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Protein

Cytochrome c oxidase subunit 1-beta

Gene

ctaDII

Organism
Paracoccus denitrificans
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Subunit 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). This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:
  • Cu2+Note: Binds 1 copper B ion per subunit.
  • hemeNote: Binds 2 heme groups per subunit.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: oxidative phosphorylation

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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi94Iron (heme A axial ligand)1
Metal bindingi276Copper B1
Metal bindingi280Copper B1
Metal bindingi325Copper B1
Metal bindingi326Copper B1
Metal bindingi411Iron (heme A3 axial ligand)1
Metal bindingi413Iron (heme A axial ligand)1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Hydrogen ion transport, Ion transport, Respiratory chain, Transport
LigandCopper, Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.9.3.1 3341

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00705

Protein family/group databases

Transport Classification Database

More...
TCDBi
3.D.4.6.1 the proton-translocating cytochrome oxidase (cox) superfamily

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cytochrome c oxidase subunit 1-beta (EC:1.9.3.1)
Alternative name(s):
Cytochrome aa3 subunit 1-beta
Cytochrome c oxidase polypeptide I-beta
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ctaDII
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiParacoccus denitrificans
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri266 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 28CytoplasmicAdd BLAST28
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei29 – 59Helical; Name=IAdd BLAST31
Topological domaini60 – 82PeriplasmicAdd BLAST23
Transmembranei83 – 120Helical; Name=IIAdd BLAST38
Topological domaini121 – 126Cytoplasmic6
Transmembranei127 – 151Helical; Name=IIIAdd BLAST25
Topological domaini152 – 176PeriplasmicAdd BLAST25
Transmembranei177 – 206Helical; Name=IVAdd BLAST30
Topological domaini207 – 217CytoplasmicAdd BLAST11
Transmembranei218 – 251Helical; Name=VAdd BLAST34
Topological domaini252 – 262PeriplasmicAdd BLAST11
Transmembranei263 – 299Helical; Name=VIAdd BLAST37
Topological domaini300 – 303Cytoplasmic4
Transmembranei304 – 331Helical; Name=VIIAdd BLAST28
Topological domaini332Periplasmic1
Transmembranei333 – 364Helical; Name=VIIIAdd BLAST32
Topological domaini365 – 369Cytoplasmic5
Transmembranei370 – 395Helical; Name=IXAdd BLAST26
Topological domaini396 – 404Periplasmic9
Transmembranei405 – 437Helical; Name=XAdd BLAST33
Topological domaini438 – 440Cytoplasmic3
Transmembranei441 – 469Helical; Name=XIAdd BLAST29
Topological domaini470 – 478Periplasmic9
Transmembranei479 – 514Helical; Name=XIIAdd BLAST36
Topological domaini515 – 558CytoplasmicAdd BLAST44

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB04147 Lauryl Dimethylamine-N-Oxide

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001834561 – 558Cytochrome c oxidase subunit 1-betaAdd BLAST558

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi66 ↔ 80
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki276 ↔ 2801'-histidyl-3'-tyrosine (His-Tyr)

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

His-276 and Tyr-280 are involved in the formation of a copper-coordinated covalent cross-link at the active site of the catalytic subunit I.

Keywords - PTMi

Disulfide bond

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-6088N

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1558
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P98002

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P98002

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P98002

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0843 LUCA

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01663 Cyt_c_Oxidase_I, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.210.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR023616 Cyt_c_oxase-like_su1_dom
IPR036927 Cyt_c_oxase-like_su1_sf
IPR000883 Cyt_C_Oxase_1
IPR023615 Cyt_c_Oxase_su1_BS
IPR033944 Cyt_c_oxase_su1_dom
IPR014241 Cyt_c_oxidase_su1_bac

The PANTHER Classification System

More...
PANTHERi
PTHR10422 PTHR10422, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00115 COX1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01165 CYCOXIDASEI

