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 A4W925

Entry ID Method Resolution Chain Position Source
AF-A4W925-F1 Predicted AlphaFoldDB

No variants for A4W925

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A4W925

1 associated diseases with A4W925

[MIM: 614462]: Hyperglycinemia, lactic acidosis, and seizures (HGCLAS)

An enzymatic defect resulting in an autosomal recessive disorder of mitochondrial metabolism. It is characterized by early-onset lactic acidosis, severe encephalomyopathy, and a pyruvate oxidation defect. Affected individuals have neonatal-onset epilepsy, poor growth, psychomotor retardation, muscular hypotonia, lactic acidosis, and elevated glycine concentration in plasma and urine. {ECO:0000269|PubMed:22152680}. Note=The disease is caused by variants affecting the gene represented in this entry.

Without disease ID
  • An enzymatic defect resulting in an autosomal recessive disorder of mitochondrial metabolism. It is characterized by early-onset lactic acidosis, severe encephalomyopathy, and a pyruvate oxidation defect. Affected individuals have neonatal-onset epilepsy, poor growth, psychomotor retardation, muscular hypotonia, lactic acidosis, and elevated glycine concentration in plasma and urine. {ECO:0000269|PubMed:22152680}. Note=The disease is caused by variants affecting the gene represented in this entry.

3 regional properties for A4W925

Type Name Position InterPro Accession
domain Elp3/MiaA/NifB-like, radical SAM core domain 127 - 333 IPR006638
domain Radical SAM 67 - 362 IPR007197
domain Lipoyl synthase, N-terminal 4 - 111 IPR031691

Functions

Description
EC Number 1.14.99.46 Miscellaneous
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
monooxygenase activity Catalysis of the incorporation of one atom from molecular oxygen into a compound and the reduction of the other atom of oxygen to water.
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from each of two donors, and molecular oxygen is reduced or incorporated into a donor.
uracil oxygenase activity Catalysis of the reaction: uracil + NADH + O2 + H+ = ureidoacrylate peracid + NAD+. Ureidoacrylate peracid is spontaneously reduced by NADH to form ureidoacrylate.

2 GO annotations of biological process

Name Definition
nitrogen utilization A series of processes that forms an integrated mechanism by which a cell or an organism detects the depletion of primary nitrogen source, usually ammonia, and then activates genes to scavenge the last traces of the primary nitrogen source and to transport and metabolize alternative nitrogen sources. The utilization process begins when the cell or organism detects nitrogen levels, includes the activation of genes whose products detect, transport or metabolize nitrogen-containing substances, and ends when nitrogen is incorporated into the cell or organism's metabolism.
uracil catabolic process The chemical reactions and pathways resulting in the breakdown of uracil, 2,4-dioxopyrimidine, one of the pyrimidine bases occurring in RNA, but not in DNA.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKIGVFVPIG NNGWLISTTA PQYMPTFELN KAIVQKAEHY HFDFALSMIK LRGFGGKTEF
70 80 90 100 110 120
WDHNLESFTL MAGLAAVTSR IQIYATAATL TLPPAIVARM ASTIDSISGG RFGVNLVTGW
130 140 150 160 170 180
QKPEYDQMGI WPGDEYFSRR YDYLTEYVQV LRDLWGTGKS DFKGDYFTMN DCRVSPQPST
190 200 210 220 230 240
PMKVICAGQS DAGMAFSAQH ADFNFCFGKG VNTPAAFAPT AARMKDAAEK TGRDVGSYVL
250 260 270 280 290 300
FMVIADETDE AARAKWEHYK AGADEDALSW LTEQSQKDTR SGADTNVRQM ADPTSAVNIN
310 320 330 340 350 360
MGTLVGSYAS VAKMLDEVAS VPGAEGVLLT FDDFLQGVET FGERIQPLME CRSHIPAVTR
EVA