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 Q98LB3

Entry ID Method Resolution Chain Position Source
AF-Q98LB3-F1 Predicted AlphaFoldDB

No variants for Q98LB3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q98LB3

No associated diseases with Q98LB3

2 regional properties for Q98LB3

Type Name Position InterPro Accession
conserved_site Dihydroxy-acid/6-phosphogluconate dehydratase, conserved site 141 - 151 IPR020558-1
conserved_site Dihydroxy-acid/6-phosphogluconate dehydratase, conserved site 481 - 492 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
MRQAAPPAAR MRMDAKVISK AKLPSRHVTV GPARAPHRSY LYAMGLSAAE IAQPLVGVAS
70 80 90 100 110 120
CWNEAAPCNI SLMRQAQVVK KGVAAANGTP REFCTITVTD GIAMGHQGMK SSLVSREVIA
130 140 150 160 170 180
DSVELTMRGH CYDALVGLAG CDKSLPGMMM AMVRLNVPSI FIYGGSILPG SYRGRQITVQ
190 200 210 220 230 240
DVFEAVGQHS VGTIGDAELL EIEQAACPSA GSCGAQFTAN TMATVAEAIG LALPYSCGAP
250 260 270 280 290 300
APYEMRDRFN FASGEKIMEL IAKNIRPRDI ITLKALENAA TVVSATGGST NAALHLPAIA
310 320 330 340 350 360
HEAGIKFDLF DVARIFEKTP YIADLKPGGK YVAKDMFEAG GIPLLMKTLL DHGYLHGDCL
370 380 390 400 410 420
TVTGRTLAEN MEHVAWNEHQ DVVRPANRPI TQTGGVVGLK GNLAPEGAIV KVAGMTELKF
430 440 450 460 470 480
SGPARCFDSE EECFEAVTQR NYREGEVLVI RYEGPRGGPG MREMLSTTAA LYGQGMGGKV
490 500 510 520 530 540
ALITDGRFSG ATRGFCIGHV GPEAAVGGPI GLIRDGDVIS IDAVNGTIEV ALSDSELAAR
550 560 570 580
AKTWKARTTD YQSGAIWKYA QTVGSARDGA VTHPGGAKET HCYADI