Q6GAF3

PR
Gene name
qoxB (SAS0995)
Protein name
Probable quinol oxidase subunit 1
Names
Quinol oxidase polypeptide I
Species
Staphylococcus aureus (strain MSSA476)
KEGG Pathway
sas:SAS0995
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

615-662 (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 Q6GAF3

Entry ID Method Resolution Chain Position Source
AF-Q6GAF3-F1 Predicted AlphaFoldDB

No variants for Q6GAF3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6GAF3

No associated diseases with Q6GAF3

2 regional properties for Q6GAF3

Type Name Position InterPro Accession
binding_site Cytochrome c oxidase, subunit I, copper-binding site 275 - 329 IPR023615
domain Cytochrome c oxidase-like, subunit I domain 38 - 556 IPR023616

Functions

Description
EC Number
Subcellular Localization
  • Cell membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 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.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
respirasome The protein complexes that form the electron transport system (the respiratory chain), associated with a cell membrane, usually the plasma membrane (in prokaryotes) or the inner mitochondrial membrane (on eukaryotes). The respiratory chain complexes transfer electrons from an electron donor to an electron acceptor and are associated with a proton pump to create a transmembrane electrochemical gradient.

4 GO annotations of molecular function

Name Definition
copper ion binding Binding to a copper (Cu) ion.
cytochrome-c oxidase activity Catalysis of the reaction: 4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.
heme binding Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor Catalysis of an oxidation-reduction (redox) reaction in which a diphenol, or related compound, acts as a hydrogen or electron donor and reduces oxygen.

1 GO annotations of biological process

Name Definition
oxidative phosphorylation The phosphorylation of ADP to ATP that accompanies the oxidation of a metabolite through the operation of the respiratory chain. Oxidation of compounds establishes a proton gradient across the membrane, providing the energy for ATP synthesis.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNFPWDQLLV KGNWMITMAQ IGAPFLVIGL IAVITYFKLW KYLYKEWFTS VDHKKIGIMY
70 80 90 100 110 120
LICAVLMFVR GGIDALLIRA QLTVPDNKFL ESNHYNEIFS THGVIMIIFM AMPFIFGLWN
130 140 150 160 170 180
IVVPLQIGAR DVAFPVLNNV SFWLFFAGMI LFNLSFIIGG SPAAGWTNYA PLAGEFSPGP
190 200 210 220 230 240
GVNYYLIAIQ ISGLGTLATG INFFVTILRC KTPTMKFMQM PMFTVTTFIT TLIVILAFPP
250 260 270 280 290 300
LTVALALMTT DRIFDTAFFT VAHGGMPMLW ANFFWVWGHP EVYIVILPAF GIYSEIIPTF
310 320 330 340 350 360
ARKRLFGHQS MVWATAGIAF LSFLVWVHHF FTMGNGALIN SFFSISTMLI GIPTGVKLFN
370 380 390 400 410 420
WLLTLYKGRI TFESPMLFSL AFIPNFLLGG VTGVMLAMAS ADYQYHNTYF LVAHFHYTLV
430 440 450 460 470 480
TGVVFACLAG LIFWYPKMMG YKLNETLNKW CFWFFMIGFN VCFLPQFILG LDGMPRRLYT
490 500 510 520 530 540
YMPSDGWFLL NLISTIGALL MAIGFLFLVV SIVYSHFKSP REATGDNWDG LGRTLEWTTA
550 560 570 580 590 600
SAIPPKYNFA ITPDWNDYDT FVDMKEHGRH YLDNHNYKDI HMPNNTPVGF WIGIFMTIGG
610 620 630 640 650 660
FFLIFETVIP ALICLFGIFG TMIYRSFQID HGYHIPAAEV AETEARLREA RIKEREAVSH
ES