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 Q8EEU9

Entry ID Method Resolution Chain Position Source
AF-Q8EEU9-F1 Predicted AlphaFoldDB

No variants for Q8EEU9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8EEU9

No associated diseases with Q8EEU9

2 regional properties for Q8EEU9

Type Name Position InterPro Accession
domain Aminotransferase class V domain 5 - 367 IPR000192
binding_site Aminotransferase class-V, pyridoxal-phosphate binding site 197 - 216 IPR020578

Functions

Description
EC Number 2.8.1.7 Sulfurtransferases
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

4 GO annotations of molecular function

Name Definition
2 iron, 2 sulfur cluster binding Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
cysteine desulfurase activity Catalysis of the reaction: L-cysteine
metal ion binding +Binding to a metal ion.
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.

1 GO annotations of biological process

Name Definition
[2Fe-2S] cluster assembly The incorporation of two iron atoms and two sulfur atoms into an iron-sulfur cluster.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKLPIYLDYA ATTPVDPRVA EKMFQYMTMD GIFGNPASRS HRYGWQAEEA VDVARNQVAD
70 80 90 100 110 120
LINADHREIV FTSGATESNN LAIKGVAHFY KKKGKHIITS KTEHKAVLDT CRQLEREGFE
130 140 150 160 170 180
VTYLEPESNG IIPMARLEAA MRDDTILVSI MHVNNEIGVI HDIDAIGELC RSKGIIFHMD
190 200 210 220 230 240
AAQSAGKLPI DVQATKVDLI SISGHKMYGP KGIGALYVRR KPRIRLEAQM HGGGHERGMR
250 260 270 280 290 300
SGTLPTHQIV GLGEASAIAK AEMATDNVRI AKLRDKLWNG IKHIEETYVN GDMNQRTSGS
310 320 330 340 350 360
LNVSFNYVEG ESLMMALKDL AVSSGSACTS ASLEPSYVLR ALGLNDEMAH SSIRFSIGRF
370 380 390 400
TTEEEIDHAI EVITQSIDKL REMSPLWEMF KDGIDLNQVQ WAHH