur cluster assembly Inferred by computational analysis [GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Kim13d, Trotter09, Loiseau05]
GO:0016783 - sulfurtransferase activity Inferred from experiment [Leimkuhler01]
GO:0030170 - pyridoxal phosphate binding Inferred from experiment Inferred by computational analysis [GOA01a, Mihara97]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01a]
GO:0009000 - selenocysteine lyase activity Inferred by computational analysis [GOA01]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016829 - lyase activity Inferred by computational analysis [UniProtGOA11a]
GO:0031071 - cysteine desulfurase activity Inferred by computational analysis [GOA01, GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism central intermediary metabolism amino acid conversion
metabolism metabolism of other compounds sulfur metabolism

Essentiality data for csdA 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 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Credits:
Created 14-Jan-2010 by Keseler I , SRI International
Last-Curated ? 14-Jan-2010 by Keseler I , SRI International


Enzymatic reaction of: cysteine sulfinate desulfinase

Synonyms: L-cysteine desulfurase

EC Number: 3.13.1.-

3-sulfinoalanine + H2O <=> L-alanine + sulfite + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

Reversibility of this reaction is unspecified.

Alternative Substrates for 3-sulfinoalanine: L-cysteine [Mihara97 ] , L-selenocysteine [Mihara97 ]

Cofactors or Prosthetic Groups: pyridoxal 5'-phosphate [Mihara97]

Activators (Unknown Mechanism): pyruvate [Mihara00, Comment 5]

Kinetic Parameters:

Substrate
Km (μM)
Citations
3-sulfinoalanine
240.0
[Mihara97]

pH(opt): 8.2 [Mihara97]


Sequence Features

Feature Class Location Citations Comment
Mutagenesis-Variant 100
[Mihara97, UniProt11]
Alternate sequence: C → A; UniProt: No loss of activity.
Mutagenesis-Variant 176
[Mihara97, UniProt11]
Alternate sequence: C → A; UniProt: No loss of activity.
N6-pyridoxal-phosphate-Lys-Modification 222
[UniProt11a]
UniProt: N6-(pyridoxal phosphate)lysine; Non-Experimental Qualifier: by similarity.
Mutagenesis-Variant 323
[Mihara97, UniProt11]
Alternate sequence: C → A; UniProt: No loss of activity.
Mutagenesis-Variant 358
[Mihara97, Mihara00, UniProt11]
Alternate sequence: C → A; UniProt: Loss of cysteine desulfurization.
Active-Site 358
[UniProt10a]
UniProt: Non-Experimental Qualifier: probable;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


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

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

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

Kim13d: Kim S, Park S (2013). "Structural changes during cysteine desulfurase CsdA and sulfur acceptor CsdE interactions provide insight into the trans-persulfuration." J Biol Chem 288(38);27172-80. PMID: 23913692

Kurihara03: Kurihara T, Mihara H, Kato S, Yoshimura T, Esaki N (2003). "Assembly of iron-sulfur clusters mediated by cysteine desulfurases, IscS, CsdB and CSD, from Escherichia coli." Biochim Biophys Acta 1647(1-2);303-9. PMID: 12686149

Lacourciere00: Lacourciere GM, Mihara H, Kurihara T, Esaki N, Stadtman TC (2000). "Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate." J Biol Chem 2000;275(31);23769-73. PMID: 10829016

Leimkuhler01: Leimkuhler S, Rajagopalan KV (2001). "A sulfurtransferase is required in the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z in Escherichia coli." J Biol Chem 276(25);22024-31. PMID: 11290749

Loiseau05: Loiseau L, Ollagnier-de Choudens S, Lascoux D, Forest E, Fontecave M, Barras F (2005). "Analysis of the heteromeric CsdA-CsdE cysteine desulfurase, assisting Fe-S cluster biogenesis in Escherichia coli." J Biol Chem 280(29);26760-9. PMID: 15901727

Mihara00: Mihara H, Kurihara T, Yoshimura T, Esaki N (2000). "Kinetic and mutational studies of three NifS homologs from Escherichia coli: Mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions." J. Biochem. 127:559-567 (2000). PMID: 10739946

Mihara97: Mihara H, Kurihara T, Yoshimura T, Soda K, Esaki N (1997). "Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme." J Biol Chem 1997;272(36);22417-24. PMID: 9278392

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Trotter09: Trotter V, Vinella D, Loiseau L, Ollagnier de Choudens S, Fontecave M, Barras F (2009). "The CsdA cysteine desulphurase promotes Fe/S biogenesis by recruiting Suf components and participates to a new sulphur transfer pathway by recruiting CsdL (ex-YgdL), a ubiquitin-modifying-like protein." Mol Microbiol 74(6);1527-42. PMID: 20054882

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-11 released on 2011-11-22 00:00:00." Database.

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."


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 Sat Nov 22, 2014, BIOCYC13A.