EzCatDB: M00222
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DB codeM00222
CATH domainDomain 12.60.40.830 : Immunoglobulin-like
Domain 22.40.50.100 : OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Domain 31.20.810.10 : Cytochrome Bc1 Complex; Chain C
Domain 41.-.-.-
Domain 52.102.10.10 : Rieske Iron-sulfur ProteinCatalytic domain
Domain 61.20.5.510 : Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Domain 71.10.287.980 : Helix Hairpins
Domain 81.-.-.-
Domain 91.-.-.-
Domain 101.-.-.-
Domain 111.-.-.-
E.C.1.10.9.1

CATH domainRelated DB codes (homologues)
2.102.10.10 : Rieske Iron-sulfur ProteinT00024
2.40.50.100 : OB fold (Dihydrolipoamide Acetyltransferase, E2P)M00163,M00145,M00188,M00189,T00223,M00190,M00191,M00208

Enzyme Name
UniProtKBKEGG

P23577P16013Q00471P00165P49728P08980P23230P00166Q08362P69461P50369Q9M3L0Q42496P80883P0C1D4P61045
Protein nameApocytochrome fApocytochrome fCytochrome b6Cytochrome b6Cytochrome b6-f complex iron-sulfur subunit, chloroplasticCytochrome b6-f complex iron-sulfur subunit, chloroplasticCytochrome b6-f complex subunit 4Cytochrome b6-f complex subunit 4Cytochrome b6-f complex subunit 5Cytochrome b6-f complex subunit 5Cytochrome b6-f complex subunit 6Cytochrome b6-f complex subunit 6Cytochrome b6-f complex subunit 7, chloroplasticCytochrome b6-f complex subunit 7Cytochrome b6-f complex subunit 8, chloroplasticCytochrome b6-f complex subunit 8plastoquinol---plastocyanin reductase
plastoquinol/plastocyanin oxidoreductase
cytochrome b6/f complex
cytochrome b6/ complex
SynonymsNoneNoneNoneNoneEC 1.10.99.1
Rieske iron-sulfur protein
RISP
ISP
Plastohydroquinone:plastocyanin oxidoreductase iron-sulfur protein
EC 1.10.99.1
Rieske iron-sulfur protein
RISP
ISP
Plastohydroquinone:plastocyanin oxidoreductase iron-sulfur protein
17 kDa polypeptide
17 kDa polypeptide
Cytochrome b6-f complex subunit V
Cytochrome b6-f complex subunit petG
Cytochrome b6-f complex subunit V
Cytochrome b6-f complex subunit petG
Cytochrome b6-f complex subunit VI
Cytochrome b6-f complex subunit petL
Cytochrome b6-f complex subunit VI
Cytochrome b6-f complex subunit petL
Cytochrome b6-f complex subunit VII
Cytochrome b6-f complex subunit petM
Cytochrome b6-f complex 4 kDa subunit
Cytochrome b6-f complex subunit VII
Cytochrome b6-f complex subunit petM
Cytochrome b6-f complex subunit VIII
Cytochrome b6-f complex subunit petN
Cytochrome b6-f complex subunit VIII
Cytochrome b6-f complex subunit petN
RefSeqNP_958358.1 (Protein)
NC_005353.1 (DNA/RNA sequence)
NP_054949.1 (Protein)
NC_002202.1 (DNA/RNA sequence)
NP_958365.1 (Protein)
NC_005353.1 (DNA/RNA sequence)
NP_054964.1 (Protein)
NC_002202.1 (DNA/RNA sequence)
XP_001698786.1 (Protein)
XM_001698734.1 (DNA/RNA sequence)

NP_958359.1 (Protein)
NC_005353.1 (DNA/RNA sequence)
NP_054965.1 (Protein)
NC_002202.1 (DNA/RNA sequence)
NP_958401.1 (Protein)
NC_005353.1 (DNA/RNA sequence)
NP_054954.1 (Protein)
NC_002202.1 (DNA/RNA sequence)
NP_958424.2 (Protein)
NC_005353.1 (DNA/RNA sequence)
NP_054953.1 (Protein)
NC_002202.1 (DNA/RNA sequence)
XP_001694096.1 (Protein)
XM_001694044.1 (DNA/RNA sequence)

