DB code: D00659
| CATH domain | 3.90.1150.10 : Aspartate Aminotransferase, domain 1 | Catalytic domain |
|---|---|---|
| 3.40.640.10 : Aspartate Aminotransferase; domain 2 | Catalytic domain | |
| E.C. | 2.8.1.7 | |
| CSA | 1ecx | |
| M-CSA | 1ecx | |
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
|---|---|---|---|---|
| P0A6B7 |
Cysteine desulfurase
|
EC
2.8.1.7
NifS protein homolog ThiI transpersulfidase |
YP_026169.1
(Protein)
NC_000913.2 (DNA/RNA sequence) YP_490758.1 (Protein) NC_007779.1 (DNA/RNA sequence) |
PF00266
(Aminotran_5)
[Graphical View] |
| P0A6B9 |
Cysteine desulfurase
|
EC
2.8.1.7
|
NP_289087.1
(Protein)
NC_002655.2 (DNA/RNA sequence) NP_311423.2 (Protein) NC_002695.1 (DNA/RNA sequence) |
PF00266
(Aminotran_5)
[Graphical View] |
| Q9X218 |
|
Aminotransferase, class V
Cysteine desulfurase EC 2.8.1.7 |
NP_229492.1
(Protein)
NC_000853.1 (DNA/RNA sequence) |
PF00266
(Aminotran_5)
[Graphical View] |
| Q55793 |
Probable cysteine desulfurase
|
EC
2.8.1.7
|
NP_442475.1
(Protein)
NC_000911.1 (DNA/RNA sequence) YP_005652536.1 (Protein) NC_017277.1 (DNA/RNA sequence) YP_007452351.1 (Protein) NC_020286.1 (DNA/RNA sequence) |
PF00266
(Aminotran_5)
[Graphical View] |
| KEGG enzyme name |
|---|
|
Cysteine desulfurase
IscS NIFS NifS SufS Cysteine desulfurylase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P0A6B7 | ISCS_ECOLI | L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor. | Homodimer. The homodimer interacts with tusA. | Cytoplasm (Probable). | Pyridoxal phosphate. |
| P0A6B9 | ISCS_ECO57 | L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor | Pyridoxal phosphate. | ||
| Q9X218 | Q9X218_THEMA | Pyridoxal phosphate. | |||
| Q55793 | CSD_SYNY3 | L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor. | Pyridoxal phosphate. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00730 | Thiamine metabolism |
| Compound table | ||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | |||||||||||||||
| KEGG-id | C00018 | C00097 | L00106 | C00041 | L00105 | I00165 | I00166 | I00167 | I00171 | C15812 | I00030 | I00032 | I00049 | |||||
| E.C. | ||||||||||||||||||
| Compound | Pyridoxal phosphate | L-cysteine | Acceptor for sulfur | L-alanine | S-sulfanyl-acceptor | External aldimine intermediate (PLP-L-Cys) | Quinonoid intermediate (PLP-Cys) | Ketimine intermediate (PLP-Cys) | Aminoacrylate intermediate (PLP-dehydroAla) | [enzyme]-S-sulfanylcysteine | Ketimine intermediate (PLP-Ala) | Quinonoid intermediate (PLP-Ala) | External aldimine intermediate (PLP-L-Ala) | |||||
| Type | aromatic ring (with nitrogen atoms),phosphate group/phosphate ion | amino acids,sulfhydryl group | others | amino acids | others,sulfhydryl group | |||||||||||||
| ChEBI |
18405 18405 |
17561 35235 17561 35235 |
16977 57972 16977 57972 |
|||||||||||||||
| PubChem |
1051 1051 |
5862 6419722 5862 6419722 |
5950 7311724 5950 7311724 |
|||||||||||||||
| 1p3wA01 |
|
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1p3wB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 3lvjA01 |
|
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|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 3lvjB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 3lvkA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 3lvlB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 3lvmA01 |
|
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|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 3lvmB01 |
|
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|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ecxA01 |
|
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|
|
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Unbound | Bound:CYS_502 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ecxB01 |
|
|
|
|
|
Unbound | Bound:CYS_503 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1eg5A01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1eg5B01 |
|
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|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1t3iA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1t3iB01 |
|
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|
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1p3wA02 |
|
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|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1p3wB02 |
|
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|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 3lvjA02 |
|
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|
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 3lvjB02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 3lvkA02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 3lvlB02 |
|
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 3lvmA02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 3lvmB02 |
|
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|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ecxA02 |
