UniProtKB - P0ABJ9 (CYDA_ECOLI)
Protein
Cytochrome bd-I ubiquinol oxidase subunit 1
Gene
cydA
Organism
Escherichia coli (strain K12)
Status
Functioni
A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H2O, transferring 1 proton/electron.5 Publications
Catalytic activityi
- EC:7.1.1.72 Publications
Cofactori
Protein has several cofactor binding sites:- heme b5 PublicationsNote: Binds 1 protoheme IX center (heme b558) per subunit.5 Publications
- heme b5 PublicationsNote: Binds 1 protoheme IX center (heme b595, originally called cytochrome a1) per heterodimer, in conjunction with CydB.5 Publications
- heme d cis-diol5 PublicationsNote: Binds 1 iron-chlorin (heme d or cytochrome d) per heterodimer, in conjunction with CydB.5 Publications
Activity regulationi
90% inhibited by cyanide and 2-heptyl-4-hydroxyquinoline N-oxide, at 1 mM and 40 µM respectively.1 Publication
Kineticsi
pH 7.0, 37 degrees Celsius.
- KM=0.1 mM for ubiquinol-11 Publication
- KM=0.28 mM for 2,3,5,6-tetramethyl-p-phenylenediamine1 Publication
- KM=0.68 mM for N,N,N',N'-tetramethyl-p-phenylenediamine1 Publication
- Vmax=383 µmol/min/mg enzyme for ubiquinol-11 Publication
- Vmax=270 µmol/min/mg enzyme for 2,3,5,6-tetramethyl-p-phenylenediamine1 Publication
- Vmax=126 µmol/min/mg enzyme for N,N,N',N'-tetramethyl-p-phenylenediamine1 Publication
: oxidative phosphorylation Pathwayi
This protein is involved in the pathway oxidative phosphorylation, which is part of Energy metabolism.View all proteins of this organism that are known to be involved in the pathway oxidative phosphorylation and in Energy metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 19 | Iron (heme b595 axial ligand)Sequence analysis | 1 | |
Metal bindingi | 186 | Iron (heme b558 axial ligand) | 1 | |
Metal bindingi | 393 | Iron (heme b558 axial ligand) | 1 |
GO - Molecular functioni
- electron transfer activity Source: EcoCyc
- heme binding Source: EcoCyc
- metal ion binding Source: UniProtKB-KW
- oxidoreductase activity, acting on diphenols and related substances as donors Source: EcoCyc
- oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor Source: GO_Central
GO - Biological processi
- aerobic electron transport chain Source: EcoCyc
- oxidative phosphorylation Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Translocase |
Biological process | Electron transport, Transport |
Ligand | Heme, Iron, Metal-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:CYDA-MONOMER MetaCyc:CYDA-MONOMER |
BRENDAi | 1.10.3.14, 2026 |
UniPathwayi | UPA00705 |
Protein family/group databases
TCDBi | 3.D.4.3.2, the proton-translocating cytochrome oxidase (cox) superfamily |
Names & Taxonomyi
Protein namesi | Recommended name: Cytochrome bd-I ubiquinol oxidase subunit 1 (EC:7.1.1.72 Publications)Alternative name(s): Cytochrome bd-I oxidase subunit I Cytochrome d ubiquinol oxidase subunit I |
Gene namesi | Name:cydA Synonyms:cyd-1 Ordered Locus Names:b0733, JW0722 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
- Cell inner membrane 2 Publications; Multi-pass membrane protein 2 Publications
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 15 | PeriplasmicCuratedAdd BLAST | 15 | |
Transmembranei | 16 – 35 | HelicalCuratedAdd BLAST | 20 | |
Topological domaini | 36 – 54 | CytoplasmicCuratedAdd BLAST | 19 | |
Transmembranei | 55 – 69 | HelicalCuratedAdd BLAST | 15 | |
Topological domaini | 70 – 96 | PeriplasmicCuratedAdd BLAST | 27 | |
Transmembranei | 97 – 114 | HelicalCuratedAdd BLAST | 18 | |
Topological domaini | 115 – 128 | CytoplasmicCuratedAdd BLAST | 14 | |
Transmembranei | 129 – 146 | HelicalCuratedAdd BLAST | 18 | |
Topological domaini | 147 – 186 | PeriplasmicCuratedAdd BLAST | 40 | |
