P0ABJ9

PR
Gene name
cydA (cyd-1, b0733, JW0722)
Protein name
Cytochrome bd-I ubiquinol oxidase subunit 1
Names
Cytochrome bd-I oxidase subunit I, Cytochrome d ubiquinol oxidase subunit I
Species
Escherichia coli (strain K12)
KEGG Pathway
eco:b0733
EC number
7.1.1.7: Hydron translocation or charge separation linked to oxidoreductase reactions
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

474-522 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

3 structures for P0ABJ9

Entry ID Method Resolution Chain Position Source
6RKO EM 268 A A 1-522 PDB
6RX4 EM 330 A A 1-522 PDB
AF-P0ABJ9-F1 Predicted AlphaFoldDB

No variants for P0ABJ9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P0ABJ9

No associated diseases with P0ABJ9

3 regional properties for P0ABJ9

Type Name Position InterPro Accession
domain Cyclin, C-terminal domain 243 - 365 IPR004367
domain Cyclin, N-terminal 114 - 240 IPR006671
domain Cyclin-like domain 149 - 234 IPR013763

Functions

Description
EC Number 7.1.1.7 Hydron translocation or charge separation linked to oxidoreductase reactions
Subcellular Localization
  • Cell inner membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
cytochrome complex A protein complex in which at least one of the proteins is a cytochrome, i.e. a heme-containing protein involved in catalysis of redox reactions.
integral component of plasma membrane The component of the plasma 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.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

5 GO annotations of molecular function

Name Definition
electron transfer activity Any molecular entity that serves as an electron acceptor and electron donor in an electron transport chain. An electron transport chain is a process in which a series of electron carriers operate together to transfer electrons from donors to any of several different terminal electron acceptors to generate a transmembrane electrochemical gradient.
heme binding Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
metal ion binding Binding to a metal ion.
oxidoreductase activity, acting on diphenols and related substances as donors Catalysis of an oxidation-reduction (redox) reaction in which a diphenol or related substance acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
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.

2 GO annotations of biological process

Name Definition
aerobic electron transport chain A process in which a series of electron carriers operate together to transfer electrons from donors such as NADH and FADH2 to oxygen to generate a transmembrane electrochemical gradient.
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
MLDIVELSRL QFALTAMYHF LFVPLTLGMA FLLAIMETVY VLSGKQIYKD MTKFWGKLFG
70 80 90 100 110 120
INFALGVATG LTMEFQFGTN WSYYSHYVGD IFGAPLAIEG LMAFFLESTF VGLFFFGWDR
130 140 150 160 170 180
LGKVQHMCVT WLVALGSNLS ALWILVANGW MQNPIASDFN FETMRMEMVS FSELVLNPVA
190 200 210 220 230 240
QVKFVHTVAS GYVTGAMFIL GISAWYMLKG RDFAFAKRSF AIAASFGMAA VLSVIVLGDE
250 260 270 280 290 300
SGYEMGDVQK TKLAAIEAEW ETQPAPAAFT LFGIPDQEEE TNKFAIQIPY ALGIIATRSV
310 320 330 340 350 360
DTPVIGLKEL MVQHEERIRN GMKAYSLLEQ LRSGSTDQAV RDQFNSMKKD LGYGLLLKRY
370 380 390 400 410 420
TPNVADATEA QIQQATKDSI PRVAPLYFAF RIMVACGFLL LAIIALSFWS VIRNRIGEKK
430 440 450 460 470 480
WLLRAALYGI PLPWIAVEAG WFVAEYGRQP WAIGEVLPTA VANSSLTAGD LIFSMVLICG
490 500 510 520
LYTLFLVAEL FLMFKFARLG PSSLKTGRYH FEQSSTTTQP AR