Skip Header

Contribute Send feedback
Read comments (?) or add your own

P0ABJ9 (CYDA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome d ubiquinol oxidase subunit 1

EC=1.10.3.-
Alternative name(s):
Cytochrome bd-I oxidase subunit I
Cytochrome d ubiquinol oxidase subunit I
Gene names
Name:cydA
Synonyms:cyd-1
Ordered Locus Names:b0733, JW0722
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length522 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cytochrome d terminal oxidase complex is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration.

Catalytic activity

Ubiquinol-8 + O2 = Ubiquinone-8 + H2O.

Cofactor

Binds 1 protoheme IX group.

Pathway

Energy metabolism; oxidative phosphorylation.

Subunit structure

Heterodimer of subunits I and II. Has been isolated from inner membrane preparations in a complex with one subunit each of CydB and YhcB, suggesting that YhcB is in fact a subunit of this complex. Ref.8

Subcellular location

Cell inner membrane; Multi-pass membrane protein Ref.8.

Sequence similarities

Belongs to the cytochrome ubiquinol oxidase subunit 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 522522Cytochrome d ubiquinol oxidase subunit 1
PRO_0000183919

Regions

Topological domain1 – 2222Cytoplasmic Probable
Transmembrane23 – 4220Helical; Probable
Topological domain43 – 9452Periplasmic Probable
Transmembrane95 – 11420Helical; Probable
Topological domain115 – 12915Cytoplasmic Probable
Transmembrane130 – 14920Helical; Probable
Topological domain150 – 18738Periplasmic Probable
Transmembrane188 – 20720Helical; Probable
Topological domain208 – 21912Cytoplasmic Probable
Transmembrane220 – 23920Helical; Probable
Topological domain240 – 392153Periplasmic Probable
Transmembrane393 – 41220Helical; Probable
Topological domain413 – 47058Cytoplasmic Probable
Transmembrane471 – 49020Helical; Probable
Topological domain491 – 52232Periplasmic Probable

Sites

Metal binding1861Iron (heme b558 axial ligand)

Amino acid modifications

Modified residue11N-formylmethionine

Experimental info

Sequence conflict2131F → L in AAA18804. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P0ABJ9 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: E757442068BCFCFE

FASTA52258,205
        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 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of the cyd locus encoding the two subunits of the cytochrome d terminal oxidase complex of Escherichia coli."
Green G.N., Fang H., Lin R.-J., Newton G., Mather M., Georgiou C.D., Gennis R.B.
J. Biol. Chem. 263:13138-13143(1988) [PubMed: 2843510] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Beta-galactosidase gene fusions as probes for the cytoplasmic regions of subunits I and II of the membrane-bound cytochrome d terminal oxidase from Escherichia coli."
Georgiou C.D., Dueweke T.J., Gennis R.B.
J. Biol. Chem. 263:13130-13137(1988) [PubMed: 3138232] [Abstract]
Cited for: TOPOLOGY.
[6]"Analysis of the topology of the cytochrome d terminal oxidase complex of Escherichia coli by alkaline phosphatase fusions."
Newton G., Yun C.H., Gennis R.B.
Mol. Microbiol. 5:2511-2518(1991) [PubMed: 1724280] [Abstract]
Cited for: TOPOLOGY.
[7]"Epitopes of monoclonal antibodies which inhibit ubiquinol oxidase activity of Escherichia coli cytochrome d complex localize functional domain."
Dueweke T.J., Gennis R.B.
J. Biol. Chem. 265:4273-4277(1990) [PubMed: 1689724] [Abstract]
Cited for: DOMAINS.
[8]"Protein complexes of the Escherichia coli cell envelope."
Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O.
J. Biol. Chem. 280:34409-34419(2005) [PubMed: 16079137] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION.
Strain: BL21-DE3.
[9]"Global topology analysis of the Escherichia coli inner membrane proteome."
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
Science 308:1321-1323(2005) [PubMed: 15919996] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: K12 / MG1655 / ATCC 47076.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03939 Unassigned DNA. Translation: AAA18804.1.
U00096 Genomic DNA. Translation: AAC73827.2.
AP009048 Genomic DNA. Translation: BAA35399.1.
RefSeqNP_415261.2. NC_000913.2.

3D structure databases

ProteinModelPortalP0ABJ9.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-36181N.
IntActP0ABJ9. 3 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000000023; EBESCP00000000023; EBESCG00000000021.
EBESCT00000000024; EBESCP00000000024; EBESCG00000000021.
EBESCT00000000025; EBESCP00000000025; EBESCG00000000021.
EBESCT00000000026; EBESCP00000000026; EBESCG00000000021.
EBESCT00000000027; EBESCP00000000027; EBESCG00000000021.
EBESCT00000015660; EBESCP00000014951; EBESCG00000014720.
GeneID945341.
GenomeReviewsGene locus JW0722 in contig AP009048_GR.
Gene locus b0733 in contig U00096_GR.
KEGGecj:JW0722.
eco:b0733.
PATRIC32116663. VBIEscCol129921_0764.

Organism-specific databases

EchoBASEEB0170.
EcoGeneEG10173. cydA.

Phylogenomic databases

eggNOGCOG1271.
GeneTreeEBGT00050000010528.
HOGENOMHBG753185.
OMAMAVTWLV.
PhylomeDBP0ABJ9.
ProtClustDBPRK15097.

Enzyme and pathway databases

BioCycEcoCyc:CYDA-MONOMER.
MetaCyc:CYDA-MONOMER.

Gene expression databases

GenevestigatorP0ABJ9.

Family and domain databases

InterProIPR002585. Cyt-d_ubiquinol_oxidase_suI.
[Graphical view]
KOK00425.
PfamPF01654. Bac_Ubq_Cox. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYDA_ECOLI
AccessionPrimary (citable) accession number: P0ABJ9
Secondary accession number(s): P11026, P75754, P76823
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: January 25, 2012
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families