Transmembranei | 187 – 203 | HelicalCuratedAdd BLAST | 17 | |
Topological domaini | 204 – 219 | CytoplasmicCuratedAdd BLAST | 16 | |
Transmembranei | 220 – 235 | HelicalCuratedAdd BLAST | 16 | |
Topological domaini | 236 – 390 | PeriplasmicCuratedAdd BLAST | 155 | |
Transmembranei | 391 – 407 | HelicalCuratedAdd BLAST | 17 | |
Topological domaini | 408 – 423 | CytoplasmicCuratedAdd BLAST | 16 | |
Transmembranei | 424 – 441 | HelicalCuratedAdd BLAST | 18 | |
Topological domaini | 442 – 472 | PeriplasmicCuratedAdd BLAST | 31 | |
Transmembranei | 473 – 487 | HelicalCuratedAdd BLAST | 15 | |
Topological domaini | 488 – 522 | CytoplasmicCuratedAdd BLAST | 35 |
GO - Cellular componenti
- cytochrome complex Source: EcoCyc
- integral component of plasma membrane Source: EcoCyc
- membrane Source: EcoCyc
- plasma membrane Source: EcoCyc
Keywords - Cellular componenti
Cell inner membrane, Cell membrane, MembranePathology & Biotechi
Disruption phenotypei
A double cydA/cydB deletion shows increased sensitivity to reductant (beta-mercapoethanol).3 Publications
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 19 | H → L or R: Loss of cytochrome b595 and heme d, no aerobic growth, complex assembles. 1 Publication | 1 | |
Mutagenesisi | 86 | H → R: No effect. 1 Publication | 1 | |
Mutagenesisi | 126 | H → P: Loss of all cofactors, no aerobic growth, complex assembles. 1 Publication | 1 | |
Mutagenesisi | 126 | H → R: No effect. 1 Publication | 1 | |
Mutagenesisi | 186 | H → L: Loss of cytochrome b558, no aerobic growth, complex assembles, this subunit is more susceptible to proteolysis. 1 Publication | 1 | |
Mutagenesisi | 314 | H → L: Grows aerobically, has altered cytochrome b/d ratio, complex assembles. 1 Publication | 1 | |
Mutagenesisi | 314 | H → P: Loss of cytochrome b595 and heme d, no aerobic growth, loss of complex. 1 Publication | 1 | |
Mutagenesisi | 393 | M → L: Cytochrome b558 shifts to a high spin configuration, complex assembles. Retains about 1% quinol oxidoreductase activity after purification. | 1 | |
Mutagenesisi | 510 | H → L: No effect. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000183919 | 1 – 522 | Cytochrome bd-I ubiquinol oxidase subunit 1Add BLAST | 522 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1 | N-formylmethionine1 Publication | 1 |
Post-translational modificationi
The N-terminus is blocked.
Keywords - PTMi
FormylationProteomic databases
jPOSTi | P0ABJ9 |
PaxDbi | P0ABJ9 |
PRIDEi | P0ABJ9 |
Expressioni
Inductioni
Under conditions of low aeration, in stationary phase (at protein level).1 Publication
Interactioni
Subunit structurei
Heterodimer of subunits I and II. Probably interacts with CydX, and overexpressed AppX.
4 PublicationsBinary interactionsi
P0ABJ9
With | #Exp. | IntAct |
---|---|---|
cydB [P0ABK2] | 5 | EBI-906928,EBI-1213195 |
Protein-protein interaction databases
BioGRIDi | 4263539, 372 interactors |
ComplexPortali | CPX-268, Cytochrome bd-I ubiquinol oxidase complex |
DIPi | DIP-36181N |
IntActi | P0ABJ9, 4 interactors |
MINTi | P0ABJ9 |
STRINGi | 511145.b0733 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0ABJ9 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Sequence similaritiesi
Belongs to the cytochrome ubiquinol oxidase subunit 1 family.Curated
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | COG1271, Bacteria |
HOGENOMi | CLU_030555_3_3_6 |
InParanoidi | P0ABJ9 |
PhylomeDBi | P0ABJ9 |
Family and domain databases
InterProi | View protein in InterPro IPR002585, Cyt-d_ubiquinol_oxidase_su_1 |
PANTHERi | PTHR30365, PTHR30365, 1 hit |
Pfami | View protein in Pfam PF01654, Cyt_bd_oxida_I, 1 hit |
PIRSFi | PIRSF006446, Cyt_quinol_oxidase_1, 1 hit |
i Sequence
Sequence statusi: Complete.
