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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-Experimental evidence at protein leveli

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.

Catalytic activityi

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

Cofactori

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

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
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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Hydrogen ion transport, Ion transport, Respiratory chain, Transport

Keywords - Ligandi

Copper, Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.9.3.1. 3341.
UniPathwayiUPA00705.

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 1-beta (EC:1.9.3.1)
Alternative name(s):
Cytochrome aa3 subunit 1-beta
Cytochrome c oxidase polypeptide I-beta
Gene namesi
Name:ctaDII
OrganismiParacoccus denitrificans
Taxonomic identifieri266 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 28CytoplasmicAdd BLAST28
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

Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001834561 – 558Cytochrome c oxidase subunit 1-betaAdd BLAST558

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi66 ↔ 80
Cross-linki276 ↔ 2801'-histidyl-3'-tyrosine (His-Tyr)

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

Interactioni

Protein-protein interaction databases

DIPiDIP-6088N.
STRINGi1051075.PDI_3131.

Structurei

Secondary structure

1558
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi19 – 21Combined sources3
Turni22 – 24Combined sources3
Helixi28 – 57Combined sources30
Beta strandi59 – 61Combined sources3
Beta strandi63 – 66Combined sources4
Beta strandi76 – 78Combined sources3
Helixi84 – 101Combined sources18
Helixi103 – 107Combined sources5
Turni108 – 110Combined sources3
Helixi111 – 119Combined sources9
Helixi128 – 150Combined sources23
Beta strandi151 – 153Combined sources3
Helixi154 – 156Combined sources3
Beta strandi157 – 159Combined sources3
Turni163 – 166Combined sources4
Helixi170 – 173Combined sources4
Beta strandi175 – 177Combined sources3
Helixi178 – 206Combined sources29
Helixi214 – 216Combined sources3
Helixi219 – 250Combined sources32
Beta strandi254 – 256Combined sources3
Helixi258 – 260Combined sources3
Helixi264 – 298Combined sources35
Helixi305 – 318Combined sources14
Helixi323 – 326Combined sources4
Helixi328 – 330Combined sources3
Helixi334 – 345Combined sources12
Helixi348 – 362Combined sources15
Helixi371 – 394Combined sources24
Helixi396 – 402Combined sources7
Beta strandi403 – 405Combined sources3
Helixi406 – 417Combined sources12
Helixi420 – 436Combined sources17
Beta strandi437 – 439Combined sources3
Helixi442 – 460Combined sources19
Helixi462 – 468Combined sources7
Beta strandi472 – 474Combined sources3
Helixi480 – 482Combined sources3
Helixi483 – 513Combined sources31
Beta strandi514 – 516Combined sources3
Helixi530 – 533Combined sources4
Beta strandi540 – 542Combined sources3
Helixi549 – 552Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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...

Miscellaneous databases

EvolutionaryTraceiP98002.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0843. LUCA.

Family and domain databases

CDDicd01663. Cyt_c_Oxidase_I. 1 hit.
Gene3Di1.20.210.10. 1 hit.
InterProiIPR000883. COX1.
IPR023616. Cyt_c_oxase-like_su1_dom.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR033944. Cyt_c_oxase_su1_dom.
IPR014241. Cyt_c_oxidase_su1_bac.
[Graphical view]
PANTHERiPTHR10422. PTHR10422. 1 hit.
PfamiPF00115. COX1. 1 hit.
[Graphical view]
PRINTSiPR01165. CYCOXIDASEI.
SUPFAMiSSF81442. SSF81442. 1 hit.
TIGRFAMsiTIGR02891. CtaD_CoxA. 1 hit.
PROSITEiPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]

Sequencei

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
Checksum:iA8402453C0C0339E
GO

Sequence databases

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

Genome annotation databases

PATRICi22854991. VBIParDen97112_1873.

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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.
STRINGi1051075.PDI_3131.

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

PATRICi22854991. VBIParDen97112_1873.

Phylogenomic databases

eggNOGiCOG0843. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00705.
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.
InterProiIPR000883. COX1.
IPR023616. Cyt_c_oxase-like_su1_dom.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR033944. Cyt_c_oxase_su1_dom.
IPR014241. Cyt_c_oxidase_su1_bac.
[Graphical view]
PANTHERiPTHR10422. PTHR10422. 1 hit.
PfamiPF00115. COX1. 1 hit.
[Graphical view]
PRINTSiPR01165. CYCOXIDASEI.
SUPFAMiSSF81442. SSF81442. 1 hit.
TIGRFAMsiTIGR02891. CtaD_CoxA. 1 hit.
PROSITEiPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCOX1B_PARDE
AccessioniPrimary (citable) accession number: P98002
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 30, 2016
This is version 127 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

Documents

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