CHLF_SYNS7
ID CHLF_SYNS7 Reviewed; 419 AA.
AC B4WP19;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Light-dependent chlorophyll f synthase {ECO:0000303|PubMed:27386923};
DE Short=Chl f synthase {ECO:0000303|PubMed:27386923};
DE AltName: Full=Super-rogue D1 {ECO:0000303|PubMed:22187288};
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=S7335_4253;
OS Synechococcus sp. (strain ATCC 29403 / PCC 7335).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=91464;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29403 / PCC 7335;
RA Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP DISCUSSION OF SEQUENCE.
RX PubMed=22187288; DOI=10.1007/s11120-011-9714-5;
RA Murray J.W.;
RT "Sequence variation at the oxygen-evolving centre of photosystem II: a new
RT class of 'rogue' cyanobacterial D1 proteins.";
RL Photosyn. Res. 110:177-184(2012).
RN [3]
RP FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 29403 / PCC 7335;
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. Chl f absorbs far red light (FRL, 707 nm in
CC 100% methanol), and is synthesized when cells are grown in FRL, where
CC it provides the advantage of extending the spectral range of harvested
CC light in terrestrial cyanobacteria (PubMed:27386923). Chl f synthesis
CC is probably light-dependent (PubMed:27386923).
CC {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 -!- DISRUPTION PHENOTYPE: No synthesis of chlorophyll f when grown in FRL
CC (705-735 nm, 26-30 umol photons/m(2)/s) (PubMed:27386923).
CC {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:22187288). {ECO:0000303|PubMed:22187288}.
CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
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DR EMBL; DS989904; EDX86548.1; -; Genomic_DNA.
DR AlphaFoldDB; B4WP19; -.
DR SMR; B4WP19; -.
DR STRING; 91464.S7335_4253; -.
DR EnsemblBacteria; EDX86548; EDX86548; S7335_4253.
DR eggNOG; ENOG502Z87P; Bacteria.
DR HOGENOM; CLU_054206_1_0_3; -.
DR OMA; DAIDWAN; -.
DR Proteomes; UP000005766; Unassembled WGS sequence.
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; IMP: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; Reference proteome;
KW Thylakoid; Transmembrane; Transmembrane helix.
FT CHAIN 1..419
FT /note="Light-dependent chlorophyll f synthase"
FT /id="PRO_0000437941"
FT TRANSMEM 73..90
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P51765"
FT TRANSMEM 162..177
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P51765"
FT TRANSMEM 186..200
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P51765"
FT TRANSMEM 241..262
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P51765"
FT TRANSMEM 323..337
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P51765"
FT BINDING 162
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 242
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 205
FT /note="Tyrosine radical intermediate"
FT /evidence="ECO:0000250|UniProtKB:P51765"
FT SITE 234
FT /note="Stabilizes free radical intermediate"
FT /evidence="ECO:0000250|UniProtKB:P51765"
SQ SEQUENCE 419 AA; 45268 MW; D6E6B398F0F42152 CRC64;
MIQTGFGRTS ALEGFEQPFD PAQAIDLESP LTSTDTSVEN TTRNAGALWP SSQPLSPWER
FCRWVTSTEN RIYIGWFGML AIPTLATAAI VFVLAIIAAP AVDMDGTGRM VSGSLLDGNN
LITAAVVPTS AAIGLHFYPI WEAASLDEWL INGGPYQLIV LHFIIGIISY QDREWELSYR
LKMRPWISLA FTAPVAASVS VLLVYPVGQG GFASGMPLGI SGTFTFMMQF QADHNILASP
LHQMGVIGVL GGALLCAVHG SLVTSTVCRA PAQTMALTTT KTGTDRQKPK KAKTYSFEHA
QAYQQTLLWR GAKFNSSRAV HFCLAALPVA GIWSAAIGVD LAAFDFDRLS FELPSHISVR
KTVVPTWSDV VNQANLGIHT VGEKTPPKFS ESGFPEFKLS EFVEPIAEDS ASTLLSPHS