P0ABJ9-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MLDIVELSRL QFALTAMYHF LFVPLTLGMA FLLAIMETVY VLSGKQIYKD
60 70 80 90 100
MTKFWGKLFG INFALGVATG LTMEFQFGTN WSYYSHYVGD IFGAPLAIEG
110 120 130 140 150
LMAFFLESTF VGLFFFGWDR LGKVQHMCVT WLVALGSNLS ALWILVANGW
160 170 180 190 200
MQNPIASDFN FETMRMEMVS FSELVLNPVA QVKFVHTVAS GYVTGAMFIL
210 220 230 240 250
GISAWYMLKG RDFAFAKRSF AIAASFGMAA VLSVIVLGDE SGYEMGDVQK
260 270 280 290 300
TKLAAIEAEW ETQPAPAAFT LFGIPDQEEE TNKFAIQIPY ALGIIATRSV
310 320 330 340 350
DTPVIGLKEL MVQHEERIRN GMKAYSLLEQ LRSGSTDQAV RDQFNSMKKD
360 370 380 390 400
LGYGLLLKRY TPNVADATEA QIQQATKDSI PRVAPLYFAF RIMVACGFLL
410 420 430 440 450
LAIIALSFWS VIRNRIGEKK WLLRAALYGI PLPWIAVEAG WFVAEYGRQP
460 470 480 490 500
WAIGEVLPTA VANSSLTAGD LIFSMVLICG LYTLFLVAEL FLMFKFARLG
510 520
PSSLKTGRYH FEQSSTTTQP AR
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 213 | F → L in AAA18804 (PubMed:2843510).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J03939 Unassigned DNA Translation: AAA18804.1 U00096 Genomic DNA Translation: AAC73827.2 AP009048 Genomic DNA Translation: BAA35399.1 |
RefSeqi | NP_415261.2, NC_000913.3 WP_000884361.1, NZ_SSZK01000033.1 |
Genome annotation databases
EnsemblBacteriai | AAC73827; AAC73827; b0733 BAA35399; BAA35399; BAA35399 |
GeneIDi | 49585519 945341 |
KEGGi | ecj:JW0722 eco:b0733 |
PATRICi | fig|1411691.4.peg.1540 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J03939 Unassigned DNA Translation: AAA18804.1 U00096 Genomic DNA Translation: AAC73827.2 AP009048 Genomic DNA Translation: BAA35399.1 |
RefSeqi | NP_415261.2, NC_000913.3 WP_000884361.1, NZ_SSZK01000033.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
6RKO | electron microscopy | 2.68 | A | 1-522 | [»] | |
6RX4 | electron microscopy | 3.30 | A | 1-522 | [»] | |
SMRi | P0ABJ9 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4263539, 372 interactors |
ComplexPortali | CPX-268, Cytochrome bd-I ubiquinol oxidase complex |
DIPi | DIP-36181N |
IntActi | P0ABJ9, 4 interactors |
MINTi | P0ABJ9 |
STRINGi | 511145.b0733 |
Protein family/group databases
TCDBi | 3.D.4.3.2, the proton-translocating cytochrome oxidase (cox) superfamily |
Proteomic databases
jPOSTi | P0ABJ9 |
PaxDbi | P0ABJ9 |
PRIDEi | P0ABJ9 |
Genome annotation databases
EnsemblBacteriai | AAC73827; AAC73827; b0733 BAA35399; BAA35399; BAA35399 |
GeneIDi | 49585519 945341 |
KEGGi | ecj:JW0722 eco:b0733 |
PATRICi | fig|1411691.4.peg.1540 |
Organism-specific databases
EchoBASEi | EB0170 |
Phylogenomic databases
eggNOGi | COG1271, Bacteria |
HOGENOMi | CLU_030555_3_3_6 |
InParanoidi | P0ABJ9 |
PhylomeDBi | P0ABJ9 |
Enzyme and pathway databases
UniPathwayi | UPA00705 |
BioCyci | EcoCyc:CYDA-MONOMER MetaCyc:CYDA-MONOMER |
BRENDAi | 1.10.3.14, 2026 |
Miscellaneous databases
PROi | PR:P0ABJ9 |
Family and domain databases
InterProi | View protein in InterPro IPR002585, Cyt-d_ubiquinol_oxidase_su_1 |
PANTHERi | PTHR30365, PTHR30365, 1 hit |
Pfami | View protein in Pfam PF01654, Cyt_bd_oxida_I, 1 hit |
PIRSFi | PIRSF006446, Cyt_quinol_oxidase_1, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | CYDA_ECOLI | |
Accessioni | P0ABJ9Primary (citable) accession number: P0ABJ9 Secondary accession number(s): P11026, P75754, P76823 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 25, 2005 |
Last sequence update: | October 25, 2005 | |
Last modified: | December 2, 2020 | |
This is version 129 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families