|
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|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ecxB02 |
|
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|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1eg5A02 |
|
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|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1eg5B02 |
|
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|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1t3iA02 |
|
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|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1t3iB02 |
|
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|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| literature[3],[8],[9] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1p3wA01 |
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|
invisible 328-333 | ||||
| 1p3wB01 |
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invisible 328-333 | ||||
| 3lvjA01 |
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invisible 327-332 | ||||
| 3lvjB01 |
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CYS 328 | invisible 329-332 | |||
| 3lvkA01 |
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CYS 328 | invisible 329-332 | |||
| 3lvlB01 |
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invisible 328-332 | ||||
| 3lvmA01 |
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invisible 328-332 | ||||
| 3lvmB01 |
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invisible 328-332 | ||||
| 1ecxA01 |
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invisible 321-332 | ||||
| 1ecxB01 |
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invisible 321-331 | ||||
| 1eg5A01 |
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invisible 321-332 | ||||
| 1eg5B01 |
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invisible 321-331 | ||||
| 1t3iA01 |
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CYS 372 | ||||
| 1t3iB01 |
|
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CYS 372 | ||||
| 1p3wA02 |
|
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HIS 104;ASP 180;GLN 183;LYS 206 | LYS 206(PLP binding) | |||
| 1p3wB02 |
|
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HIS 104;ASP 180;GLN 183;LYS 206 | LYS 206(PLP binding) | |||
| 3lvjA02 |
|
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HIS 104;ASP 180;GLN 183;LYS 206 | LYS 206(PLP binding) | |||
| 3lvjB02 |
|
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HIS 104;ASP 180;GLN 183;LYS 206 | LYS 206(PLP binding) | |||
| 3lvkA02 |
|
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HIS 104;ASP 180;GLN 183;LYS 206 | LYS 206(PLP binding) | |||
| 3lvlB02 |
|
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HIS 104;ASP 180;GLN 183;LYS 206 | LYS 206(PLP binding) | |||
| 3lvmA02 |
|
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HIS 104;ASP 180;GLN 183;LYS 206 | LYS 206(PLP binding) | |||
| 3lvmB02 |
|
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HIS 104;ASP 180;GLN 183;LYS 206 | LYS 206(PLP binding) | |||
| 1ecxA02 |
|
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HIS 99;ASP 177;GLN 180;LYS 203 | LYS 203(PLP binding) | |||
| 1ecxB02 |
|
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HIS 99;ASP 177;GLN 180;LYS 203 | LYS 203(PLP binding) | |||
| 1eg5A02 |
|
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HIS 99;ASP 177;GLN 180;LYS 203 | LYS 203(PLP binding) | |||
| 1eg5B02 |
|
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HIS 99;ASP 177;GLN 180;LYS 203 | LYS 203(PLP binding) | |||
| 1t3iA02 |
|
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HIS 128;ASP 205;GLN 208;LYS 231 | LYS 231(PLP binding) | |||
| 1t3iB02 |
|
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HIS 128;ASP 205;GLN 208;LYS 231 | LYS 231(PLP binding) | |||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[1]
|
SCHEME3, p.4719 | |
|
[3]
|
SCHEME1, p.459-460 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8161529 |
| Journal | Biochemistry |
| Year | 1994 |
| Volume | 33 |
| Pages | 4714-20 |
| Authors | Zheng L, White RH, Cash VL, Dean DR |
| Title | Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments |
PROTEIN SEQUENCE OF 1-9, |
| Medline ID | |
| PubMed ID | 10739946 |
| Journal | J Biochem |
| Year | 2000 |
| Volume | 127 |
| Pages | 559-67 |
| Authors | Mihara H, Kurihara T, Yoshimura T, Esaki N |
| Title | Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments |
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), |
| Medline ID | |
| PubMed ID | 10715213 |
| Journal | J Mol Biol |
| Year | 2000 |
| Volume | 297 |
| Pages | 451-64 |
| Authors | Kaiser JT, Clausen T, Bourenkow GP, Bartunik HD, Steinbacher S, Huber R |
| Title | Crystal structure of a NifS-like protein from Thermotoga maritima: implications for iron sulphur cluster assembly. |