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF81442 SSF81442, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02891 CtaD_CoxA, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50855 COX1, 1 hit
PS00077 COX1_CUB, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P98002-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MADAAVHGHG DHHDTRGFFT RWFMSTNHKD IGILYLFTAG IVGLISVCFT
60 70 80 90 100
VYMRMELQHP GVQYMCLEGA RLIADASAEC TPNGHLWNVM ITYHGVLMMF
110 120 130 140 150
FVVIPALFGG FGNYFMPLHI GAPDMAFPRL NNLSYWMYVC GVALGVASLL
160 170 180 190 200
APGGNDQMGS GVGWVLYPPL STTEAGYSMD LAIFAVHVSG ASSILGAINI
210 220 230 240 250
ITTFLNMRAP GMTLFKVPLF AWSVFITAWL ILLSLPVLAG AITMLLMDRN
260 270 280 290 300
FGTQFFDPAG GGDPVLYQHI LWFFGHPEVY IIILPGFGII SHVISTFAKK
310 320 330 340 350
PIFGYLPMVL AMAAIGILGF VVWAHHMYTA GMSLTQQAYF MLATMTIAVP
360 370 380 390 400
TGIKVFSWIA TMWGGSIEFK TPMLWAFGFL FLFTVGGVTG VVLSQAPLDR
410 420 430 440 450
VYHDTYYVVA HFHYVMSLGA VFGIFAGVYY WIGKMSGRQY PEWAGQLHFW
460 470 480 490 500
MMFIGSNLIF FPQHFLGRQG MPRRYIDYPV EFAYWNNISS IGAYISFASF
510 520 530 540 550
LFFIGIVFYT LFAGKRVNVP NYWNEHADTL EWTLPSPPPE HTFETLPKRE

DWDRAHAH
Length:558
Mass (Da):62,439
Last modified:November 1, 1995 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA8402453C0C0339E
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Y07533 Genomic DNA Translation: CAA68821.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S08270

NCBI Reference Sequences

More...
RefSeqi
WP_011748228.1, NZ_PPGA01000019.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07533 Genomic DNA Translation: CAA68821.1
PIRiS08270
RefSeqiWP_011748228.1, NZ_PPGA01000019.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AR1X-ray2.70A1-558[»]
1QLEX-ray3.00A17-554[»]
1ZYYmodel-A17-545[»]
3EHBX-ray2.32A1-558[»]
3HB3X-ray2.25A1-558[»]
ProteinModelPortaliP98002
SMRiP98002
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6088N

Chemistry databases

DrugBankiDB04147 Lauryl Dimethylamine-N-Oxide

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

eggNOGiCOG0843 LUCA

Enzyme and pathway databases

UniPathwayi
UPA00705

BRENDAi1.9.3.1 3341

Miscellaneous databases

EvolutionaryTraceiP98002

Family and domain databases

CDDicd01663 Cyt_c_Oxidase_I, 1 hit
Gene3Di1.20.210.10, 1 hit
InterProiView protein in InterPro
IPR023616 Cyt_c_oxase-like_su1_dom
IPR036927 Cyt_c_oxase-like_su1_sf
IPR000883 Cyt_C_Oxase_1
IPR023615 Cyt_c_Oxase_su1_BS
IPR033944 Cyt_c_oxase_su1_dom
IPR014241 Cyt_c_oxidase_su1_bac
PANTHERiPTHR10422 PTHR10422, 1 hit
PfamiView protein in Pfam
PF00115 COX1, 1 hit
PRINTSiPR01165 CYCOXIDASEI
SUPFAMiSSF81442 SSF81442, 1 hit
TIGRFAMsiTIGR02891 CtaD_CoxA, 1 hit
PROSITEiView protein in PROSITE
PS50855 COX1, 1 hit
PS00077 COX1_CUB, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCOX1B_PARDE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P98002
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: December 5, 2018
This is version 136 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

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