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 P58888

Entry ID Method Resolution Chain Position Source
AF-P58888-F1 Predicted AlphaFoldDB

No variants for P58888

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P58888

No associated diseases with P58888

3 regional properties for P58888

Type Name Position InterPro Accession
domain Oxidoreductase FAD/NAD(P)-binding 94 - 180 IPR001433
domain FAD-binding domain, ferredoxin reductase-type 1 - 87 IPR017927
domain Dihydroorotate dehydrogenase, electron transfer subunit, iron-sulphur cluster binding domain 196 - 228 IPR019480

Functions

Description
EC Number
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

4 GO annotations of molecular function

Name Definition
2 iron, 2 sulfur cluster binding Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands.
electron transfer activity Any molecular entity that serves as an electron acceptor and electron donor in an electron transport chain. An electron transport chain is a process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
flavin adenine dinucleotide binding Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
metal ion binding Binding to a metal ion.

1 GO annotations of biological process

Name Definition
'de novo' UMP biosynthetic process The chemical reactions and pathways resulting in the formation of UMP, uridine monophosphate, starting with the synthesis of (S)-dihydroorotate from bicarbonate; UMP biosynthesis may either occur via reduction by quinone, NAD(+) or oxygen.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLRRVSIEET WEVAKNIKAF RLSEKLEFTP GQFIMLWLPG VEEKPLSLAD KNLIMVKKVG
70 80 90 100 110 120
RFTNELFKLK EGDYVWIRGP YGHGFSGKGK SVALIAGGIG IPPIYALAKY GNFKRSILIY
130 140 150 160 170 180
GARTKEEIAL PKDIESYVDE VIITTDDGSY GIKGFPTDVL MERRSEFDYV YACGPEIMLA
190 200 210 220 230 240
KILEIMEFEN VEVSAERYMK CGIGVCGSCA LGPYLVCRDG PVFSGKQLIN TEFGKYSRTP
DGRIKPL