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 H8F3R6

Entry ID Method Resolution Chain Position Source
AF-H8F3R6-F1 Predicted AlphaFoldDB

No variants for H8F3R6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for H8F3R6

No associated diseases with H8F3R6

2 regional properties for H8F3R6

Type Name Position InterPro Accession
domain Peptide chain release factor class I 228 - 335 IPR000352
domain Peptide chain release factor 29 - 218 IPR005139

Functions

Description
EC Number 4.1.3.1 Oxo-acid-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
isocitrate lyase activity Catalysis of the reaction: isocitrate = glyoxylate + succinate.
metal ion binding Binding to a metal ion.
methylisocitrate lyase activity Catalysis of the reaction: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate.

2 GO annotations of biological process

Name Definition
glyoxylate cycle A modification of the TCA cycle occurring in some plants and microorganisms, in which isocitrate is cleaved to glyoxylate and succinate. Glyoxylate can then react with acetyl-CoA to form malate.
tricarboxylic acid cycle A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAIAETDTEV HTPFEQDFEK DVAATQRYFD SSRFAGIIRL YTARQVVEQR GTIPVDHIVA
70 80 90 100 110 120
REAAGAFYER LRELFAARKS ITTFGPYSPG QAVSMKRMGI EAIYLGGWAT SAKGSSTEDP
130 140 150 160 170 180
GPDLASYPLS QVPDDAAVLV RALLTADRNQ HYLRLQMSER QRAATPAYDF RPFIIADADT
190 200 210 220 230 240
GHGGDPHVRN LIRRFVEVGV PGYHIEDQRP GTKKCGHQGG KVLVPSDEQI KRLNAARFQL
250 260 270 280 290 300
DIMRVPGIIV ARTDAEAANL IDSRADERDQ PFLLGATKLD VPSYKSCFLA MVRRFYELGV
310 320 330 340 350 360
KELNGHLLYA LGDSEYAAAG GWLERQGIFG LVSDAVNAWR EDGQQSIDGI FDQVESRFVA
370 380 390 400 410 420
AWEDDAGLMT YGEAVADVLE FGQSEGEPIG MAPEEWRAFA ARASLHAARA KAKELGADPP
430 440 450 460 470 480
WDCELAKTPE GYYQIRGGIP YAIAKSLAAA PFADILWMET KTADLADARQ FAEAIHAEFP
490 500 510 520 530 540
DQMLAYNLSP SFNWDTTGMT DEEMRRFPEE LGKMGFVFNF ITYGGHQIDG VAAEEFATAL
550 560 570 580 590 600
RQDGMLALAR LQRKMRLVES PYRTPQTLVG GPRSDAALAA SSGRTATTKA MGKGSTQHQH
610 620 630 640 650 660
LVQTEVPRKL LEEWLAMWSG HYQLKDKLRV QLRPQRAGSE VLELGIHGES DDKLANVIFQ
670 680 690 700 710 720
PIQDRRGRTI LLVRDQNTFG AELRQKRLMT LIHLWLVHRF KAQAVHYVTP TDDNLYQTSK
730 740 750 760
MKSHGIFTEV NQEVGEIIVA EVNHPRIAEL LTPDRVALRK LITKEA