XP_001698251.1 (Protein)
XM_001698199.1 (DNA/RNA sequence)
NP_054925.1 (Protein)
NC_002202.1 (DNA/RNA sequence)
PfamPF01333 (Apocytochr_F_C)
[Graphical view]
PF01333 (Apocytochr_F_C)
[Graphical view]
PF13631 (Cytochrom_B_N_2)
[Graphical view]
PF00033 (Cytochrom_B_N)
[Graphical view]
PF08802 (CytB6-F_Fe-S)
PF00355 (Rieske)
[Graphical view]
PF08802 (CytB6-F_Fe-S)
PF00355 (Rieske)
[Graphical view]
PF00032 (Cytochrom_B_C)
[Graphical view]
PF00032 (Cytochrom_B_C)
[Graphical view]
PF02529 (PetG)
[Graphical view]
PF02529 (PetG)
[Graphical view]
PF05115 (PetL)
[Graphical view]
PF05115 (PetL)
[Graphical view]
PF08041 (PetM)
[Graphical view]
PF08041 (PetM)
[Graphical view]
PF03742 (PetN)
[Graphical view]
PF03742 (PetN)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00195Photosynthesis

UniProtKB:Accession NumberP23577P16013Q00471P00165P49728P08980P23230P00166Q08362P69461P50369Q9M3L0Q42496P80883P0C1D4P61045
Entry nameCYF_CHLRECYF_SPIOLCYB6_CHLRECYB6_SPIOLUCRIA_CHLREUCRIA_SPIOLPETD_CHLREPETD_SPIOLPETG_CHLREPETG_SPIOLPETL_CHLREPETL_SPIOLPETM_CHLREPETM_SPIOLPETN_CHLREPETN_SPIOL
Activity



Plastoquinol-1 + 2 oxidized plastocyanin = plastoquinone + 2 reduced plastocyanin.Plastoquinol-1 + 2 oxidized plastocyanin = plastoquinone + 2 reduced plastocyanin.









SubunitThe 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are petG, petL, petM and petN. The complex functions as a dimer.The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are petG, petL, petM and petN. The complex functions as a dimer (By similarity).The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are petG, petL, petM and petN. The complex functions as a dimer.The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are petG, petL, petM and petN. The complex functions as a dimer (By similarity).The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are petG, petL, petM and petN. The complex functions as a dimer.The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are petG, petL, petM and petN. The complex functions as a dimer (By similarity).The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are petG, petL, petM and petN. The complex functions as a dimer.The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are petG, petL, petM and petN. The complex functions as a dimer (By similarity).The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are petG, petL, petM and petN. The complex functions as a dimer.The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are petG, petL, petM and petN. The complex functions as a dimer (By similarity).The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are petG, petL, petM and petN. The complex functions as a dimer (By similarity).The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are petG, petL, petM and petN. The complex functions as a dimer (By similarity).The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are petG, petL, petM and petN. The complex functions as a dimer.The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are petG, petL, petM and petN. The complex functions as a dimer (By similarity).The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are petG, petL, petM and petN. The complex functions as a dimer.The 4 large subunits of the cytochrome b6-f complex are cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and the Rieske protein, while the 4 small subunits are petG, petL, petM and petN. The complex functions as a dimer (By similarity).
Subcellular locationPlastid, chloroplast thylakoid membrane, Single-pass membrane protein.Plastid, chloroplast thylakoid membrane, Single-pass membrane protein (By similarity).Plastid, chloroplast thylakoid membrane, Multi-pass membrane protein.Plastid, chloroplast thylakoid membrane, Multi-pass membrane protein (By similarity).Plastid, chloroplast thylakoid membrane, Single-pass membrane protein. Note=The transmembrane helix obliquely spans the membrane in one monomer, and its extrinsic C- terminal domain is part of the other monomer.Plastid, chloroplast thylakoid membrane, Single-pass membrane protein (By similarity). Note=The transmembrane helix obliquely spans the membrane in one monomer, and its extrinsic C-terminal domain is part of the other monomer (By similarity).Plastid, chloroplast thylakoid membrane, Multi-pass membrane protein.Plastid, chloroplast thylakoid membrane, Multi-pass membrane protein (By similarity).Plastid, chloroplast thylakoid membrane, Single-pass membrane protein.Plastid, chloroplast thylakoid membrane, Single-pass membrane protein (By similarity).Plastid, chloroplast thylakoid membrane, Single-pass membrane protein (By similarity).Plastid, chloroplast thylakoid membrane, Single-pass membrane protein (By similarity).Plastid, chloroplast thylakoid membrane, Single-pass membrane protein.Plastid, chloroplast thylakoid membrane, Single-pass membrane protein (By similarity).Plastid, chloroplast thylakoid membrane, Single-pass membrane protein.Plastid, chloroplast thylakoid membrane, Single-pass membrane protein (By similarity).
CofactorBinds 1 heme group covalently.Binds 1 heme group covalently (By similarity).Binds 2 heme groups. One heme group is bound covalently by a single cysteine link, the other one non-covalently.Binds 2 heme groups. One heme group is bound covalently by a single cysteine link, the other one non-covalently.Binds 1 2Fe-2S cluster per subunit.Binds 1 2Fe-2S cluster per subunit.










Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00032L00023C05306C16693C03162C02061C03025
CompoundHeme[2Fe-2S]Chlorophyll aPlastoquinolOxidized plastocyaninPlastoquinoneReduced plastocyanin
Typearomatic ring (with nitrogen atoms),carboxyl group,heavy metalheavy metal,sulfide grouparomatic ring (with nitrogen atoms),carbohydrate,divalent metal (Ca2+, Mg2+),lipidaromatic ring (only carbon atom),lipidheavy metal,peptide/proteinaromatic ring (only carbon atom),lipidheavy metal,peptide/protein
ChEBI17627
26355
33739
18230
16323

80663

PubChem

44602414
16667503
12085802
24892729

10219885

               
1q90A01Bound:HEMUnboundUnboundUnboundUnboundUnboundUnbound
1q90A02UnboundUnboundUnboundUnboundUnboundUnboundUnbound
1q90BBound:3xHEMUnboundUnboundUnboundUnboundUnboundUnbound
1q90RUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1q90CUnboundBound:FESUnboundUnboundUnboundAnalogue:TDSUnbound
1rfsAUnboundBound:FESUnboundUnboundUnboundUnboundUnbound
1q90DUnboundUnboundBound:CL1UnboundUnboundUnboundUnbound
1q90GUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1q90LUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1q90MUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1q90NUnboundUnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
literature [14], [15]
pdbCatalytic residuesCofactor-binding residues
          
1q90A01 
TYR 1;HIS 25(Fe binding);CYS 21;CYS 24(Porphyrin binding)
1q90A02 
 
1q90B 
CYS 35(Porphyrin-3 binding);HIS 86;HIS 187(Fe-2 binding);HIS 100;HIS 202(Fe-1 binding)
1q90R 
 
1q90CHIS 155
CYS 134;HIS 136;CYS 152;HIS 155(2Fe-2S cluster binding)
1rfsAHIS 128
CYS 107;HIS 109;CYS 125;HIS 128(2Fe-2S cluster binding)
1q90D 
 
1q90G 
 
1q90L 
 
1q90M 
 
1q90N 
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]p.1617, p.1620, p.1622
[11]

[12]

[13]p.20931-20932
[14]p.415-417
[15]Fig.2, p.1014
[17]p.5925-5926
[19]p.16334-16335

