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 D7UQ40

Entry ID Method Resolution Chain Position Source
AF-D7UQ40-F1 Predicted AlphaFoldDB

No variants for D7UQ40

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for D7UQ40

No associated diseases with D7UQ40

2 regional properties for D7UQ40

Type Name Position InterPro Accession
domain FAD linked oxidase, N-terminal 95 - 228 IPR006094
domain FAD-binding domain, PCMH-type 91 - 261 IPR016166

Functions

Description
EC Number 1.1.3.42 With oxygen as acceptor
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
FAD binding Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
isomerase activity Catalysis of the geometric or structural changes within one molecule. Isomerase is the systematic name for any enzyme of EC class 5.
oxidoreductase activity Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MRLIILNLLS LGITPSVVGH SGPHRQETQN LNNFLESNAI NPAAINGETR HTGGVHLACA
70 80 90 100 110 120
ILEASNQTAV VFPSDGELYT QIDKAHASAT APKNPACIYT PNDVKGVSLG VKVATFVQAK
130 140 150 160 170 180
FAIRSGGHSP MEYFANIDGG VLISLAGIKT LEYNADTQTQ RSGFGNLWQD VYRHVNAQGR
190 200 210 220 230 240
TVVGGRTGSV GLALTLGGGL SHFSNAYGWA AQNVLSYEMV LADGSIVIAS EEENSDLYFA
250 260 270 280 290 300
VKAGANNFGI VTHIVQRTYP LGKIWGGSMI FPGNASAQFM AALADYQAKG QLDKKSAILP
310 320 330 340 350 360
YVGLIADAVV AQFSYLEPVE RPEAFEAFYD IPVIQDLTQV WDTFAAMVTA PIPYNMTRFS
370 380 390 400 410 420
YATTDLLYDK EAYLEIERIC HKYIPRMRKL EGGDIMLMPQ PISVSMVGEA RARGSDPMGV
430 440 450 460 470 480
ADQPQLWFVV SSGWNLAQDD AEAESIMLDA LAEVEEYTKS RALHLPFYFL NDAFSTQMPL
490 500 510
QSYGAVTYGK LQAASRKYDP TRVFQELVPG GFKLV