O13345
Gene name |
aflQ |
Protein name |
O-methylsterigmatocystin oxidoreductase |
Names |
OMST oxidoreductase, Aflatoxin B synthase, Aflatoxin biosynthesis protein Q, Cytochrome P450 64, Cytochrome P450 monooxygenase aflQ |
Species |
Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1) |
KEGG Pathway |
ag:AAS66031 |
EC number |
1.14.14.117: With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for O13345
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O13345-F1 | Predicted | AlphaFoldDB |
3 variants for O13345
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| 143 | A>S | strain: SRRC 2043 [UniProt] | No | ||
| 400 | H>L | strain: SRRC 2043; loss of activity [UniProt] | No | ||
| 528 | I>Y | strain: SRRC 2043 [UniProt] | No |
No associated diseases with O13345
1 regional properties for O13345
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Cytochrome P450, conserved site | 433 - 442 | IPR017972 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.14.14.117 | With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| aflatoxin B synthase activity | Catalyzes the reaction: 8-O-methylsterigmatocystin + 2 + 2 O(2) <=> aflatoxin B + 2 + H(2)O + methanol + CO(2). Produces both aflatoxin B(1) and aflatoxin B(2). |
| heme binding | Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. |
| iron ion binding | Binding to an iron (Fe) ion. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| aflatoxin biosynthetic process | The chemical reactions and pathways resulting in the formation of aflatoxin, a fungal metabolite found as a contaminant in moldy grains that induces liver cancer. Aflatoxin induces a G to T transversion at codon 249 of p53, leading to its inactivation. Aflatoxin is converted to a chemical carcinogen by P450. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MIYSIIICAG | ALLGFLILQK | LLAPKDTRPP | LPPGPWRKPI | IGNLTDFPPK | GTPEWLFWAK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| HHERYGPMSS | LEVMGQTIIM | INDAHLGIEI | MHKKSALSQM | IPDAPFAHMA | GWGMSLATER |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NKQAWKTIRA | NMKQEIGTRR | AIATFHPKME | IGIRRFLLRT | LDNPDDLRFH | IRKEANAFMM |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DVAYGYTIAP | HGKDELYDLT | QQSVRQFSHI | FSPGEWSVNF | FPILRYVPSW | FPGASFQIKA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AEYKRTIERM | TMVPYLWIKD | QVARGCTRPS | ILLRLLQKGH | YESGSHQEQV | LVWTNAEFVM |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GGSDTTVSAV | SSFFVAMALY | PEVQHQAREE | LDRVVGPTTL | ATFEHRSQLP | FIDALVKEVF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RWHPASPLGA | PHITQEDQIW | DGYLLPKGAL | LLPNIWTFTH | DPSVYHDPMV | FKPERFLERQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SSPPETDPMK | FVFGFGRRIC | PGRFVTDEKL | FLIACHAISC | FLISPKDPGA | PEPDWLPGVI |
| 490 | 500 | 510 | 520 | ||
| SQPGPFDLNV | VPRSPAHEEL | IRSIETDHPW | KNADATDISQ | FMARNQMI |