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 B0RCQ8

Entry ID Method Resolution Chain Position Source
AF-B0RCQ8-F1 Predicted AlphaFoldDB

No variants for B0RCQ8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B0RCQ8

No associated diseases with B0RCQ8

5 regional properties for B0RCQ8

Type Name Position InterPro Accession
domain Pyruvate carboxyltransferase 40 - 317 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
MKSTQTPSGM PIHKYRPFHE QITVDLRDRT WPARRITEAP RWCAVDLRDG NQALIDPMSP
70 80 90 100 110 120
ERKRIMFNLL VRMGYKEIEV GFPSASQTDF DFVRSLIEEG AIPDDVTIQV LTQAREHLIA
130 140 150 160 170 180
RTYESIRGAK QAIVHLYNST SVLQREVVFR TDRQGIIDIA LEGARLCKRY EETIPETDVY
190 200 210 220 230 240
YEYSPESYTG TELEFAAEIC NRVVEVFDPT PERKVILNLP ATVEMATPNV YADSIEWMCR
250 260 270 280 290 300
HLDRRDEILV SLHPHNDRGT AVAAAELGYL AGADRIEGCL FGNGERTGNV DLVALGINLF
310 320 330 340 350 360
TQGIDPQIDF SDLDGIKRTA EHCNQLAVPE RSPWAGDLVY TAFSGSHQDA IKKGFEAMAV
370 380 390 400 410 420
DAAAQGVTVD DIPWAVPYLP VDPQDLGRSY EAVIRVNSQS GKGGVAYLLK ADHSLDLPRR
430 440 450 460 470 480
LQIEFSGVVQ AKTDAEGGEV TSAQIWSVFQ DEYLPAPLDR VEEKWGRFEL TSTRTSSDMG
490 500 510 520 530 540
GSVSLDVVLR DGDEVREASA SGNGPIAAFL QVLADQGVEV RLLDYVEHAL SASGDALAAS
550 560 570 580
YVELEVEGVR LWGVGIDEDS STASLEAIVS GVNRAIRRTV REPELAAV