DB code: S00028
| RLCP classification | 10.21011.100.10210 : Electron transfer | |
|---|---|---|
| CATH domain | 1.10.620.20 : Ribonucleotide Reductase, subunit A | Catalytic domain |
| E.C. | 1.14.19.2 | |
| CSA | 1afr | |
| M-CSA | 1afr | |
| MACiE | M0136 | |
| CATH domain | Related DB codes (homologues) |
|---|---|
| 1.10.620.20 : Ribonucleotide Reductase, subunit A | M00151 M00204 M00205 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
|---|---|---|---|---|
| P22337 |
Acyl-[acyl-carrier-protein] desaturase, chloroplastic
|
EC
1.14.19.2
Stearoyl-ACP desaturase Delta(9) stearoyl-acyl carrier protein desaturase |
XP_002531889.1
(Protein)
XM_002531843.1 (DNA/RNA sequence) |
PF03405
(FA_desaturase_2)
[Graphical View] |
| KEGG enzyme name |
|---|
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acyl-[acyl-carrier-protein] desaturase
stearyl acyl carrier protein desaturase stearyl-ACP desaturase acyl-[acyl-carrier-protein], hydrogen-donor:oxygen oxidoreductase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P22337 | STAD_RICCO | Stearoyl-[acyl-carrier-protein] + reduced acceptor + O(2) = oleoyl-[acyl-carrier-protein] + acceptor + 2 H(2)O. | Homodimer. | Plastid, chloroplast. Plastid. Note=In green tissue, found in chloroplasts. In non-photosynthetic tissue, found in plastids. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00061 | Fatty acid biosynthesis | |
| MAP01040 | Biosynthesis of unsaturated fatty acids |
| Compound table | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | ||||||||||
| KEGG-id | C99999 | C00007 | C00138 | C04088 | C00001 | C00139 | C01203 | ||||||
| E.C. | |||||||||||||
| Compound | Diiron | O2 | Reduced ferredoxin | Stearoyl-[acyl-carrier protein] | H2O | Oxidized ferredoxin | Oleoyl-[acyl-carrier protein] | ||||||
| Type | heavy metal | others | heavy metal,peptide/protein,sulfide group | carbohydrate,lipid,peptide/protein,phosphate group/phosphate ion,sulfide group | H2O | heavy metal,peptide/protein,sulfide group | carbohydrate,lipid,peptide/protein,phosphate group/phosphate ion,sulfide group | ||||||
| ChEBI |
15379 26689 27140 15379 26689 27140 |
15377 15377 |
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| PubChem |
977 977 |
22247451 962 22247451 962 |
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| 1afrA |
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Bound:FE2-FE2 | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1afrB |
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Bound:FE2-FE2 | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1afrC |
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Bound:FE2-FE2 | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1afrD |
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Bound:FE2-FE2 | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1afrE |
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Bound:FE2-FE2 | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1afrF |
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Bound:FE2-FE2 | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1oq4A |
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Bound:_FE-_FE | Analogue:AZI | Unbound | Unbound | Unbound | Unbound | ||
| 1oq4B |
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Bound:_FE-_FE | Analogue:AZI | Unbound | Unbound | Unbound | Unbound | ||
| 1oq4C |
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Bound:_FE-_FE | Analogue:AZI | Unbound | Unbound | Unbound | Unbound | ||
| 1oq4D |
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Bound:_FE-_FE | Analogue:AZI | Unbound | Unbound | Unbound | Unbound | ||
| 1oq4E |
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Bound:_FE-_FE | Analogue:AZI | Unbound | Unbound | Unbound | Unbound | ||
| 1oq4F |
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Bound:_FE-_FE | Analogue:AZI | Unbound | Unbound | Unbound | Unbound | ||
| 1oq7A |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1oq7B |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1oq7C |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1oq7D |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1oq7E |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1oq7F |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1oq9A |
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Bound:_FE-_FE | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1oqbA |
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Analogue:FE2 | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1oqbB |
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Analogue:FE2 | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1oqbC |
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Analogue:FE2 | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1oqbD |
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Analogue:FE2 | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1oqbE |
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Analogue:FE2 | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1oqbF |
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Analogue:FE2 | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| Reference for Active-site residues | ||
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| resource | references | E.C. |
| literature [1] | ||
| Active-site residues | ||||||||||
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| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1afrA |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1afrB |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1afrC |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1afrD |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1afrE |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1afrF |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1oq4A |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1oq4B |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1oq4C |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1oq4D |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1oq4E |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1oq4F |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1oq7A |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1oq7B |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1oq7C |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1oq7D |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1oq7E |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1oq7F |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1oq9A |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1oqbA |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1oqbB |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1oqbC |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1oqbD |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1oqbE |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| 1oqbF |
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TRP 62;HIS 146;THR 199;ASP 228 | GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2) | |||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[1]
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p.4086-4088 | |
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[7]
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Fig.5, Fig.6, p.423-425 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) |
| Medline ID | 97015109 |
| PubMed ID | 8861937 |
| Journal | EMBO J |
| Year | 1996 |
| Volume | 15 |
| Pages | 4081-92 |
| Authors | Lindqvist Y, Huang W, Schneider G, Shanklin J |
| Title | Crystal structure of delta9 stearoyl-acyl carrier protein desaturase from castor seed and its relationship to other di-iron proteins. |
| Related PDB | 1afr |
| Related UniProtKB | P22337 |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9144157 |
| Journal | Proc Natl Acad Sci U S A |
| Year | 1997 |
| Volume | 94 |
| Pages | 4872-7 |
| Authors | Cahoon EB, Lindqvist Y, Schneider G, Shanklin J |
| Title | Redesign of soluble fatty acid desaturases from plants for altered substrate specificity and double bond position. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9778341 |
| Journal | Biochemistry |
| Year | 1998 |
| Volume | 37 |
| Pages | 14664-71 |
| Authors | Broadwater JA, Ai J, Loehr TM, Sanders-Loehr J, Fox BG |
| Title | Peroxodiferric intermediate of stearoyl-acyl carrier protein delta 9 desaturase: oxidase reactivity during single turnover and implications for the mechanism of desaturation. |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9812895 |
| Journal | Science |
| Year | 1998 |
| Volume | 282 |
| Pages | 1315-7 |
| Authors | Broun P, Shanklin J, Whittle E, Somerville C |
| Title | Catalytic plasticity of fatty acid modification enzymes underlying chemical diversity of plant lipids. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11294879 |
| Journal | J Biol Chem |
| Year | 2001 |
| Volume | 276 |
| Pages | 21500-5 |
| Authors | Whittle E, Shanklin J |
| Title | Engineering delta 9-16:0-acyl carrier protein (ACP) desaturase specificity based on combinatorial saturation mutagenesis and logical redesign of the castor delta 9-18:0-ACP desaturase. |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | X|ray crystallography |
| Medline ID | |
| PubMed ID | 12704186 |
| Journal | J Biol Chem |
| Year | 2003 |
| Volume | 278 |
| Pages | 25072-80 |
| Authors | Moche M, Shanklin J, Ghoshal A, Lindqvist Y |
| Title |
Azide and acetate complexes plus two iron-depleted crystal structures of the di-iron enzyme delta9 stearoyl-acyl carrier protein desaturase. |
| Related PDB | 1oq4 1oq7 1oq9 1oqb |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 15260504 |
| Journal | Acc Chem Res |
| Year | 2004 |
| Volume | 37 |
| Pages | 421-9 |
| Authors | Fox BG, Lyle KS, Rogge CE |
| Title | Reactions of the diiron enzyme stearoyl-acyl carrier protein desaturase. |
| Related PDB | |
| Related UniProtKB | |
| [8] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 15667224 |
| Journal | Biochemistry |
| Year | 2005 |
| Volume | 44 |
| Pages | 1309-15 |
| Authors | Davydov R, Behrouzian B, Smoukov S, Stubbe J, Hoffman BM, Shanklin J |
| Title | Effect of substrate on the diiron(III) site in stearoyl acyl carrier protein delta 9-desaturase as disclosed by cryoreduction electron paramagnetic resonance/electron nuclear double resonance spectroscopy. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
|
This enzyme was transferred from E.C.1.14.99.6 to E.C. According to the literature [1], According to the literature [7], (A) Electron transfer from Ferredoxin to this enzyme active site; Oxidation of ferredoxin (protein). (B) Electron transfer from acyl-chain to diiron center, (C) O2 reduction to H2O at diiron center: O2 + 4 e(-) + 4 H(+) => 2 H2O The reaction proceeds as follows: (A) Electron transfer from Ferredoxin to this enzyme active site; Oxidation of ferredoxin (protein). (A1) Indirect transfer from [2Fe-2S] of ferredoxin to the diiron of active site of this enzyme through Trp62, |
| Created | Updated |
|---|---|
| 2004-01-26 | 2012-06-01 |