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UCRIA_SPIOL
ID   UCRIA_SPIOL             Reviewed;         230 AA.
AC   P08980;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Cytochrome b6-f complex iron-sulfur subunit, chloroplastic;
DE            EC=7.1.1.6;
DE   AltName: Full=Plastohydroquinone:plastocyanin oxidoreductase iron-sulfur protein;
DE   AltName: Full=Rieske iron-sulfur protein;
DE            Short=ISP;
DE            Short=RISP;
DE   Flags: Precursor;
GN   Name=petC;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Monatol;
RA   Steppuhn J., Rother C., Hermans J., Jansen T., Salnikow J., Hauska G.,
RA   Herrmann R.G.;
RT   "The complete amino-acid sequence of the Rieske FeS-precursor protein from
RT   spinach chloroplasts deduced from cDNA analysis.";
RL   Mol. Gen. Genet. 210:171-177(1987).
RN   [2]
RP   PROTEIN SEQUENCE OF 52-147.
RA   Pfefferkorn B., Meyer H.E.;
RT   "N-terminal amino acid sequence of the Rieske iron-sulfur protein from the
RT   cytochrome b6/f-complex of spinach thylakoids.";
RL   FEBS Lett. 206:233-237(1986).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 92-230 IN COMPLEX WITH 2FE-2S
RP   CLUSTER, AND COFACTOR.
RX   PubMed=9438861; DOI=10.1016/s0969-2126(97)00309-2;
RA   Carrell C.J., Zhang H., Cramer W.A., Smith J.L.;
RT   "Biological identity and diversity in photosynthesis and respiration:
RT   structure of the lumen-side domain of the chloroplast Rieske protein.";
RL   Structure 5:1613-1625(1997).
CC   -!- FUNCTION: Component of the cytochrome b6-f complex, which mediates
CC       electron transfer between photosystem II (PSII) and photosystem I
CC       (PSI), cyclic electron flow around PSI, and state transitions.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinol + 2 H(+)(in) + 2 oxidized [plastocyanin] = a
CC         plastoquinone + 4 H(+)(out) + 2 reduced [plastocyanin];
CC         Xref=Rhea:RHEA:22148, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562,
CC         Rhea:RHEA-COMP:10039, Rhea:RHEA-COMP:10040, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17757, ChEBI:CHEBI:29036, ChEBI:CHEBI:49552,
CC         ChEBI:CHEBI:62192; EC=7.1.1.6;
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000269|PubMed:9438861};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit.
CC       {ECO:0000269|PubMed:9438861};
CC   -!- SUBUNIT: The 4 large subunits of the cytochrome b6-f complex are
CC       cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and
CC       the Rieske protein, while the 4 small subunits are petG, petL, petM and
CC       petN. The complex functions as a dimer (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000305|PubMed:9438861}; Single-pass membrane protein
CC       {ECO:0000305|PubMed:9438861}. Note=The transmembrane helix obliquely
CC       spans the membrane in one monomer, and its extrinsic C-terminal domain
CC       is part of the other monomer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: This protein is 1 of 2 subunits of the cytochrome b6-f
CC       complex that are encoded in the nucleus.
CC   -!- MISCELLANEOUS: The Rieske iron-sulfur protein is a high potential 2Fe-
CC       2S protein.
CC   -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_01335}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA29590.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X06244; CAA29590.1; ALT_INIT; mRNA.
DR   PIR; S00454; S00454.
DR   PDB; 1RFS; X-ray; 1.83 A; A=92-230.
DR   PDB; 6RQF; EM; 3.58 A; D/L=52-230.
DR   PDBsum; 1RFS; -.
DR   PDBsum; 6RQF; -.
DR   AlphaFoldDB; P08980; -.
DR   SMR; P08980; -.
DR   IntAct; P08980; 1.
DR   PRIDE; P08980; -.
DR   EvolutionaryTrace; P08980; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0045158; F:electron transporter, transferring electrons within cytochrome b6/f complex of photosystem II activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009496; F:plastoquinol--plastocyanin reductase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.102.10.10; -; 1.
DR   HAMAP; MF_01335; Cytb6_f_Rieske; 1.
DR   InterPro; IPR023960; Cyt_b6_f_Rieske.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR014349; Rieske_Fe-S_prot.
DR   InterPro; IPR005805; Rieske_Fe-S_prot_C.
DR   PANTHER; PTHR10134; PTHR10134; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   PRINTS; PR00162; RIESKE.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; 3D-structure; Chloroplast; Direct protein sequencing;
KW   Disulfide bond; Electron transport; Iron; Iron-sulfur; Membrane;
KW   Metal-binding; Plastid; Thylakoid; Transit peptide; Translocase;
KW   Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT         1..51
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           52..230
FT                   /note="Cytochrome b6-f complex iron-sulfur subunit,
FT                   chloroplastic"
FT                   /id="PRO_0000030693"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          116..212
FT                   /note="Rieske"
FT   BINDING         158
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000269|PubMed:9438861"
FT   BINDING         160
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000269|PubMed:9438861"
FT   BINDING         176
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000269|PubMed:9438861"
FT   BINDING         179
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000269|PubMed:9438861"
FT   DISULFID        163..178
FT                   /evidence="ECO:0000269|PubMed:9438861"
FT   HELIX           116..122
FT                   /evidence="ECO:0007829|PDB:1RFS"
FT   STRAND          128..132
FT                   /evidence="ECO:0007829|PDB:1RFS"
FT   HELIX           134..136
FT                   /evidence="ECO:0007829|PDB:1RFS"
FT   STRAND          138..143
FT                   /evidence="ECO:0007829|PDB:1RFS"
FT   STRAND          147..149
FT                   /evidence="ECO:0007829|PDB:1RFS"
FT   STRAND          151..155
FT                   /evidence="ECO:0007829|PDB:1RFS"
FT   TURN            159..161
FT                   /evidence="ECO:0007829|PDB:1RFS"
FT   TURN            169..172
FT                   /evidence="ECO:0007829|PDB:1RFS"
FT   STRAND          173..175
FT                   /evidence="ECO:0007829|PDB:1RFS"
FT   TURN            177..179
FT                   /evidence="ECO:0007829|PDB:1RFS"
FT   STRAND          182..184
FT                   /evidence="ECO:0007829|PDB:1RFS"
FT   STRAND          189..193
FT                   /evidence="ECO:0007829|PDB:1RFS"
FT   STRAND          200..206
FT                   /evidence="ECO:0007829|PDB:1RFS"
FT   STRAND          209..214
FT                   /evidence="ECO:0007829|PDB:1RFS"
FT   TURN            220..222
FT                   /evidence="ECO:0007829|PDB:1RFS"
SQ   SEQUENCE   230 AA;  24325 MW;  FA2C54B4C6586059 CRC64;
     MASFTLSSAT PSQLCSSKNG MFAPSLALAK AGRVNVLISK ERIRGMKLTC QATSIPADNV
     PDMQKRETLN LLLLGALSLP TGYMLLPYAS FFVPPGGGAG TGGTIAKDAL GNDVIAAEWL
     KTHAPGDRTL TQGLKGDPTY LVVESDKTLA TFGINAVCTH LGCVVPFNAA ENKFICPCHG
     SQYNNQGRVV RGPAPLSLAL AHCDVDDGKV VFVPWTETDF RTGEAPWWSA
 
 
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