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Protein

Cytochrome c oxidase subunit 1

Gene

cbaA

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • hemeBy similarityNote: Binds 2 heme groups.By similarity
  • Cu cationBy similarityNote: Binds a copper B center.By similarity

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 bindingi72Iron (heme A axial ligand)Curated1
Metal bindingi233Copper B1
Metal bindingi237Copper B1
Metal bindingi282Copper BCurated1
Metal bindingi283Copper BCurated1
Metal bindingi384Iron (heme A3 axial ligand)Curated1
Metal bindingi386Iron (heme A axial ligand)Curated1

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. 2305.
UniPathwayiUPA00705.

Protein family/group databases

TCDBi3.D.4.2.1. the proton-translocating cytochrome oxidase (cox) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome c oxidase subunit 1 (EC:1.9.3.1)
Alternative name(s):
Cytochrome c ba(3) subunit I
Cytochrome c oxidase polypeptide I
Cytochrome cba3 subunit 1
Gene namesi
Name:cbaA
Ordered Locus Names:TTHA1135
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei21 – 41HelicalSequence analysisAdd BLAST21
Transmembranei74 – 94HelicalSequence analysisAdd BLAST21
Transmembranei105 – 125HelicalSequence analysisAdd BLAST21
Transmembranei144 – 164HelicalSequence analysisAdd BLAST21
Transmembranei187 – 207HelicalSequence analysisAdd BLAST21
Transmembranei227 – 247HelicalSequence analysisAdd BLAST21
Transmembranei267 – 287HelicalSequence analysisAdd BLAST21
Transmembranei300 – 320HelicalSequence analysisAdd BLAST21
Transmembranei345 – 365HelicalSequence analysisAdd BLAST21
Transmembranei385 – 405HelicalSequence analysisAdd BLAST21
Transmembranei420 – 440HelicalSequence analysisAdd BLAST21
Transmembranei471 – 491HelicalSequence analysisAdd BLAST21
Transmembranei527 – 547HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001834621 – 562Cytochrome c oxidase subunit 1Add BLAST562

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki233 ↔ 2371'-histidyl-3'-tyrosine (His-Tyr)

Interactioni

Protein-protein interaction databases

STRINGi300852.TTHA1135.

Structurei

Secondary structure

1562
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 14Combined sources5
Helixi16 – 36Combined sources21
Helixi38 – 45Combined sources8
Turni46 – 48Combined sources3
Helixi52 – 58Combined sources7
Helixi65 – 77Combined sources13
Helixi79 – 97Combined sources19
Helixi103 – 125Combined sources23
Turni132 – 135Combined sources4
Beta strandi137 – 139Combined sources3
Helixi143 – 173Combined sources31
Helixi181 – 206Combined sources26
Helixi208 – 213Combined sources6
Beta strandi215 – 219Combined sources5
Helixi221 – 232Combined sources12
Helixi234 – 249Combined sources16
Helixi251 – 254Combined sources4
Helixi262 – 275Combined sources14
Helixi280 – 283Combined sources4
Turni284 – 286Combined sources3
Beta strandi288 – 290Combined sources3
Helixi292 – 326Combined sources35
Beta strandi331 – 333Combined sources3
Helixi334 – 337Combined sources4
Helixi344 – 366Combined sources23
Helixi369 – 371Combined sources3
Helixi372 – 375Combined sources4
Beta strandi376 – 378Combined sources3
Helixi380 – 388Combined sources9
Turni389 – 391Combined sources3
Helixi392 – 399Combined sources8
Turni400 – 403Combined sources4
Helixi404 – 409Combined sources6
Helixi415 – 444Combined sources30
Beta strandi448 – 450Combined sources3
Helixi453 – 455Combined sources3
Helixi457 – 459Combined sources3
Helixi461 – 463Combined sources3
Helixi464 – 492Combined sources29
Beta strandi493 – 495Combined sources3
Helixi499 – 503Combined sources5
Helixi520 – 524Combined sources5
Helixi527 – 550Combined sources24

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EHKX-ray2.40A1-562[»]
2QPDX-ray3.25A2-562[»]
2QPEX-ray2.90A2-562[»]
3BVDX-ray3.37A2-562[»]
3EH3X-ray3.10A2-562[»]
3EH4X-ray2.90A2-562[»]
3EH5X-ray2.80A2-562[»]
3QJQX-ray2.90A2-562[»]
3QJRX-ray3.20A2-562[»]
3QJSX-ray2.80A2-562[»]
3QJTX-ray2.95A2-562[»]
3QJUX-ray2.90A2-562[»]
3QJVX-ray2.80A2-562[»]
3S33X-ray4.45A2-562[»]
3S38X-ray4.20A2-562[»]
3S39X-ray4.80A2-562[»]
3S3AX-ray4.25A2-562[»]
3S3BX-ray3.30A2-562[»]
3S3CX-ray4.00A2-562[»]
3S3DX-ray3.75A2-562[»]
3S8FX-ray1.80A2-562[»]
3S8GX-ray1.80A2-562[»]
4FA7X-ray2.50A2-562[»]
4FAAX-ray2.80A2-562[»]
4G70X-ray2.60A2-562[»]
4G71X-ray2.90A2-562[»]
4G72X-ray3.19A2-562[»]
4G7QX-ray2.60A2-562[»]
4G7RX-ray3.05A2-562[»]
4G7SX-ray2.00A2-562[»]
4GP4X-ray2.80A2-562[»]
4GP5X-ray2.70A2-562[»]
4GP8X-ray2.80A2-562[»]
4N4YX-ray2.90A2-562[»]
ProteinModelPortaliQ5SJ79.
SMRiQ5SJ79.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SJ79.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4107RQ2. Bacteria.
COG0843. LUCA.
HOGENOMiHOG000249472.
KOiK02274.
OMAiLVVHNTS.
PhylomeDBiQ5SJ79.

