DP00088: Ubiquinol oxidase subunit 1FASTA viewXML view

General information
DisProt:DP00088
Name:Ubiquinol oxidase subunit 1
Synonym(s):CYOB_ECOLI
Ubiquinol oxidase polypeptide I
Cytochrome o subunit 1
Oxidase BO(3) subunit 1
Cytochrome o ubiquinol oxidase subunit 1
Ubiquinol oxidase chain A
First appeared in release:Release 1.0 (08/01/2003)
UniProt:P0ABI8
UniGene: 
SwissProt: CYOB_ECOLI
TrEMBL:  
NCBI (GI): 78099993
Source organism:Escherichia coli (strain K12)
Sequence length:663
Percent disordered:30%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MFGKLSLDAV PFHEPIVMVT IAGIILGGLA LVGLITYFGK WTYLWKEWLT SVDHKRLGIM - 60
YIIVAIVMLL RGFADAIMMR SQQALASAGE AGFLPPHHYD QIFTAHGVIM IFFVAMPFVI - 120
GLMNLVVPLQ IGARDVAFPF LNNLSFWFTV VGVILVNVSL GVGEFAQTGW LAYPPLSGIE - 180
YSPGVGVDYW IWSLQLSGIG TTLTGINFFV TILKMRAPGM TMFKMPVFTW ASLCANVLII - 240
ASFPILTVTV ALLTLDRYLG THFFTNDMGG NMMMYINLIW AWGHPEVYIL ILPVFGVFSE - 300
IAATFSRKRL FGYTSLVWAT VCITVLSFIV WLHHFFTMGA GANVNAFFGI TTMIIAIPTG - 360
VKIFNWLFTM YQGRIVFHSA MLWTIGFIVT FSVGGMTGVL LAVPGADFVL HNSLFLIAHF - 420
HNVIIGGVVF GCFAGMTYWW PKAFGFKLNE TWGKRAFWFW IIGFFVAFMP LYALGFMGMT - 480
RRLSQQIDPQ FHTMLMIAAS GAVLIALGIL CLVIQMYVSI RDRDQNRDLT GDPWGGRTLE - 540
WATSSPPPFY NFAVVPHVHE RDAFWEMKEK GEAYKKPDHY EEIHMPKNSG AGIVIAAFST - 600
IFGFAMIWHI WWLAIVGFAG MIITWIVKSF DEDVDYYVPV AEIEKLENQH FDEITKAGLK - 660
NGN



Functional narrative    

Ubiquinol oxidase polypeptide I is a protein that is one of four subunits with cofactors protoheme IX (heme b55 and b562) and copper B. It is a heteroctamer of two A chains, two B chains, two C chains and two D chains The overall structure of the enzyme is similar to those of cytochrome c oxidases; however, the memebane spanning region of subunit I contains a cluster of polar residues exposed to the interior of the lipid bilayer that is not present in cytochrome c oxidases. The protein works to catalyze O2 reduction to water and uses available free energy to drive a proton pump gradient across the membrane during respiration in E.coli. Ubiquinol oxidase also catalyzes the terminal step in the electron transport chain. All of the centers of reduction-oxidation are located in this subunit. The protein is a member of the heme-copper respiratory oxidase family.

Region 1: 1-51 Region 3: 82-95 Region 4: 180-185 Region 5: 521-540 Region 2: 553-663

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name: 
Location:1 - 51
Length:51
Region sequence:

MFGKLSLDAVPFHEPIVMVTIAGIILGGLALVGLITYFGKWTYLWKEWLTS

Modification type: Engineered
PDB: 1FFT:A, 1FFT:F
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography (ethanol ((v/v)) 5 %; MgCl2 100 mM; NaCl 100 mM; PEG 1500 (approximately (w/v)) 9 %)

References:
  1. Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M. "The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site." Nat Struct Biol. 2000; 7(10): 910-7. PubMed: 11017202

  2. Chepuri V, Lemieux L, Au DC, Gennis RB. "The sequence of the cyo operon indicates substantial structural similarities between the cytochrome o ubiquinol oxidase of Escherichia coli and the aa3-type family of cytochrome c oxidases." J Biol Chem. 1990; 265(19): 11185-92. PubMed: 2162835

Comments:
 



Region 2
Type:Disordered
Name: 
Location:553 - 663
Length:111
Region sequence:

AVVPHVHERDAFWEMKEKGEAYKKPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWW
LAIVGFAGMIITWIVKSFDEDVDYYVPVAEIEKLENQHFDEITKAGLKNGN

Modification type: Engineered
PDB: 1FFT:A, 1FFT:F
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography (ethanol ((v/v)) 5 %; MgCl2 100 mM; NaCl 100 mM; PEG 1500 (approximately (w/v)) 9 %)

References:
  1. Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M. "The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site." Nat Struct Biol. 2000; 7(10): 910-7. PubMed: 11017202

  2. Chepuri V, Lemieux L, Au DC, Gennis RB. "The sequence of the cyo operon indicates substantial structural similarities between the cytochrome o ubiquinol oxidase of Escherichia coli and the aa3-type family of cytochrome c oxidases." J Biol Chem. 1990; 265(19): 11185-92. PubMed: 2162835

Comments:
 



Region 3
Type:Disordered
Name: 
Location:82 - 95
Length:14
Region sequence:

QQALASAGEAGFLP

Modification type: Engineered
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography (ethanol ((v/v)) 5 %; MgCl2 100 mM; NaCl 100 mM; PEG 1500 (approximately (w/v)) 9 %)

References:
  1. Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M. "The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site." Nat Struct Biol. 2000; 7(10): 910-7. PubMed: 11017202

  2. Chepuri V, Lemieux L, Au DC, Gennis RB. "The sequence of the cyo operon indicates substantial structural similarities between the cytochrome o ubiquinol oxidase of Escherichia coli and the aa3-type family of cytochrome c oxidases." J Biol Chem. 1990; 265(19): 11185-92. PubMed: 2162835

Comments:
 



Region 4
Type:Disordered
Name: 
Location:180 - 185
Length:6
Region sequence:

EYSPGV

Modification type: Engineered
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography (ethanol ((v/v)) 5 %; MgCl2 100 mM; NaCl 100 mM; PEG 1500 (approximately (w/v)) 9 %)

References:
  1. Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M. "The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site." Nat Struct Biol. 2000; 7(10): 910-7. PubMed: 11017202

  2. Chepuri V, Lemieux L, Au DC, Gennis RB. "The sequence of the cyo operon indicates substantial structural similarities between the cytochrome o ubiquinol oxidase of Escherichia coli and the aa3-type family of cytochrome c oxidases." J Biol Chem. 1990; 265(19): 11185-92. PubMed: 2162835

Comments:
 



Region 5
Type:Disordered
Name: 
Location:521 - 540
Length:20
Region sequence:

RDRDQNRDLTGDPWGGRTLE

Modification type: Engineered
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography (ethanol ((v/v)) 5 %; MgCl2 100 mM; NaCl 100 mM; PEG 1500 (approximately (w/v)) 9 %)

References:
  1. Abramson J, Riistama S, Larsson G, Jasaitis A, Svensson-Ek M, Laakkonen L, Puustinen A, Iwata S, Wikstrom M. "The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site." Nat Struct Biol. 2000; 7(10): 910-7. PubMed: 11017202

  2. Chepuri V, Lemieux L, Au DC, Gennis RB. "The sequence of the cyo operon indicates substantial structural similarities between the cytochrome o ubiquinol oxidase of Escherichia coli and the aa3-type family of cytochrome c oxidases." J Biol Chem. 1990; 265(19): 11185-92. PubMed: 2162835

Comments:
 



References

  1. Wilmanns M, Lappalainen P, Kelly M, Sauer-Eriksson E, Saraste M. "Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper center." Proc Natl Acad Sci U S A. 1995; 92(26): 11955-9. PubMed: 8618822


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