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Protein

Cytochrome c oxidase subunit 1-beta

Gene

ctaDII

Organism
Paracoccus denitrificans
Status
Reviewed-Annotation score: -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

Keywordsi

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

Enzyme and pathway databases

BRENDAi1.9.3.1 3341
UniPathwayi
UPA00705

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

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Chemistry databases

DrugBankiDB04147 Lauryl Dimethylamine-N-Oxide

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

Structurei

Secondary structure

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

3D structure databases

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
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

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
RefSeqiWP_011748228.1, NZ_PPGA01000019.1

Similar proteinsi

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:
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

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
ProtoNetiSearch...

Entry informationi

Entry nameiCOX1B_PARDE
AccessioniPrimary (citable) accession number: P98002
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 23, 2018
This is version 135 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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