Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cytochrome c oxidase subunit 2

Gene

ctaC

Organism
Paracoccus denitrificans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).

Catalytic activityi

4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.

Cofactori

binuclear copper center (CuA)Note: Binds a binuclear copper A center per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi210Copper A11
Metal bindingi245Copper A11
Metal bindingi245Copper A21
Metal bindingi247Copper A2; via carbonyl oxygen1
Metal bindingi249Copper A11
Metal bindingi249Copper A21
Metal bindingi253Copper A21
Metal bindingi256Copper A11

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BRENDAi1.9.3.1. 3341.

Protein family/group databases

TCDBi3.D.4.6.1. the proton-translocating cytochrome oxidase (cox) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c oxidase subunit 2 (EC:1.9.3.1)
Alternative name(s):
Cytochrome aa3 subunit 2
Cytochrome c oxidase polypeptide II
Oxidase aa(3) subunit 2
Gene namesi
Name:ctaC
Synonyms:coiI, ctaB
OrganismiParacoccus denitrificans
Taxonomic identifieri266 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini30 – 55PeriplasmicAdd BLAST26
Transmembranei56 – 88HelicalAdd BLAST33
Topological domaini89 – 103CytoplasmicAdd BLAST15
Transmembranei104 – 134HelicalAdd BLAST31
Topological domaini135 – 280PeriplasmicAdd BLAST146

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Add BLAST29
ChainiPRO_000000605930 – 280Cytochrome c oxidase subunit 2Add BLAST251
PropeptideiPRO_0000006060281 – 298C-terminal propeptideAdd BLAST18

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei30Pyrrolidone carboxylic acid1

Keywords - PTMi

Pyrrolidone carboxylic acid

Interactioni

Protein-protein interaction databases

DIPiDIP-6089N.
STRINGi318586.Pden_4321.

Structurei

Secondary structure

1298
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni32 – 35Combined sources4
Beta strandi38 – 40Combined sources3
Helixi55 – 88Combined sources34
Turni91 – 93Combined sources3
Beta strandi94 – 96Combined sources3
Helixi104 – 133Combined sources30
Beta strandi140 – 148Combined sources9
Beta strandi151 – 156Combined sources6
Turni157 – 160Combined sources4
Beta strandi161 – 165Combined sources5
Helixi170 – 172Combined sources3
Helixi174 – 176Combined sources3
Helixi180 – 182Combined sources3
Turni183 – 185Combined sources3
Beta strandi187 – 189Combined sources3
Beta strandi191 – 208Combined sources18
Beta strandi210 – 214Combined sources5
Helixi215 – 217Combined sources3
Beta strandi219 – 223Combined sources5
Beta strandi229 – 234Combined sources6
Beta strandi236 – 243Combined sources8
Turni251 – 254Combined sources4
Beta strandi258 – 263Combined sources6
Helixi265 – 278Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AR1X-ray2.70B1-298[»]
1QLEX-ray3.00B30-281[»]
1ZYYmodel-B30-281[»]
3EHBX-ray2.32B1-298[»]
3HB3X-ray2.25B1-298[»]
ProteinModelPortaliP08306.
SMRiP08306.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08306.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CV4. Bacteria.
COG1622. LUCA.

Family and domain databases

Gene3Di1.10.287.90. 1 hit.
2.60.40.420. 1 hit.
InterProiIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR014222. Cyt_c_oxidase_su2.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
[Graphical view]
PfamiPF00116. COX2. 1 hit.
PF02790. COX2_TM. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 1 hit.
SSF81464. SSF81464. 1 hit.
TIGRFAMsiTIGR02866. CoxB. 1 hit.
PROSITEiPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08306-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMAIATKRRG VAAVMSLGVA TMTAVPALAQ DVLGDLPVIG KPVNGGMNFQ
60 70 80 90 100
PASSPLAHDQ QWLDHFVLYI ITAVTIFVCL LLLICIVRFN RRANPVPARF
110 120 130 140 150
THNTPIEVIW TLVPVLILVA IGAFSLPILF RSQEMPNDPD LVIKAIGHQW
160 170 180 190 200
YWSYEYPNDG VAFDALMLEK EALADAGYSE DEYLLATDNP VVVPVGKKVL
210 220 230 240 250
VQVTATDVIH AWTIPAFAVK QDAVPGRIAQ LWFSVDQEGV YFGQCSELCG
260 270 280 290
INHAYMPIVV KAVSQEKYEA WLAGAKEEFA ADASDYLPAS PVKLASAE
Length:298
Mass (Da):32,539
Last modified:August 1, 1988 - v1
Checksum:i918A64A9E3B93366
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti160 – 161GV → AF AA sequence (PubMed:2820725).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05828 Genomic DNA. Translation: CAA29268.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05828 Genomic DNA. Translation: CAA29268.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AR1X-ray2.70B1-298[»]
1QLEX-ray3.00B30-281[»]
1ZYYmodel-B30-281[»]
3EHBX-ray2.32B1-298[»]
3HB3X-ray2.25B1-298[»]
ProteinModelPortaliP08306.
SMRiP08306.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6089N.
STRINGi318586.Pden_4321.

Protein family/group databases

TCDBi3.D.4.6.1. the proton-translocating cytochrome oxidase (cox) superfamily.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CV4. Bacteria.
COG1622. LUCA.

Enzyme and pathway databases

BRENDAi1.9.3.1. 3341.

Miscellaneous databases

EvolutionaryTraceiP08306.

Family and domain databases

Gene3Di1.10.287.90. 1 hit.
2.60.40.420. 1 hit.
InterProiIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR014222. Cyt_c_oxidase_su2.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
[Graphical view]
PfamiPF00116. COX2. 1 hit.
PF02790. COX2_TM. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 1 hit.
SSF81464. SSF81464. 1 hit.
TIGRFAMsiTIGR02866. CoxB. 1 hit.
PROSITEiPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS50999. COX2_TM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCOX2_PARDE
AccessioniPrimary (citable) accession number: P08306
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: November 2, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.