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 O53182

Entry ID Method Resolution Chain Position Source
AF-O53182-F1 Predicted AlphaFoldDB

No variants for O53182

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O53182

No associated diseases with O53182

No regional properties for O53182

Type Name Position InterPro Accession
No domain, repeats, and functional sites for O53182

Functions

Description
EC Number 1.2.7.3 With an iron-sulfur protein as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
peptidoglycan-based cell wall A protective structure outside the cytoplasmic membrane composed of peptidoglycan (also known as murein), a molecule made up of a glycan (sugar) backbone of repetitively alternating N-acetylglucosamine and N-acetylmuramic acid with short, attached, cross-linked peptide chains containing unusual amino acids. An example of this component is found in Escherichia coli.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

2 GO annotations of molecular function

Name Definition
2-oxoglutarate synthase activity Catalysis of the reaction: 2-oxoglutarate + CoA + oxidized ferredoxin = succinyl-CoA + CO2 + reduced ferredoxin.
magnesium ion binding Binding to a magnesium (Mg) ion.

2 GO annotations of biological process

Name Definition
response to oxidative stress Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.
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
MDPNGSGAGP ESHDAAFHAA PDRQRLENVV IRFAGDSGDG MQLTGDRFTS EAALFGNDLA
70 80 90 100 110 120
TQPNYPAEIR APAGTLPGVS SFQIQIADYD ILTAGDRPDV LVAMNPAALK ANIGDLPLGG
130 140 150 160 170 180
MVIVNSDEFT KRNLTKVGYV TNPLESGELS DYVVHTVAMT TLTLGAVEAI GASKKDGQRA
190 200 210 220 230 240
KNMFALGLLS WMYGRELEHS EAFIREKFAR KPEIAEANVL ALKAGWNYGE TTEAFGTTYE
250 260 270 280 290 300
IPPATLPPGE YRQISGNTAL AYGIVVAGQL AGLPVVLGSY PITPASDILH ELSKHKNFNV
310 320 330 340 350 360
VTFQAEDEIG GICAALGAAY GGALGVTSTS GPGISLKSEA LGLGVMTELP LLVIDVQRGG
370 380 390 400 410 420
PSTGLPTKTE QADLLQALYG RNGESPVAVL APRSPADCFE TALEAVRIAV SYHTPVILLS
430 440 450 460 470 480
DGAIANGSEP WRIPDVNALP PIKHTFAKPG EPFQPYARDR ETLARQFAIP GTPGLEHRIG
490 500 510 520 530 540
GLEAANGSGD ISYEPTNHDL MVRLRQAKID GIHVPDLEVD DPTGDAELLL IGWGSSYGPI
550 560 570 580 590 600
GEACRRARRR GTKVAHAHLR YLNPFPANLG EVLRRYPKVV APELNLGQLA QVLRGKYLVD
610 620 630 640 650
VQSVTKVKGV SFLADEIGRF IRAALAGRLA ELEQDKTLVA RLSAATAGAG ANG