| Related PDB | 1ecx 1eg5 |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11577100 |
| Journal | J Biol Chem |
| Year | 2001 |
| Volume | 276 |
| Pages | 44521-6 |
| Authors | Urbina HD, Silberg JJ, Hoff KG, Vickery LE |
| Title | Transfer of sulfur from IscS to IscU during Fe/S cluster assembly. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11825893 |
| Journal | J Biol Chem |
| Year | 2002 |
| Volume | 277 |
| Pages | 12868-73 |
| Authors | Yang W, Rogers PA, Ding H |
| Title | Repair of nitric oxide-modified ferredoxin [2Fe-2S] cluster by cysteine desulfurase (IscS). |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11972033 |
| Journal | Proc Natl Acad Sci U S A |
| Year | 2002 |
| Volume | 99 |
| Pages | 5948-52 |
| Authors | Kato S, Mihara H, Kurihara T, Takahashi Y, Tokumoto U, Yoshimura T, Esaki N |
| Title | Cys-328 of IscS and Cys-63 of IscU are the sites of disulfide bridge formation in a covalently bound IscS/IscU complex: implications for the mechanism of iron-sulfur cluster assembly. |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12382038 |
| Journal | Appl Microbiol Biotechnol |
| Year | 2002 |
| Volume | 60 |
| Pages | 12-23 |
| Authors | Mihara H, Esaki N |
| Title | Bacterial cysteine desulfurases: their function and mechanisms. |
| Related PDB | |
| Related UniProtKB | |
| [8] | |
| Resource | |
| Comments |
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), |
| Medline ID | |
| PubMed ID | 12860127 |
| Journal | J Mol Biol |
| Year | 2003 |
| Volume | 330 |
| Pages | 1049-59 |
| Authors | Cupp-Vickery JR, Urbina H, Vickery LE |
| Title |
Crystal structure of IscS, |
| Related PDB | 1p3w |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments |
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), |
| Medline ID | |
| PubMed ID | 15379559 |
| Journal | Biochemistry |
| Year | 2004 |
| Volume | 43 |
| Pages | 12210-9 |
| Authors | Tirupati B, Vey JL, Drennan CL, Bollinger JM Jr |
| Title |
Kinetic and structural characterization of Slr0077/SufS, |
| Related PDB | 1t3i |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 19883076 |
| Journal | Biochemistry |
| Year | 2009 |
| Volume | 48 |
| Pages | 12014-23 |
| Authors | Behshad E, Bollinger JM Jr |
| Title |
Kinetic analysis of cysteine desulfurase CD0387 from Synechocystis sp. |
| Related PDB | |
| Related UniProtKB | |
| [11] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 19308466 |
| Journal | J Biol Inorg Chem |
| Year | 2009 |
| Volume | 14 |
| Pages | 829-39 |
| Authors | Nuth M, Cowan JA |
| Title | Iron-sulfur cluster biosynthesis: characterization of IscU-IscS complex formation and a structural model for sulfide delivery to the [2Fe-2S] assembly site. |
| Related PDB | |
| Related UniProtKB | |
| [12] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 19946146 |
| Journal | J Biol Chem |
| Year | 2010 |
| Volume | 285 |
| Pages | 2302-8 |
| Authors | Zhang W, Urban A, Mihara H, Leimkuhler S, Kurihara T, Esaki N |
| Title | IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli. |
| Related PDB | |
| Related UniProtKB | |
| [13] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 20404999 |
| Journal | PLoS Biol |
| Year | 2010 |
| Volume | 8 |
| Pages | e1000354 |
| Authors | Shi R, Proteau A, Villarroya M, Moukadiri I, Zhang L, Trempe JF, Matte A, Armengod ME, Cygler M |
| Title | Structural basis for Fe-S cluster assembly and tRNA thiolation mediated by IscS protein-protein interactions. |
| Related PDB | 3lvj 3lvk 3lvl 3lvm |
| Related UniProtKB | |
| Comments |
|---|
|
This enzyme catalyzes the elimination of sulfur from L-cysteine to produce L-alanine and sulfane sulfur, This enzyme catalyzes the following reactions (see [3], (A) Formation of external aldimine of PLP with amine group of L-cysteine (I00165) (from the internal aldimine with Lys). (B) Isomerization of the Cys external aldimine to form a Cys ketimine intermediate(I00167), (C) Transfer of thiol group from the ketimine intermediate (I00167) to active-site Cys, (D) Isomerization of the aminoacrylate intermediate (I00171), (E) Isomerization of the Ala ketimine intermediate(I00030) to form an Ala external aldimine(I00049), (F) Formation of internal aldimine of PLP with active-site Lys (from the external aldimine (I00049), (G) Transfer of thiol group from the persulfide intermediate (C15812) to the acceptor protein. #### Acording to the literature [3] and [8], Asp205 and Gln208 (of 1t3i) may modulate the activity of PLP. His128 might act as a general acid/base to protonate either PLP or Cys ketimine intermediate, Lys231 may also act as a general acid/base to deprotonate and protonate the external aldimine intermediates (I00165 and I00049). Cys372 acts as a nucleophile to accept the thiol group from the Cys ketimine intermediate(I00167), |
| Created | Updated |
|---|---|
| 2013-07-24 | 2013-11-14 |