P10867

PR
Gene name
Gulo
Protein name
L-gulonolactone oxidase
Names
LGO, L-gulono-gamma-lactone oxidase, GLO
Species
Rattus norvegicus (Rat)
KEGG Pathway
rno:60671
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

66-142 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P10867

Entry ID Method Resolution Chain Position Source
AF-P10867-F1 Predicted AlphaFoldDB

No variants for P10867

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P10867

No associated diseases with P10867

4 regional properties for P10867

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
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
P58710 Gulo L-gulonolactone oxidase Mus musculus (Mouse) PR
Q8HXW0 GULO L-gulonolactone oxidase Sus scrofa (Pig) PR
Q2RAP0 GLDH1 L-galactono-1,4-lactone dehydrogenase 1, mitochondrial Oryza sativa subsp japonica (Rice) PR
Q2QXY1 GLDH2 L-galactono-1,4-lactone dehydrogenase 2, mitochondrial Oryza sativa subsp japonica (Rice) PR
10 20 30 40 50 60
MVHGYKGVQF QNWAKTYGCS PEVYYQPTSV EEVREVLALA REQKKKVKVV GGGHSPSDIA
70 80 90 100 110 120
CTDGFMIHMG KMNRVLQVDK EKKQITVEAG ILLADLHPQL DEHGLAMSNL GAVSDVTVAG
130 140 150 160 170 180
VIGSGTHNTG IKHGILATQV VALTLMTADG EVLECSESRN ADVFQAARVH LGCLGIILTV
190 200 210 220 230 240
TLQCVPQFHL QETSFPSTLK EVLDNLDSHL KRSEYFRFLW FPHTENVSII YQDHTNKAPS
250 260 270 280 290 300
SASNWFWDYA IGFYLLEFLL WTSTYLPCLV GWINRFFFWM LFNCKKESSN LSHKIFTYEC
310 320 330 340 350 360
RFKQHVQDWA IPREKTKEAL LELKAMLEAH PKVVAHYPVE VRFTRGDDIL LSPCFQRDSC
370 380 390 400 410 420
YMNIIMYRPY GKDVPRLDYW LAYETIMKKF GGRPHWAKAH NCTQKDFEEM YPTFHKFCDI
430
REKLDPTGMF LNSYLEKVFY