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 Q9VW26

Entry ID Method Resolution Chain Position Source
AF-Q9VW26-F1 Predicted AlphaFoldDB

No variants for Q9VW26

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9VW26

No associated diseases with Q9VW26

No regional properties for Q9VW26

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q9VW26

Functions

Description
EC Number 2.6.1.13 Transaminases
Subcellular Localization
  • Mitochondrion matrix
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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.

4 GO annotations of molecular function

Name Definition
identical protein binding Binding to an identical protein or proteins.
ornithine(lysine) transaminase activity Catalysis of the reaction: 2-oxoglutarate + L-ornithine = H2O + L-glutamate + 3,4-dihydro-2H-pyrrole-2-carboxylate.
ornithine-oxo-acid transaminase activity Catalysis of the reaction: L-ornithine + a 2-oxo acid = L-glutamate 5-semialdehyde + an L-amino acid.
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.

4 GO annotations of biological process

Name Definition
arginine catabolic process to glutamate The chemical reactions and pathways resulting in the breakdown of arginine into other compounds, including glutamate.
arginine catabolic process to proline via ornithine The chemical reactions and pathways resulting in the breakdown of arginine into other compounds, including proline, via ornithine.
L-proline biosynthetic process The chemical reactions and pathways resulting in the formation of L-proline, an L-enantiomer of a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins.
ornithine metabolic process The chemical reactions and pathways involving ornithine, an amino acid only rarely found in proteins, but which is important in living organisms as an intermediate in the reactions of the urea cycle and in arginine biosynthesis.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MFAKLSARGI ATRMSFLAQK TASQETTAAA GSRSELVYAR ENKYGAHNYH PLPVALTKGE
70 80 90 100 110 120
GVFVWDVEGK RYFDYLSAYS AVNQGHCHPK IVAALTAQAS KLALTSRAFY SDVLGEYEEY
130 140 150 160 170 180
VTKLFGFDKV LPMNTGVEGG ETACKLARKW GYLEKKIPAN QAKIIFARNN FWGRTLSAVS
190 200 210 220 230 240
ASNDPSSYEG FGPFMPGFEL IEYDNVSALE ESLKDPNVCA FMVEPIQGEA GVVVPSDGYL
250 260 270 280 290 300
KKVRELCTKY NVLWIADEVQ TGLARTGKLL AVDYEQVQPD ILILGKALSG GMYPVSAVLC
310 320 330 340 350 360
NDQVMLCIKP GEHGSTYGGN PLGCRVAMAA LEVLQEEKLA ENAFKMGDLL RNELSTLPKD
370 380 390 400 410 420
VVSVVRGKGL LNAIVINQKF DAWEVCLRLK ENGLLAKPTH GDIIRFAPPL VINETQMRES
430
IDIIRKTILS M