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 Q5E9N4

Entry ID Method Resolution Chain Position Source
AF-Q5E9N4-F1 Predicted AlphaFoldDB

No variants for Q5E9N4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5E9N4

No associated diseases with Q5E9N4

2 regional properties for Q5E9N4

Type Name Position InterPro Accession
domain Apoptosis-antagonizing transcription factor, C-terminal 464 - 548 IPR012617
domain AATF leucine zipper-containing domain 220 - 373 IPR025160

Functions

Description
EC Number 2.6.1.4 Transaminases
Subcellular Localization
  • Mitochondrion
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
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.

7 GO annotations of molecular function

Name Definition
2-aminoadipate transaminase activity Catalysis of the reaction: 2-oxoglutarate + L-2-aminoadipate = 2-oxoadipate + L-glutamate.
glycine:2-oxoglutarate aminotransferase activity Catalysis of the reaction: glycine + 2-oxoglutarate = glyoxylate + L-glutamate.
kynurenine-glyoxylate transaminase activity Catalysis of the reaction: L-kynurenine + glyoxylate = 4-(2-aminophenyl)-2,4-dioxobutanoate + glycine.
kynurenine-oxoglutarate transaminase activity Catalysis of the reaction: L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.
methionine-glyoxylate transaminase activity Catalysis of the reaction: L-methionine + glyoxylate = 4-methylthio-2-oxobutanoate + glycine.
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.
transaminase activity Catalysis of the transfer of an amino group to an acceptor, usually a 2-oxo acid.

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.
alpha-amino acid metabolic process The chemical reactions and pathways involving an alpha-amino 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.
kynurenine metabolic process The chemical reactions and pathways involving kynurenine, the amino acid 3-(2-aminobenzoyl)-alanine.
L-lysine catabolic process to acetyl-CoA via saccharopine The chemical reactions and pathways resulting in the breakdown of L-lysine into other compounds, including acetyl-CoA, via the intermediate saccharopine.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q8N5Z0 AADAT Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial Homo sapiens (Human) PR
Q9WVM8 Aadat Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial Mus musculus (Mouse) PR
10 20 30 40 50 60
MNYARFITAT SAARKPSTIR VMTEILSKAP KSVISLATGA PNPNTFPFKT AVITIENGKP
70 80 90 100 110 120
IQFNEQMMKR ALQYSQSAGI PELLSWLKQL QVKLHNPPTI HYAPTQGQMD LCVTCGSQEG
130 140 150 160 170 180
LCKVFEMIVN PGDNILVNEP IYSGTIHALQ PLGCNMINVS SDEHGIIPDS LREILSKWKP
190 200 210 220 230 240
EDSKNPKKNS PKFLYTVPNG NNPSGNSLTA ERKREIYELA RKYDFLIIED DPYYFMQFNK
250 260 270 280 290 300
PWAPTFLSMD EDGRVIRADS FSKVLSSGLR IGFITGPKPL IERIVLHIQV STMHPSTFAQ
310 320 330 340 350 360
LLVSQLLYQW GEEGFLGHVD RVIDFYRKQR DALMAAADKW LSGLAEWHVP TAGMFLWVKI
370 380 390 400 410 420
KGIHDVRKLI EEKAFKKEIF MLPGCGFYTD SSAPCPYFRA SFSSASPEQM DLAFQRLAQL
IKESL