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 P12345

Entry ID Method Resolution Chain Position Source
AF-P12345-F1 Predicted AlphaFoldDB

No variants for P12345

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P12345

No associated diseases with P12345

2 regional properties for P12345

Type Name Position InterPro Accession
binding_site Aminotransferases, class-I, pyridoxal-phosphate-binding site 276 - 289 IPR004838
domain Aminotransferase, class I/classII 58 - 425 IPR004839

Functions

Description
EC Number 2.6.1.1 Transaminases
Subcellular Localization
  • Mitochondrion matrix
  • Cell membrane
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
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.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

3 GO annotations of molecular function

Name Definition
kynurenine-oxoglutarate transaminase activity Catalysis of the reaction: L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.
L-aspartate:2-oxoglutarate aminotransferase activity Catalysis of the reaction: L-aspartate + 2-oxoglutarate = oxaloacetate + 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.

6 GO annotations of biological process

Name Definition
2-oxoglutarate metabolic process The chemical reactions and pathways involving oxoglutarate, the dianion of 2-oxoglutaric acid. It is a key constituent of the TCA cycle and a key intermediate in amino-acid metabolism.
aspartate metabolic process The chemical reactions and pathways involving aspartate, the anion derived from aspartic acid, 2-aminobutanedioic acid.
biosynthetic process The chemical reactions and pathways resulting in the formation of substances; typically the energy-requiring part of metabolism in which simpler substances are transformed into more complex ones.
glutamate metabolic process The chemical reactions and pathways involving glutamate, the anion of 2-aminopentanedioic acid.
lipid transport The directed movement of lipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Lipids are compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent.
protein folding The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MALLHSARVL SGVASAFHPG LAAAASARAS SWWAHVEMGP PDPILGVTEA YKRDTNSKKM
70 80 90 100 110 120
NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK GLDKEYLPIG GLAEFCRASA ELALGENSEV
130 140 150 160 170 180
VKSGRFVTVQ TISGTGALRI GASFLQRFFK FSRDVFLPKP SWGNHTPIFR DAGMQLQSYR
190 200 210 220 230 240
YYDPKTCGFD FTGALEDISK IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA TVVKKRNLFA
250 260 270 280 290 300
FFDMAYQGFA SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTVICKDADE
310 320 330 340 350 360
AKRVESQLKI LIRPMYSNPP IHGARIASTI LTSPDLRKQW LQEVKGMADR IIGMRTQLVS
370 380 390 400 410 420
NLKKEGSTHS WQHITDQIGM FCFTGLKPEQ VERLTKEFSI YMTKDGRISV AGVTSGNVGY
LAHAIHQVTK