CYF_MASLA
ID CYF_MASLA Reviewed; 333 AA.
AC P83793; Q5YJJ7;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Cytochrome f;
DE Flags: Precursor;
GN Name=petA;
OS Mastigocladus laminosus (Fischerella sp.).
OC Bacteria; Cyanobacteria; Nostocales; Hapalosiphonaceae; Mastigocladus.
OX NCBI_TaxID=83541;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Yan J., Zhang H., Cramer W.A.;
RT "Cloning and characterization of the petBD and petCA operon from the
RT thermophilic cyanobacterium Mastigocladus laminosus.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH HEME IN CYTOCHROME
RP B6-F COMPLEX, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND
RP TOPOLOGY.
RX PubMed=14526088; DOI=10.1126/science.1090165;
RA Kurisu G., Zhang H., Smith J.L., Cramer W.A.;
RT "Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning
RT the cavity.";
RL Science 302:1009-1014(2003).
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:0000305|PubMed:14526088}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000269|PubMed:14526088};
CC Note=Binds 1 heme group covalently. {ECO:0000269|PubMed:14526088};
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. {ECO:0000269|PubMed:14526088}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000269|PubMed:14526088}; Single-pass membrane protein
CC {ECO:0000269|PubMed:14526088}.
CC -!- SIMILARITY: Belongs to the cytochrome f family. {ECO:0000305}.
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DR EMBL; AY390356; AAR26241.1; -; Genomic_DNA.
DR PDB; 1VF5; X-ray; 3.00 A; C/P=45-333.
DR PDB; 2D2C; X-ray; 3.80 A; C/P=45-333.
DR PDB; 2E74; X-ray; 3.00 A; C=45-333.
DR PDB; 2E75; X-ray; 3.55 A; C=45-333.
DR PDB; 2E76; X-ray; 3.41 A; C=45-333.
DR PDB; 4H0L; X-ray; 3.25 A; C=45-333.
DR PDB; 4H13; X-ray; 3.07 A; C=45-333.
DR PDB; 4I7Z; X-ray; 2.80 A; C=45-333.
DR PDB; 4PV1; X-ray; 3.00 A; C=45-333.
DR PDBsum; 1VF5; -.
DR PDBsum; 2D2C; -.
DR PDBsum; 2E74; -.
DR PDBsum; 2E75; -.
DR PDBsum; 2E76; -.
DR PDBsum; 4H0L; -.
DR PDBsum; 4H13; -.
DR PDBsum; 4I7Z; -.
DR PDBsum; 4PV1; -.
DR AlphaFoldDB; P83793; -.
DR SMR; P83793; -.
DR DrugBank; DB08453; 2-Nonyl-4-quinolinol 1-oxide.
DR DrugBank; DB04646; Dibromothymoquinone.
DR EvolutionaryTrace; P83793; -.
DR GO; GO:0031361; C:integral component of thylakoid membrane; IEA:InterPro.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.40.830; -; 1.
DR HAMAP; MF_00610; Cytb6_f_cytF; 1.
DR InterPro; IPR024058; Cyt-f_TM.
DR InterPro; IPR002325; Cyt_f.
DR InterPro; IPR024094; Cyt_f_lg_dom.
DR InterPro; IPR036826; Cyt_f_lg_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR Pfam; PF01333; Apocytochr_F_C; 1.
DR Pfam; PF16639; Apocytochr_F_N; 1.
DR PRINTS; PR00610; CYTOCHROMEF.
DR SUPFAM; SSF103431; SSF103431; 1.
DR SUPFAM; SSF49441; SSF49441; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR PROSITE; PS51010; CYTF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Photosynthesis; Signal; Thylakoid; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT CHAIN 38..333
FT /note="Cytochrome f"
FT /id="PRO_0000207977"
FT TOPO_DOM 38..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:14526088"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:14526088"
FT TOPO_DOM 320..333
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305|PubMed:14526088"
FT BINDING 45
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:14526088"
FT BINDING 66
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:14526088"
FT BINDING 69
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:14526088"
FT BINDING 70
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:14526088"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:4I7Z"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2E74"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:4I7Z"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:4I7Z"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:4I7Z"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:4I7Z"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:4I7Z"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:4I7Z"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:4I7Z"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:4I7Z"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:4I7Z"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:4I7Z"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:4I7Z"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:4I7Z"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:4I7Z"
FT STRAND 189..200
FT /evidence="ECO:0007829|PDB:4I7Z"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:4I7Z"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:1VF5"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:2E74"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:4I7Z"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:2E74"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:4I7Z"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:2E74"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:4I7Z"
FT STRAND 283..293
FT /evidence="ECO:0007829|PDB:4I7Z"
FT HELIX 296..328
FT /evidence="ECO:0007829|PDB:4I7Z"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:2E76"
SQ SEQUENCE 333 AA; 36450 MW; E768F5C264323061 CRC64;
MRNSCKKARR TRPLKATIQA LLVAIATMTF FFTSDIALPQ SAAAYPFWAQ QTYPETPREP
TGRIVCANCH LAAKPAEVEV PQSVLPDTVF KAVVKIPYDT KLQQVAADGS KVGLNVGAVL
MLPEGFKIAP EERIPEELKK EVGDVYFQPY KEGQDNVLLV GPLPGEQYQE IVFPVLSPNP
TTDKNIHFGK YAIHLGANRG RGQIYPTGEK SNNNVFTASA TGTITKIAKE EDEYGNVKYQ
VSIQTDSGKT VVDTIPAGPE LIVSEGQAVK AGEALTNNPN VGGFGQDDTE IVLQDPNRVK
WMIAFICLVM LAQLMLILKK KQVEKVQAAE MNF
