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

4 structures for O07566

Entry ID Method Resolution Chain Position Source
4K2B X-ray 231 A A/B 1-441 PDB
4K2I X-ray 222 A A/B 1-441 PDB
4K2M X-ray 171 A A/B 1-441 PDB
AF-O07566-F1 Predicted AlphaFoldDB

No variants for O07566

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O07566

No associated diseases with O07566

No regional properties for O07566

Type Name Position InterPro Accession
No domain, repeats, and functional sites for O07566

Functions

Description
EC Number 2.6.1.104 Transaminases
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

2 GO annotations of molecular function

Name Definition
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.

2 GO annotations of biological process

Name Definition
antibiotic biosynthetic process The chemical reactions and pathways resulting in the formation of an antibiotic, a substance produced by or derived from certain fungi, bacteria, and other organisms, that can destroy or inhibit the growth of other microorganisms.
polysaccharide biosynthetic process The chemical reactions and pathways resulting in the formation of a polysaccharide, a polymer of many (typically more than 10) monosaccharide residues linked glycosidically.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MQKQVKISGK SKENMSLLKH LKGDVQGKEL VIEDSIVNER WKQVLKEKID IEHDLFNYQK
70 80 90 100 110 120
NREISKVPFL PVDRLITNDE VEDILNTLTE VLPTGKFTSG PYLEQFEKVL STYLHKRYVI
130 140 150 160 170 180
ATSSGTDAIM IGLLALGLNP GDEVIMPANS FSATENAVLA SGGVPIYVDI NPQTFCIDPD
190 200 210 220 230 240
KIEEAITPYT KFILPVHLYG KHSDMQHIRQ IANRYKLKVI EDACQGIGLT DLGKYADITT
250 260 270 280 290 300
LSFNPYKNFG VCGKAGAIAT DNEELAKKCI QFSYHGFEVN VKNKKVINFG FNSKMDNLQA
310 320 330 340 350 360
AIGLERMKYL SLNNFKRLFL ADRYITQLAE LQNKGYIELP ELSEDHVWHL FPIKVRTEDR
370 380 390 400 410 420
ADIMTKLNED FGVQTDVYYP ILSHMQKTPL VQDKYAGLQL VHTEKAHSQV LHLPLYPSFT
430 440
LEEQDRVMEG LFHVIKQEIG V