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 A4YF03

Entry ID Method Resolution Chain Position Source
AF-A4YF03-F1 Predicted AlphaFoldDB

No variants for A4YF03

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A4YF03

No associated diseases with A4YF03

3 regional properties for A4YF03

Type Name Position InterPro Accession
domain Aconitase/3-isopropylmalate dehydratase large subunit, alpha/beta/alpha domain 21 - 406 IPR001030
binding_site Aconitase family, 4Fe-4S cluster binding site 347 - 360 IPR018136
domain 3-Isopropylmalate dehydratase, catalytic domain 30 - 408 IPR033941

Functions

Description
EC Number 4.2.1.33 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
3-isopropylmalate dehydratase activity Catalysis of the reaction: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate.
4 iron, 4 sulfur cluster binding Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
metal ion binding Binding to a metal ion.

1 GO annotations of biological process

Name Definition
leucine biosynthetic process The chemical reactions and pathways resulting in the formation of leucine, 2-amino-4-methylpentanoic acid.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTGTLTEKIL SRASGKTVSP GDVIEAKTDI VAFHDLTGYH VIEVMEKANM MKIFDKTKIV
70 80 90 100 110 120
VAFDHLAPPP DVRSAEIQGN IRKFVKEMRL PNFHDINVGI LHELLIEQYA LPGQVIVAAD
130 140 150 160 170 180
SHTTTSGAVG AFAQGMGASD VAAAVITGKT WLVVPQPFKV TLKGNPGKWI NGKDVALELL
190 200 210 220 230 240
GKFKADYFNG MSIEVHVENP KAFPMDYRAT VSNMGIEMNA DALMFVPDVE TKDYIKTMRG
250 260 270 280 290 300
KEVELVTPDP GAKYLDEHTI ELDKLEPLVA APYSVDNVKT AREESKVPVD QVYIGSCTNG
310 320 330 340 350 360
RLSDFRIASE ILKGKKVKTR CIAIPSSYTM FKQAMEMGYI EDLVNAGCVV TYGTCGPCLG
370 380 390 400 410
GHFGVAGPGE VIVSTSSRNF RGRMGSNEAK VYLSGPSVAA ASAATGYITD PRDVQ