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 A3MUK8

Entry ID Method Resolution Chain Position Source
AF-A3MUK8-F1 Predicted AlphaFoldDB

No variants for A3MUK8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A3MUK8

No associated diseases with A3MUK8

2 regional properties for A3MUK8

Type Name Position InterPro Accession
conserved_site Dihydroxy-acid/6-phosphogluconate dehydratase, conserved site 124 - 134 IPR020558-1
conserved_site Dihydroxy-acid/6-phosphogluconate dehydratase, conserved site 466 - 477 IPR020558-2

Functions

Description
EC Number 4.2.1.9 Hydro-lyases
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

3 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.
dihydroxy-acid dehydratase activity Catalysis of the reaction: 2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O.
magnesium ion binding Binding to a magnesium (Mg) ion.

2 GO annotations of biological process

Name Definition
isoleucine biosynthetic process The chemical reactions and pathways resulting in the formation of isoleucine, (2R*,3R*)-2-amino-3-methylpentanoic acid.
valine biosynthetic process The chemical reactions and pathways resulting in the formation of valine, 2-amino-3-methylbutanoic acid.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MVRVRIRSPS WYDGVDNAPH RVYLRAVGFT EEDFSKPLVG VAVSWSELGP CNYHTLELAR
70 80 90 100 110 120
YVKEGVKEAG GAALAAPTIV VNDGINMGTP GMRYSLISRE LIADSIEAQF NAHGVDAWVG
130 140 150 160 170 180
IGGCDKTQPG IIMAMVRLNL PSVYLYGGSA EAGWLGEREL TVEDVFEAVG AYYAGRITLE
190 200 210 220 230 240
ELKRVEELSF PTYGTCQGMF TANTMALLAE AMGVSLLGSA TPPATSARRR KFAVESGKAA
250 260 270 280 290 300
VRALELGIKP RDVVTYDALY NAAVALFATA GSTNAILHLL AIAHEAGVKF ALEDFDKIGK
310 320 330 340 350 360
RVPVIAALRP AGPYAMQDLD RVGGVPRLLK KLYKAGLLRG EALTVEGEPI GKLLERWEPP
370 380 390 400 410 420
AVPEAGVLYD VDRPYKPHGG IRILWGNLAP RGAVMKIGAA EVLKFEGKAL VFDGEAEAFK
430 440 450 460 470 480
AVAAGEVKPG HVVVIRYEGP KGAPGMPEML KVTAAIVGAG LGESVALVTD GRFSGATRGI
490 500 510 520 530 540
MVGHVAPEAA AGGPIALVEN GDRIVIDGEA GLLKLDVSDE ELERRRRQWT PPPPKYKGGL
550 560
LAKYAALVSQ ADQGAVTTPE TCQC