P47039
Gene name |
BNA3 (YJL060W, J1138) |
Protein name |
Probable kynurenine--oxoglutarate transaminase BNA3 |
Names |
Biosynthesis of nicotinic acid protein 3, Kynurenine aminotransferase |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YJL060W |
EC number |
2.6.1.7: Transaminases |
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
2 structures for P47039
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 3B46 | X-ray | 200 A | A/B | 1-444 | PDB |
| AF-P47039-F1 | Predicted | AlphaFoldDB |
4 variants for P47039
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s10-323632 | 84 | M>I | No | SGRP | |
| s10-323876 | 166 | V>L | No | SGRP | |
| s10-323919 | 180 | R>K | No | SGRP | |
| s10-323970 | 197 | S>F | No | SGRP |
No associated diseases with P47039
Functions
| Description | ||
|---|---|---|
| EC Number | 2.6.1.7 | Transaminases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| 2-aminoadipate transaminase activity | Catalysis of the reaction: 2-oxoglutarate + L-2-aminoadipate = 2-oxoadipate + L-glutamate. |
| kynurenine-oxoglutarate transaminase activity | Catalysis of the reaction: L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate. |
| pyridoxal phosphate binding | Binding to pyridoxal 5' phosphate, 3-hydroxy-5-(hydroxymethyl)-2-methyl4-pyridine carboxaldehyde 5' phosphate, the biologically active form of vitamin B6. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| kynurenic acid biosynthetic process | The chemical reactions and pathways resulting in the formation of kynurenic acid, 4-hydroxyquinoline-2-carboxylic acid. |
| L-kynurenine catabolic process | The chemical reactions and pathways resulting in the breakdown of L-kynurenine, the L-enantiomer of the amino acid kynurenine (3-(2-aminobenzoyl)-alanine). |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKQRFIRQFT | NLMSTSRPKV | VANKYFTSNT | AKDVWSLTNE | AAAKAANNSK | NQGRELINLG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QGFFSYSPPQ | FAIKEAQKAL | DIPMVNQYSP | TRGRPSLINS | LIKLYSPIYN | TELKAENVTV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TTGANEGILS | CLMGLLNAGD | EVIVFEPFFD | QYIPNIELCG | GKVVYVPINP | PKELDQRNTR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GEEWTIDFEQ | FEKAITSKTK | AVIINTPHNP | IGKVFTREEL | TTLGNICVKH | NVVIISDEVY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EHLYFTDSFT | RIATLSPEIG | QLTLTVGSAG | KSFAATGWRI | GWVLSLNAEL | LSYAAKAHTR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ICFASPSPLQ | EACANSINDA | LKIGYFEKMR | QEYINKFKIF | TSIFDELGLP | YTAPEGTYFV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LVDFSKVKIP | EDYPYPEEIL | NKGKDFRISH | WLINELGVVA | IPPTEFYIKE | HEKAAENLLR |
| 430 | 440 | ||||
| FAVCKDDAYL | ENAVERLKLL | KDYL |