Cytochrome c oxidase, aa3 type, subunit I - Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)

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Q3J5A7 (Q3J5A7_RHOS4) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 55. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Submitted name:
Cytochrome c oxidase, aa3 type, subunit I EMBL ABA78027.1

Gene names

Name:	coxI EMBL ABA78027.1
Ordered Locus Names:	RHOS4_04590
ORF Names:	RSP_1877 EMBL ABA78027.1

Organism

Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) [Reference proteome] [HAMAP] EMBL ABA78027.1

Taxonomic identifier

272943 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter ›

Protein attributes

Sequence length	566 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the heme-copper respiratory oxidase family. RuleBase RU000370

Ontologies

Keywords
Biological process	Electron transport Respiratory chain RuleBase RU000370 Transport
Cellular component	Membrane
Domain	Transmembrane RuleBase RU000370
Ligand	Calcium PDB 3OM3 PDB 3OMA PDB 3OMI PDB 3OMN Copper PDB 3OMA PDB 3OMI Heme RuleBase RU000370 PDB 3OM3 PDB 3OMA PDB 3OMI PDB 3OMN Iron Metal-binding
Molecular function	Oxidoreductase RuleBase RU000370
Technical term	3D-structure PDB 3OM3 PDB 3OMA PDB 3OMI PDB 3OMN Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aerobic respiration Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: InterPro respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	copper ion binding Inferred from electronic annotation. Source: InterPro cytochrome-c oxidase activity Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

Calcium PDB 3OM3 PDB 3OMA PDB 3OMI PDB 3OMN

Metal binding

Calcium; via carbonyl oxygen PDB 3OM3 PDB 3OMA PDB 3OMI PDB 3OMN

Metal binding

Calcium; via carbonyl oxygen PDB 3OM3 PDB 3OMA PDB 3OMI PDB 3OMN

Metal binding

Calcium PDB 3OM3 PDB 3OMA PDB 3OMI PDB 3OMN

Metal binding

102

Iron (heme 1 axial ligand); via tele nitrogen PDB 3OM3 PDB 3OMA PDB 3OMI PDB 3OMN

Metal binding

284

Copper; via pros nitrogen

Metal binding

333

Copper; via tele nitrogen

Metal binding

334

Copper; via tele nitrogen

Metal binding

419

Iron (heme 2 axial ligand); via tele nitrogen PDB 3OM3 PDB 3OMA PDB 3OMI PDB 3OMN

Metal binding

421

Iron (heme 1 axial ligand); via tele nitrogen PDB 3OM3 PDB 3OMA PDB 3OMI PDB 3OMN

Sequences

Sequence

Length

Mass (Da)

Tools

Q3J5A7 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 65A74DBCC5C550B0
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FASTA

566

63,147

        10         20         30         40         50         60 
MADAAIHGHE HDRRGFFTRW FMSTNHKDIG VLYLFTGGLV GLISVAFTVY MRMELMAPGV 

        70         80         90        100        110        120 
QFMCAEHLES GLVKGFFQSL WPSAVENCTP NGHLWNVMIT GHGILMMFFV VIPALFGGFG 

       130        140        150        160        170        180 
NYFMPLHIGA PDMAFPRMNN LSYWLYVAGT SLAVASLFAP GGNGQLGSGI GWVLYPPLST 

       190        200        210        220        230        240 
SESGYSTDLA IFAVHLSGAS SILGAINMIT TFLNMRAPGM TMHKVPLFAW SIFVTAWLIL 

       250        260        270        280        290        300 
LALPVLAGAI TMLLTDRNFG TTFFQPSGGG DPVLYQHILW FFGHPEVYII VLPAFGIVSH 

       310        320        330        340        350        360 
VIATFAKKPI FGYLPMVYAM VAIGVLGFVV WAHHMYTAGL SLTQQSYFMM ATMVIAVPTG 

       370        380        390        400        410        420 
IKIFSWIATM WGGSIELKTP MLWALGFLFL FTVGGVTGIV LSQASVDRYY HDTYYVVAHF 

       430        440        450        460        470        480 
HYVMSLGAVF GIFAGIYFWI GKMSGRQYPE WAGKLHFWMM FVGANLTFFP QHFLGRQGMP 

       490        500        510        520        530        540 
RRYIDYPEAF ATWNFVSSLG AFLSFASFLF FLGVIFYTLT RGARVTANNY WNEHADTLEW 

       550        560 
TLTSPPPEHT FEQLPKREDW ERAPAH

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.
[2]	"Crystallographic and online spectral evidence for role of conformational change and conserved water in cytochrome oxidase proton pump." Liu J., Qin L., Ferguson-Miller S. Proc. Natl. Acad. Sci. U.S.A. 108:1284-1289(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 17-551 IN COMPLEX WITH CALCIUM; COPPER AND HEME.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

CP000143 Genomic DNA. Translation: ABA78027.1.

RefSeq

YP_351928.1. NC_007493.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3OM3	X-ray	2.60	A/C	17-551	[»]
3OMA	X-ray	2.30	A/C	17-551	[»]
3OMI	X-ray	2.15	A/C	17-551	[»]
3OMN	X-ray	2.15	A/C	17-551	[»]

ProteinModelPortal

Q3J5A7.

SMR

Q3J5A7. Positions 14-560.

ModBase

Search...

Protein-protein interaction databases

STRING

272943.RSP_1877.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3719145.

KEGG

rsp:RSP_1877.

PATRIC

23150734. VBIRhoSph57909_0767.

Phylogenomic databases

eggNOG

COG0843.

HOGENOM

HOG000085274.

K02274.

OMA

FLIGGIM.

ProtClustDB

CLSK933538.

Enzyme and pathway databases

BioCyc

RSPH272943:GJAS-472-MONOMER.

Family and domain databases

Gene3D

1.20.210.10. 1 hit.

InterPro

IPR000883. Cyt_c_Oxase_su1.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR023616. Cyt_c_Oxase_su1_dom.
IPR014241. Cyt_c_oxidase_su1_bac.
[Graphical view]

PANTHER

PTHR10422. PTHR10422. 1 hit.

Pfam

PF00115. COX1. 1 hit.
[Graphical view]

PRINTS

PR01165. CYCOXIDASEI.

SUPFAM

SSF81442. COX1. 1 hit.

TIGRFAMs

TIGR02891. CtaD_CoxA. 1 hit.

PROSITE

PS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q3J5A7.

Entry information

Entry name

Q3J5A7_RHOS4

Accession

Primary (citable) accession number: Q3J5A7

Entry history

Integrated into UniProtKB/TrEMBL:	November 8, 2005
Last sequence update:	November 8, 2005
Last modified:	May 1, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information