Family and domain databases

CDDicd01660. ba3-like_Oxidase_I. 1 hit.
Gene3Di1.20.210.10. 1 hit.
InterProiIPR033943. ba3-like_Oxidase_I.
IPR000883. COX1.
IPR023616. Cyt_c_oxase-like_su1_dom.
IPR023615. Cyt_c_Oxase_su1_BS.
[Graphical view]
PANTHERiPTHR10422. PTHR10422. 1 hit.
PfamiPF00115. COX1. 1 hit.
[Graphical view]
PRINTSiPR01165. CYCOXIDASEI.
SUPFAMiSSF81442. SSF81442. 1 hit.
PROSITEiPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5SJ79-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVRASEISR VYEAYPEKKA TLYFLVLGFL ALIVGSLFGP FQALNYGNVD
60 70 80 90 100
AYPLLKRLLP FVQSYYQGLT LHGVLNAIVF TQLFAQAIMV YLPARELNMR
110 120 130 140 150
PNMGLMWLSW WMAFIGLVVA ALPLLANEAT VLYTFYPPLK GHWAFYLGAS
160 170 180 190 200
VFVLSTWVSI YIVLDLWRRW KAANPGKVTP LVTYMAVVFW LMWFLASLGL
210 220 230 240 250
VLEAVLFLLP WSFGLVEGVD PLVARTLFWW TGHPIVYFWL LPAYAIIYTI
260 270 280 290 300
LPKQAGGKLV SDPMARLAFL LFLLLSTPVG FHHQFADPGI DPTWKMIHSV
310 320 330 340 350
LTLFVAVPSL MTAFTVAASL EFAGRLRGGR GLFGWIRALP WDNPAFVAPV
360 370 380 390 400
LGLLGFIPGG AGGIVNASFT LDYVVHNTAW VPGHFHLQVA SLVTLTAMGS
410 420 430 440 450
LYWLLPNLTG KPISDAQRRL GLAVVWLWFL GMMIMAVGLH WAGLLNVPRR
460 470 480 490 500
AYIAQVPDAY PHAAVPMVFN VLAGIVLLVA LLLFIYGLFS VLLSRERKPE
510 520 530 540 550
LAEAPLPFAE VISGPEDRRL VLAMDRIGFW FAVAAILVVL AYGPTLVQLF
560
GHLNPVPGWR LW
Length:562
Mass (Da):62,528
Last modified:December 21, 2004 - v1
Checksum:i769B9E2F2033617B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09121 Genomic DNA. Translation: AAB00370.1.
AP008226 Genomic DNA. Translation: BAD70958.1.
RefSeqiWP_011173204.1. NC_006461.1.
YP_144401.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70958; BAD70958; BAD70958.
GeneIDi3168993.
KEGGittj:TTHA1135.
PATRICi23957229. VBITheThe93045_1114.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09121 Genomic DNA. Translation: AAB00370.1.
AP008226 Genomic DNA. Translation: BAD70958.1.
RefSeqiWP_011173204.1. NC_006461.1.
YP_144401.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EHKX-ray2.40A1-562[»]
2QPDX-ray3.25A2-562[»]
2QPEX-ray2.90A2-562[»]
3BVDX-ray3.37A2-562[»]
3EH3X-ray3.10A2-562[»]
3EH4X-ray2.90A2-562[»]
3EH5X-ray2.80A2-562[»]
3QJQX-ray2.90A2-562[»]
3QJRX-ray3.20A2-562[»]
3QJSX-ray2.80A2-562[»]
3QJTX-ray2.95A2-562[»]
3QJUX-ray2.90A2-562[»]
3QJVX-ray2.80A2-562[»]
3S33X-ray4.45A2-562[»]
3S38X-ray4.20A2-562[»]
3S39X-ray4.80A2-562[»]
3S3AX-ray4.25A2-562[»]
3S3BX-ray3.30A2-562[»]
3S3CX-ray4.00A2-562[»]
3S3DX-ray3.75A2-562[»]
3S8FX-ray1.80A2-562[»]
3S8GX-ray1.80A2-562[»]
4FA7X-ray2.50A2-562[»]
4FAAX-ray2.80A2-562[»]
4G70X-ray2.60A2-562[»]
4G71X-ray2.90A2-562[»]
4G72X-ray3.19A2-562[»]
4G7QX-ray2.60A2-562[»]
4G7RX-ray3.05A2-562[»]
4G7SX-ray2.00A2-562[»]
4GP4X-ray2.80A2-562[»]
4GP5X-ray2.70A2-562[»]
4GP8X-ray2.80A2-562[»]
4N4YX-ray2.90A2-562[»]
ProteinModelPortaliQ5SJ79.
SMRiQ5SJ79.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1135.

Protein family/group databases

TCDBi3.D.4.2.1. the proton-translocating cytochrome oxidase (cox) superfamily.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70958; BAD70958; BAD70958.
GeneIDi3168993.
KEGGittj:TTHA1135.
PATRICi23957229. VBITheThe93045_1114.

Phylogenomic databases

eggNOGiENOG4107RQ2. Bacteria.
COG0843. LUCA.
HOGENOMiHOG000249472.
KOiK02274.
OMAiLVVHNTS.
PhylomeDBiQ5SJ79.

Enzyme and pathway databases

UniPathwayiUPA00705.
BRENDAi1.9.3.1. 2305.

Miscellaneous databases

EvolutionaryTraceiQ5SJ79.

Family and domain databases

CDDicd01660. ba3-like_Oxidase_I. 1 hit.
Gene3Di1.20.210.10. 1 hit.
InterProiIPR033943. ba3-like_Oxidase_I.
IPR000883. COX1.
IPR023616. Cyt_c_oxase-like_su1_dom.
IPR023615. Cyt_c_Oxase_su1_BS.
[Graphical view]
PANTHERiPTHR10422. PTHR10422. 1 hit.
PfamiPF00115. COX1. 1 hit.
[Graphical view]
PRINTSiPR01165. CYCOXIDASEI.
SUPFAMiSSF81442. SSF81442. 1 hit.
PROSITEiPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCOX1_THET8
AccessioniPrimary (citable) accession number: Q5SJ79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: December 21, 2004
Last modified: November 30, 2016
This is version 111 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, Complete proteome, Reference proteome

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.