CHLF_CHLFP
ID CHLF_CHLFP Reviewed; 376 AA.
AC P0DOC9;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Light-dependent chlorophyll f synthase {ECO:0000303|PubMed:27386923};
DE Short=Chl f synthase {ECO:0000303|PubMed:27386923};
DE EC=1.-.-.-;
DE AltName: Full=Super-rogue PsbA4 {ECO:0000303|PubMed:27386923};
DE Short=Sr-PsbA4 {ECO:0000303|PubMed:27386923};
GN Name=chlF {ECO:0000303|PubMed:27386923};
GN Synonyms=psbA4 {ECO:0000303|PubMed:27386923}; ORFNames=UYEDRAFT_01161;
OS Chlorogloeopsis fritschii (strain PCC 9212).
OC Bacteria; Cyanobacteria; Nostocales; Chlorogloeopsidaceae; Chlorogloeopsis.
OX NCBI_TaxID=184925;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23221676; DOI=10.1093/gbe/evs117;
RA Dagan T., Roettger M., Stucken K., Landan G., Koch R., Major P.,
RA Gould S.B., Goremykin V.V., Rippka R., Tandeau de Marsac N., Gugger M.,
RA Lockhart P.J., Allen J.F., Brune I., Maus I., Puehler A., Martin W.F.;
RT "Genomes of Stigonematalean cyanobacteria (subsection V) and the evolution
RT of oxygenic photosynthesis from prokaryotes to plastids.";
RL Genome Biol. Evol. 5:31-44(2013).
RN [2]
RP FUNCTION, SUBUNIT, INDUCTION BY FAR RED LIGHT, AND DISRUPTION PHENOTYPE.
RX PubMed=27386923; DOI=10.1126/science.aaf9178;
RA Ho M.Y., Shen G., Canniffe D.P., Zhao C., Bryant D.A.;
RT "Light-dependent chlorophyll f synthase is a highly divergent paralog of
RT PsbA of photosystem II.";
RL Science 0:0-0(2016).
CC -!- FUNCTION: Synthesizes chlorophyll f or chlorophyllide f (Chl f, 2-
CC formyl chlorophyll a), probably by oxidation of chlorophyll a or
CC chlorophyllide a and reduction of plastoquinone. The reaction is
CC probably light-dependent (PubMed:27386923). Chl f absorbs far red light
CC (FRL, 707 nm in 100% methanol), and is synthesized when cells are grown
CC in FRL, where it provides the advantage of extending the spectral range
CC of harvested light in terrestrial cyanobacteria (PubMed:27386923). When
CC ectopically expressed in Synechococcus PCC 7002 (which does not grow in
CC FRL and does not make Chl f) produces Chl f (0.059% of total
CC chlorophyll) (PubMed:27386923). {ECO:0000269|PubMed:27386923}.
CC -!- SUBUNIT: Homodimer (PubMed:27386923). {ECO:0000305|PubMed:27386923}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:P51765}.
CC -!- INDUCTION: By growth in FRL (705-735 nm, 26-30 umol photons/m(2)/s)
CC (PubMed:27386923). {ECO:0000269|PubMed:27386923}.
CC -!- DISRUPTION PHENOTYPE: No synthesis of chlorophyll f when grown in FRL
CC (PubMed:27386923), decreased accumulation of some proteins up-regulated
CC during FRL photoacclimation (FaRLiP). {ECO:0000269|PubMed:27386923}.
CC -!- MISCELLANEOUS: Due to differences in the C-terminus this protein cannot
CC bind the oxygen-evolving Mn4-Ca-O5 cluster bound by 'normal' PsbA,
CC however it probably still binds plastoquinone and chlorophyll
CC (PubMed:27386923). {ECO:0000303|PubMed:27386923}.
CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
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DR EMBL; AJLM01000026; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0DOC9; -.
DR SMR; P0DOC9; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
DR GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036067; P:light-dependent chlorophyll biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR Gene3D; 1.20.85.10; -; 1.
DR InterPro; IPR036854; Photo_II_D1/D2_sf.
DR InterPro; IPR000484; Photo_RC_L/M.
DR PANTHER; PTHR33149; PTHR33149; 1.
DR Pfam; PF00124; Photo_RC; 1.
DR PRINTS; PR00256; REACTNCENTRE.
DR SUPFAM; SSF81483; SSF81483; 1.
DR PROSITE; PS00244; REACTION_CENTER; 1.
PE 1: Evidence at protein level;
KW Chlorophyll; Chlorophyll biosynthesis; Chromophore; Magnesium; Membrane;
KW Metal-binding; Oxidoreductase; Photosynthesis; Thylakoid; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..376
FT /note="Light-dependent chlorophyll f synthase"
FT /id="PRO_0000437940"
FT TRANSMEM 51..68
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P51765"
FT TRANSMEM 140..155
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P51765"
FT TRANSMEM 164..178
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P51765"
FT TRANSMEM 219..240
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P51765"
FT TRANSMEM 298..312
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P51765"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140
FT /ligand="a chlorophyll"
FT /ligand_id="ChEBI:CHEBI:139291"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P51765"
FT BINDING 220
FT /ligand="a chlorophyll"
FT /ligand_id="ChEBI:CHEBI:139291"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P51765"
FT SITE 183
FT /note="Tyrosine radical intermediate"
FT /evidence="ECO:0000250|UniProtKB:P51765"
FT SITE 212
FT /note="Stabilizes free radical intermediate"
FT /evidence="ECO:0000250|UniProtKB:P51765"
SQ SEQUENCE 376 AA; 41660 MW; F0C4A4FB4E1ECC4D CRC64;
MKLESDHVIA TSDSSDYTSE PTANKLSKRR KKVNYWEKFC SWVTSTENRL YVGWFGVLMI
PCVLTAATVF IIAIIAAPPV DMDGIGVPIS GSILSGNNII TAAVVPTSAA IGLHFYPIWE
AASIDEWLYN GGPYQLIVLH FLIGIIAYQD REWELSYRLG MRPWISLAFT APVAASVSVL
LIYPVGQGSL SAGMPLGISG TFHFMLQFQA DHNILMSPLH QLGVIGVLGG AFAAAMHGSL
VTSTLIRSHN HSESESINKG YKLGQQHPTY NFRSAQVYLW HLIWQRVSFP NSRKLHFFLA
ALPVAGIWSA ALGVDIAAFD FDYLQFHQPE LKSQGQIIHT WADTIDWASL GIKVLDERHI
YDFPENLTAG EVVPWK
