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Q05572 (FIXN_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cytochrome c oxidase subunit 1 homolog, bacteroid
EC=1.9.3.1
Alternative name(s):
Cytochrome CBB3 subunit 1
Cytochrome c oxidase polypeptide I homolog
Heme B/copper cytochrome c oxidase subunit
Gene names
Name:fixN
Ordered Locus Names:RA0665
ORF Names:SMa1220
Encoded onPlasmid pSymA (megaplasmid 1)
OrganismRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]
Taxonomic identifier266834 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium ›

Protein attributes

Sequence length539 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c or a quinol are transferred to the bimetallic center formed by a high-spin heme and copper B.

Catalytic activity

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

Pathway

Energy metabolism; oxidative phosphorylation.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Developmental stage

Bacteroid (nitrogen-fixing endosymbiont).

Induction

By low oxygen levels.

Miscellaneous

This cytochrome oxidase is probably a cbb3-type.

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 539539Cytochrome c oxidase subunit 1 homolog, bacteroid
PRO_0000183470

Regions

Transmembrane4 – 2421Helical; Potential
Transmembrane28 – 4821Helical; Potential
Transmembrane75 – 9521Helical; Potential
Transmembrane118 – 13821Helical; Potential
Transmembrane154 – 17421Helical; Potential
Transmembrane187 – 20721Helical; Potential
Transmembrane214 – 23421Helical; Potential
Transmembrane265 – 28521Helical; Potential
Transmembrane298 – 31821Helical; Potential
Transmembrane330 – 35021Helical; Potential
Transmembrane368 – 38821Helical; Potential
Transmembrane405 – 42521Helical; Potential
Transmembrane443 – 46321Helical; Potential
Transmembrane475 – 49521Helical; Potential
Transmembrane499 – 51921Helical; Potential

Sites

Metal binding1171Iron (heme B axial ligand) Probable
Metal binding2661Copper B Probable
Metal binding3161Copper B Probable
Metal binding3171Copper B Probable
Metal binding4041Iron (high-spin heme B axial ligand) Probable
Metal binding4061Iron (heme B axial ligand) Probable

Sequences

Sequence LengthMass (Da)Tools
Q05572 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 6471FBF102719076

FASTA53960,869
        10         20         30         40         50         60 
MKHTVEMVVL SVGAFLALVG AGLAQDRLFG AHMWVLFFAL LAGTLVLMRR VDFRPAVAGH 

        70         80         90        100        110        120 
PGRRREYFDE VVKYGVVATV FWGVVGFLVG VVVALQLAFP ELNVEPWFNF GRVRPLHTSA 

       130        140        150        160        170        180 
VIFAFGGNAL IATSFYVVQR TSRARLFGGD LGWFVFWGYQ LFIVLAASGY LLGITQSREY 

       190        200        210        220        230        240 
AEPEWYVDLW LTIVWVAYLV AFLGTIMKRK EPHIYVANWF YLAFIVTIAM LHVVNNLAVP 

       250        260        270        280        290        300 
VSFLGSKSYS AFSGVQDALT QWWYGHNAVG FFLTAGFLAM MYYFIPKQVN RPVYSYRLSI 

       310        320        330        340        350        360 
IHFWAIIFMY IWAGPHHLHY TALPDWAQTL GMVFSIMLWM PSWGGMINGL MTLSGAWDKI 

       370        380        390        400        410        420 
RTDPVVRMMV MAVAFYGMAT FEGPMMSIKT VNSLSHYTDW TIGHVHSGAL GWNGLITFGA 

       430        440        450        460        470        480 
IYYLVPKLWN RERLYSVRMV NWHFWLATLG IVVYAAVMWV AGIQQGLMWR EYDDQGFLVY 

       490        500        510        520        530 
SFAETVAAMF PYYVMRAAGG ALFLAGALLM AFNVTMTILG RVRDEEPIFG AAPLPAPAE

« Hide

References

« Hide 'large scale' references
[1]Kahn D., Daveran-Mingot M.-L.
Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: RCR2011 / SU47.
[2]"Nucleotide sequence and predicted functions of the entire Sinorhizobium meliloti pSymA megaplasmid."
Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F., Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L., Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H. expand/collapse author list , Palm C., Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A., Long S.R.
Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.
[3]"The composite genome of the legume symbiont Sinorhizobium meliloti."
Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. expand/collapse author list , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.
Science 293:668-672(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z21854 Genomic DNA. Translation: CAA79901.1.
AE006469 Genomic DNA. Translation: AAK65323.1.
PIRA95345.
S39988.
RefSeqNP_435911.1. NC_003037.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING266834.SMa1220.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK65323; AAK65323; SMa1220.
GeneID1235701.
KEGGsme:SMa1220.
PATRIC23627812. VBISinMel96828_0685.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3278.
HOGENOMHOG000277908.
KOK00404.
OMALMWRATQ.
ProtClustDBPRK14488.

Enzyme and pathway databases

BioCycSMEL266834:GJF6-5673-MONOMER.
UniPathwayUPA00705.

Family and domain databases

Gene3D1.20.210.10. 1 hit.
InterProIPR000883. Cyt_c_Oxase_su1.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR023616. Cyt_c_Oxase_su1_dom.
IPR004677. Cyt_c_oxidase_cbb3_su1.
[Graphical view]
PANTHERPTHR10422. PTHR10422. 1 hit.
PfamPF00115. COX1. 1 hit.
[Graphical view]
SUPFAMSSF81442. COX1. 1 hit.
TIGRFAMsTIGR00780. ccoN. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFIXN_RHIME
AccessionPrimary (citable) accession number: Q05572
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents