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
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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.
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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.
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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:
- X-ray crystallography (ethanol ((v/v)) 5 %; MgCl2 100 mM; NaCl 100 mM; PEG 1500 (approximately (w/v)) 9 %)
| References:
- 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
- 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:
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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:
- X-ray crystallography (ethanol ((v/v)) 5 %; MgCl2 100 mM; NaCl 100 mM; PEG 1500 (approximately (w/v)) 9 %)
| References:
- 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
- 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:
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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:
- X-ray crystallography (ethanol ((v/v)) 5 %; MgCl2 100 mM; NaCl 100 mM; PEG 1500 (approximately (w/v)) 9 %)
| References:
- 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
- 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:
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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:
- X-ray crystallography (ethanol ((v/v)) 5 %; MgCl2 100 mM; NaCl 100 mM; PEG 1500 (approximately (w/v)) 9 %)
| References:
- 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
- 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:
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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:
- X-ray crystallography (ethanol ((v/v)) 5 %; MgCl2 100 mM; NaCl 100 mM; PEG 1500 (approximately (w/v)) 9 %)
| References:
- 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
- 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:
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References |
- 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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