references
[1]
PubMed ID1847076
JournalBiochemistry
Year1991
Volume30
Pages1892-901
AuthorsBritt RD, Sauer K, Klein MP, Knaff DB, Kriauciunas A, Yu CA, Yu L, Malkin R
TitleElectron spin echo envelope modulation spectroscopy supports the suggested coordination of two histidine ligands to the Rieske Fe-S centers of the cytochrome b6f complex of spinach and the cytochrome bc1 complexes of Rhodospirillum rubrum, Rhodobacter sphaeroides R-26, and bovine heart mitochondria.
[2]
PubMed ID8394319
JournalJ Bioenerg Biomembr
Year1993
Volume25
Pages233-44
AuthorsBeattie DS
TitleA proposed pathway of proton translocation through the bc complexes of mitochondria and chloroplasts.
[3]
CommentsX-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 104-230.
PubMed ID9438861
JournalStructure
Year1997
Volume5
Pages1613-25
AuthorsCarrell CJ, Zhang H, Cramer WA, Smith JL
TitleBiological identity and diversity in photosynthesis and respiration: structure of the lumen-side domain of the chloroplast Rieske protein.
Related PDB1rfs
Related UniProtKBP08980
[4]
PubMed ID10423236
JournalBiochemistry
Year1999
Volume38
Pages9590-9
AuthorsCarrell CJ, Schlarb BG, Bendall DS, Howe CJ, Cramer WA, Smith JL
TitleStructure of the soluble domain of cytochrome f from the cyanobacterium Phormidium laminosum.
[5]
PubMed ID10359083
JournalFEBS Lett
Year1999
Volume450
Pages245-50
AuthorsSchoepp B, Brugna M, Riedel A, Nitschke W, Kramer DM
TitleThe Qo-site inhibitor DBMIB favours the proximal position of the chloroplast Rieske protein and induces a pK-shift of the redox-linked proton.
[6]
PubMed ID10591526
JournalJ Bioenerg Biomembr
Year1999
Volume31
Pages201-13
AuthorsSoriano GM, Ponamarev MV, Carrell CJ, Xia D, Smith JL, Cramer WA
TitleComparison of the cytochrome bc1 complex with the anticipated structure of the cytochrome b6f complex: Le plus ca change le plus c'est la meme chose.
[7]
PubMed ID11004464
JournalBiochim Biophys Acta
Year2000
Volume1459
Pages467-74
AuthorsBreyton C
TitleThe cytochrome b(6)f complex: structural studies and comparison with the bc(1) complex.
[8]
PubMed ID11460929
JournalJ Bioenerg Biomembr
Year2001
Volume33
Pages9-26
AuthorsSchmidt CL, Shaw L
TitleA comprehensive phylogenetic analysis of Rieske and Rieske-type iron-sulfur proteins.
[9]
PubMed ID11526115
JournalJ Biol Chem
Year2001
Volume276
Pages42761-6
AuthorsMolik S, Karnauchov I, Weidlich C, Herrmann RG, Klosgen RB
TitleThe Rieske Fe/S protein of the cytochrome b6/f complex in chloroplasts: missing link in the evolution of protein transport pathways in chloroplasts?
[10]
PubMed ID11788579
JournalJ Biol Chem
Year2002
Volume277
Pages10949-54
AuthorsSchneider D, Skrzypczak S, Anemuller S, Schmidt CL, Seidler A, Rogner M
TitleHeterogeneous Rieske proteins in the cytochrome b6f complex of Synechocystis PCC6803?
[11]
PubMed ID12207018
JournalJ Biol Chem
Year2002
Volume277
Pages41865-71
AuthorsSoriano GM, Guo LW, De Vitry C, Kallas T, Cramer WA
TitleElectron transfer from the Rieske iron-sulfur protein (ISP) to cytochrome f in vitro. Is a guided trajectory of the ISP necessary for competent docking?
[12]
PubMed ID12944318
JournalBiophys J
Year2003
Volume85
Pages2055-68
AuthorsGross EL, Pearson DC Jr
TitleBrownian dynamics simulations of the interaction of Chlamydomonas cytochrome f with plastocyanin and cytochrome c6.
[13]
PubMed ID12672829
JournalJ Biol Chem
Year2003
Volume278
Pages20925-33
AuthorsYan J, Cramer WA
TitleFunctional insensitivity of the cytochrome b6f complex to structure changes in the hinge region of the Rieske iron-sulfur protein.
[14]
CommentsX-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 31-206.
PubMed ID14647374
JournalNature
Year2003
Volume426
Pages413-8
AuthorsStroebel D, Choquet Y, Popot JL, Picot D
TitleAn atypical haem in the cytochrome b(6)f complex.
Related PDB1q90
Related UniProtKBP49728
[15]
PubMed ID14526088
JournalScience
Year2003
Volume302
Pages1009-14
AuthorsKurisu G, Zhang H, Smith JL, Cramer WA
TitleStructure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity.
[16]
PubMed ID14585099
JournalBiochem J
Year2004
Volume378
Pages45-51
AuthorsCrowley PB, Hunter DM, Sato K, McFarlane W, Dennison C
TitleThe parsley plastocyanin-turnip cytochrome f complex: a structurally distorted but kinetically functional acidic patch.
[17]
PubMed ID15147175
JournalBiochemistry
Year2004
Volume43
Pages5921-9
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TitleEvolution of photosynthesis: time-independent structure of the cytochrome b6f complex.
[18]
PubMed ID15196013
JournalBiochemistry
Year2004
Volume43
Pages7707-16
AuthorsRoberts AG, Bowman MK, Kramer DM
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[19]
PubMed ID15610027
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Year2004
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[20]
PubMed ID15313237
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Year2004
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[21]
PubMed ID15316016
JournalJ Biol Chem
Year2004
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Pages44621-7
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[22]
PubMed ID15522300
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Year2004
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[23]
PubMed ID15003236
JournalTrends Plant Sci
Year2004
Volume9
Pages130-7
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TitleCytochrome b6f: structure for signalling and vectorial metabolism.

comments
This enzyme, Rieske iron-sulfur protein, is a component of cytochrome b6/f complex. This enzyme transfers electrons from plastoquinol to plastocyanin, a copper-containing protein. The electrons transferred to the plastocyanin are donated to a heam cofactor of cytochrome f, which is also a component of cycochrome b6/f complex.
The cytochrome b6/f complex is composed of four large subunits and four small subunits:
The large subunits are:
cytochrome b6: Swiss-prot;Q00471, PDB;1q90 chain B,
subunit IV (or petD): Swiss-prot;P23230, PDB;1q90 chain D,
cytochrome f: Swiss-prot;P23577, PDB;1q90 chain A,
Rieske iron-sulfur protein (ISP): Swiss-prot;P49728, P08980 (PDB;1q90 chains R/C & 1rfs).
The small subunits are:
petG: Swiss-prot;Q08362, PDB;1q90 chain G,
petL: Swiss-prot;P50369, PDB;1q90 chain L,
petM: Swiss-prot;Q42496, PDB;1q90 chain M,
petN: Swiss-prot;P61045, PDB;1q90 chain N

createdupdated
2004-01-292012-10-02


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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