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 P58710

Entry ID Method Resolution Chain Position Source
AF-P58710-F1 Predicted AlphaFoldDB

20 variants for P58710

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389338034 2 V>* No EVA
rs3389292175 13 W>* No EVA
rs3389338020 56 P>L No EVA
rs3389340607 58 D>Y No EVA
rs3389262060 90 G>D No EVA
rs3389353476 99 Q>* No EVA
rs3389328709 119 G>S No EVA
rs3389353477 127 H>Y No EVA
rs31067467 151 T>A No EVA
rs219467087 153 L>V No EVA
rs3389301529 203 L>I No EVA
rs3389309848 268 R>E* No EVA
rs3389338037 270 V>G No EVA
rs3389344521 285 K>N No EVA
rs3389342007 373 D>E No EVA
rs3389332598 429 M>K No EVA
rs3389335370 429 M>L No EVA
rs3405211060 430 F>* No EVA
rs3404977929 441 Y>L No EVA
rs3405301332 441 Y>Y No EVA

No associated diseases with P58710

4 regional properties for P58710

Type Name Position InterPro Accession
binding_site Oxygen oxidoreductase covalent FAD-binding site 21 - 54 IPR006093
domain FAD linked oxidase, N-terminal 21 - 156 IPR006094
domain D-arabinono-1,4-lactone oxidase, C-terminal domain 180 - 437 IPR007173
domain FAD-binding domain, PCMH-type 17 - 187 IPR016166

Functions

Description
EC Number 1.1.3.8 With oxygen as acceptor
Subcellular Localization
  • Microsome membrane ; Single-pass membrane protein
  • Endoplasmic reticulum membrane ; Single-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

5 GO annotations of molecular function

Name Definition
D-arabinono-1,4-lactone oxidase activity Catalysis of the reaction: D-arabinono-1,4-lactone + O(2) = dehydro-D-arabinono-1,4-lactone + H(2)O(2) + H(+).
FAD binding Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
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.
L-gulonolactone oxidase activity Catalysis of the reaction: L-gulono-1,4-lactone + O2 = L-xylo-hex-3-ulonolactone + H2O2.
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.

1 GO annotations of biological process

Name Definition
L-ascorbic acid biosynthetic process The chemical reactions and pathways resulting in the formation of L-ascorbic acid; L-ascorbic acid ionizes to give L-ascorbate, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate, which is required as a cofactor in the oxidation of prolyl residues to hydroxyprolyl, and other reactions.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q3ZC33 GULO L-gulonolactone oxidase Bos taurus (Bovine) PR
Q8HXW0 GULO L-gulonolactone oxidase Sus scrofa (Pig) PR
P10867 Gulo L-gulonolactone oxidase Rattus norvegicus (Rat) PR
Q2QXY1 GLDH2 L-galactono-1,4-lactone dehydrogenase 2, mitochondrial Oryza sativa subsp japonica (Rice) PR
Q2RAP0 GLDH1 L-galactono-1,4-lactone dehydrogenase 1, mitochondrial Oryza sativa subsp japonica (Rice) PR
10 20 30 40 50 60
MVHGYKGVQF QNWAKTYGCS PEMYYQPTSV GEVREVLALA RQQNKKVKVV GGGHSPSDIA
70 80 90 100 110 120
CTDGFMIHMG KMNRVLQVDK EKKQVTVEAG ILLTDLHPQL DKHGLALSNL GAVSDVTVGG
130 140 150 160 170 180
VIGSGTHNTG IKHGILATQV VALTLMKADG TVLECSESSN ADVFQAARVH LGCLGVILTV
190 200 210 220 230 240
TLQCVPQFHL LETSFPSTLK EVLDNLDSHL KKSEYFRFLW FPHSENVSII YQDHTNKEPS
250 260 270 280 290 300
SASNWFWDYA IGFYLLEFLL WTSTYLPRLV GWINRFFFWL LFNCKKESSN LSHKIFSYEC
310 320 330 340 350 360
RFKQHVQDWA IPREKTKEAL LELKAMLEAH PKVVAHYPVE VRFTRGDDIL LSPCFQRDSC
370 380 390 400 410 420
YMNIIMYRPY GKDVPRLDYW LAYETIMKKF GGRPHWAKAH NCTRKDFEKM YPAFHKFCDI
430
REKLDPTGMF LNSYLEKVFY