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 A9WML8

Entry ID Method Resolution Chain Position Source
AF-A9WML8-F1 Predicted AlphaFoldDB

No variants for A9WML8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A9WML8

No associated diseases with A9WML8

5 regional properties for A9WML8

Type Name Position InterPro Accession
domain Pyruvate carboxyltransferase 40 - 320 IPR000891
conserved_site Alpha-isopropylmalate/homocitrate synthase, conserved site 47 - 63 IPR002034-1
conserved_site Alpha-isopropylmalate/homocitrate synthase, conserved site 250 - 263 IPR002034-2
domain 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain 439 - 576 IPR013709
domain LeuA, N-terminal catalytic TIM barrel domain 39 - 322 IPR039371

Functions

Description
EC Number 2.3.3.13 Acyl groups converted into alkyl groups on transfer
Subcellular Localization
  • Cytoplasm
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

1 GO annotations of molecular function

Name Definition
2-isopropylmalate synthase activity Catalysis of the reaction: 3-methyl-2-oxobutanoate + acetyl-CoA + H(2)O = (2S)-2-isopropylmalate + CoA + H(+).

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
MRNAQKPSGM PVHRYLPFHE QIEVELPDRT WPTKRITTAP RWCAVDLRDG NQALIDPMSP
70 80 90 100 110 120
ARKLKMFELL VKMGYKEIEV GFPSASQTDF DFVRQLIQGG HIPEDVTIQV LTQAREHLIE
130 140 150 160 170 180
RTYESLVGAK QAIVHLYNST SVLQRRVVFN EDQDGIMALA TQGALLCKKY QETLTDTKIT
190 200 210 220 230 240
YEYSPESFTG TELDYAVRVC NAVADIFEAS ADNQVIVNLP ATVEMITPNV YADSIEWMSH
250 260 270 280 290 300
NLHPREGIIL SLHPHNDRGT GVAAAELGYL AGADRIEGCL FGNGERAGNV DLVTLGLNMF
310 320 330 340 350 360
SQGVDPMIDF SDIDEIRRTV EYCNQLPAPE RMPYGGDLVF TAFSGSHQDA IKKGFEALER
370 380 390 400 410 420
DADAAGIAVA DTVWAVPYLP VDPKDLGRSY EAVIRVNSQS GKGGVAYLLK SEHSLDLPRR
430 440 450 460 470 480
AQIEFSGVIQ RRTDSVGGEV SADQRWEAFT DEYLPSPAGH PGGQWGRYAL GSMNADTEED
490 500 510 520 530 540
GTTKLNTAMR IDGVEQRRSG SGNGPIAALL NILHDDGVDV RVLDYSEHAL SEGGNASAAS
550 560 570 580
YVECAVGDRV LWGLGIDPNT TVSSLKAVIS AVNRAIRDNQ VD