Q2RAP0

PR
Gene name
GLDH1 (Os11g0143500, LOC_Os11g04740, OsJ_32931)
Protein name
L-galactono-1,4-lactone dehydrogenase 1, mitochondrial
Names
Species
Oryza sativa subsp japonica (Rice)
KEGG Pathway
osa:4349749
EC number
1.3.2.3: With a cytochrome as acceptor
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-62 (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 Q2RAP0

Entry ID Method Resolution Chain Position Source
AF-Q2RAP0-F1 Predicted AlphaFoldDB

No variants for Q2RAP0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2RAP0

No associated diseases with Q2RAP0

3 regional properties for Q2RAP0

Type Name Position InterPro Accession
domain FAD linked oxidase, N-terminal 102 - 232 IPR006094
domain D-arabinono-1,4-lactone oxidase, C-terminal domain 259 - 571 IPR007173
domain FAD-binding domain, PCMH-type 95 - 266 IPR016166

Functions

Description
EC Number 1.3.2.3 With a cytochrome as acceptor
Subcellular Localization
  • Mitochondrion 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
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.
mitochondrial membrane Either of the lipid bilayers that surround the mitochondrion and form the mitochondrial envelope.

4 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.
galactonolactone dehydrogenase activity Catalysis of the reaction: L-galactono-1,4-lactone + 2 ferricytochrome c = L-ascorbate + 2 ferrocytochrome c.
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
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
10 20 30 40 50 60
MRRLLLAGIL RRASSSPSSH HHLHLVRALS ASSPLPASDA DLRKYAGYAL LLLGCGAATY
70 80 90 100 110 120
YSFPLPPDAL HKKAVPFKYA PLPDDLHAVS NWSATHEVHT RVLLQPDSLP ALHDALAAAH
130 140 150 160 170 180
GECRKLRPLG SGLSPNGLAL SRAGMVNLAL MDKVLGVDAK KKTVTVQAGI RVAELVDALR
190 200 210 220 230 240
EHGLTLQNFA SIREQQVGGI IQVGAHGTGA RLPPIDEQVI SMKLVTPAKG TIELSREKDP
250 260 270 280 290 300
DLFYLARCGL GGLGVVAEVT LQCVERHQLI EHTFVSNADE VKKNHKKWLS ENKHIKYLWI
310 320 330 340 350 360
PYTDTVVVVQ CNPPSRWRTP KFTSKYGKDE AIQHVRDLYH ESLKKYRTKA ESNDPEVDQL
370 380 390 400 410 420
SFTELRDRLL TLDPLDKDHV IRINKAEAEY WKKSEGYRMG WSDEILGFDC GGQQWVSETC
430 440 450 460 470 480
FPAGTLAKPN MKDLDYIEEL LQLIEKEDIP APAPIEQRWT ACSRSPMSPA SSSQEDDIFS
490 500 510 520 530 540
WVGIIMYLPT SDARQRKEIT EEFFNYRSKT QTNLWDGYSA YEHWAKIEVP KDKDELAELQ
550 560 570 580
ARLRKRFPVD AYNKARMELD PNKVLSNAKL EKLFPVTEVQ HEK