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 Q2QXY1

Entry ID Method Resolution Chain Position Source
AF-Q2QXY1-F1 Predicted AlphaFoldDB

No variants for Q2QXY1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2QXY1

No associated diseases with Q2QXY1

2 regional properties for Q2QXY1

Type Name Position InterPro Accession
domain Iron hydrogenase, small subunit 412 - 467 IPR003149
domain Iron hydrogenase, large subunit, C-terminal 113 - 404 IPR004108

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
Q2RAP0 GLDH1 L-galactono-1,4-lactone dehydrogenase 1, 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 VLHDALAAAH
130 140 150 160 170 180
GERRKLRPLG SGLSPNGLAL SRAGMVNLAL MDKVLDVDAK KKTVTVQAGI RVAELVDTLR
190 200 210 220 230 240
EHGLTLQNFA SIREQQVGGI IQVGAHGTGA RLPPIDEQVI SMKLVTPAKG TIELSREKDP
250 260 270 280 290 300
DLFYLARCGL GGLGVVAEVT LQCVERHQLI EHTFVSSADE VKKNHKKWLS ENKHIKYLWI
310 320 330 340 350 360
PYTDTVVVVQ CNPPSRWRTP KFTSKYGKDE AIQHVRDLYR ESLKKYRTKA ESNDPEVDQL
370 380 390 400 410 420
SFTELRDRLL ALDPLDKDHV 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 KDKDELTELL
550 560 570 580
ARLRKRFPVD AYNKARMELD PNKVLSNAKL EKLFPVTEVQ HVK