PSAA_CYAM1
ID PSAA_CYAM1 Reviewed; 748 AA.
AC Q85FY7;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A1 {ECO:0000255|HAMAP-Rule:MF_00458};
DE EC=1.97.1.12 {ECO:0000255|HAMAP-Rule:MF_00458};
DE AltName: Full=PSI-A {ECO:0000255|HAMAP-Rule:MF_00458};
DE AltName: Full=PsaA {ECO:0000255|HAMAP-Rule:MF_00458};
GN Name=psaA {ECO:0000255|HAMAP-Rule:MF_00458};
OS Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC Cyanidioschyzon.
OX NCBI_TaxID=280699;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3377 / 10D;
RX PubMed=12755171; DOI=10.1093/dnares/10.2.67;
RA Ohta N., Matsuzaki M., Misumi O., Miyagishima S.-Y., Nozaki H., Tanaka K.,
RA Shin-i T., Kohara Y., Kuroiwa T.;
RT "Complete sequence and analysis of the plastid genome of the unicellular
RT red alga Cyanidioschyzon merolae.";
RL DNA Res. 10:67-77(2003).
CC -!- FUNCTION: PsaA and PsaB bind P700, the primary electron donor of
CC photosystem I (PSI), as well as the electron acceptors A0, A1 and FX.
CC PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase,
CC converting photonic excitation into a charge separation, which
CC transfers an electron from the donor P700 chlorophyll pair to the
CC spectroscopically characterized acceptors A0, A1, FX, FA and FB in
CC turn. Oxidized P700 is reduced on the lumenal side of the thylakoid
CC membrane by plastocyanin or cytochrome c6.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced [plastocyanin]
CC = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:30407, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC Rhea:RHEA-COMP:10039, Rhea:RHEA-COMP:10040, ChEBI:CHEBI:29036,
CC ChEBI:CHEBI:30212, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:49552; EC=1.97.1.12; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00458};
CC -!- COFACTOR:
CC Note=P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more
CC chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-
CC 4S iron-sulfur center. {ECO:0000255|HAMAP-Rule:MF_00458};
CC -!- SUBUNIT: The PsaA/B heterodimer binds the P700 chlorophyll special pair
CC and subsequent electron acceptors. PSI consists of a core antenna
CC complex that captures photons, and an electron transfer chain that
CC converts photonic excitation into a charge separation. The eukaryotic
CC PSI reaction center is composed of at least 11 subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00458}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-
CC pass membrane protein.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000255|HAMAP-
CC Rule:MF_00458}.
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DR EMBL; AB002583; BAC76206.1; -; Genomic_DNA.
DR RefSeq; NP_849044.1; NC_004799.1.
DR PDB; 5ZGB; EM; 3.63 A; A=1-748.
DR PDB; 5ZGH; EM; 3.82 A; A=1-748.
DR PDB; 6FOS; X-ray; 4.00 A; A=9-748.
DR PDB; 7BLZ; EM; 3.10 A; A=6-748.
DR PDBsum; 5ZGB; -.
DR PDBsum; 5ZGH; -.
DR PDBsum; 6FOS; -.
DR PDBsum; 7BLZ; -.
DR AlphaFoldDB; Q85FY7; -.
DR SMR; Q85FY7; -.
DR STRING; 45157.CMV135CT; -.
DR EnsemblPlants; CMV135CT; CMV135CT; CMV135C.
DR GeneID; 844935; -.
DR Gramene; CMV135CT; CMV135CT; CMV135C.
DR KEGG; cme:CymeCp112; -.
DR eggNOG; ENOG502QRYE; Eukaryota.
DR HOGENOM; CLU_016126_1_0_1; -.
DR Proteomes; UP000007014; Chloroplast.
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:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.1130.10; -; 1.
DR HAMAP; MF_00458; PSI_PsaA; 1.
DR InterPro; IPR006243; PSI_PsaA.
DR InterPro; IPR001280; PSI_PsaA/B.
DR InterPro; IPR020586; PSI_PsaA/B_CS.
DR InterPro; IPR036408; PSI_PsaA/B_sf.
DR PANTHER; PTHR30128:SF61; PTHR30128:SF61; 1.
DR Pfam; PF00223; PsaA_PsaB; 1.
DR PIRSF; PIRSF002905; PSI_A; 1.
DR PRINTS; PR00257; PHOTSYSPSAAB.
DR SUPFAM; SSF81558; SSF81558; 1.
DR TIGRFAMs; TIGR01335; psaA; 1.
DR PROSITE; PS00419; PHOTOSYSTEM_I_PSAAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Chlorophyll; Chloroplast; Chromophore;
KW Electron transport; Iron; Iron-sulfur; Magnesium; Membrane; Metal-binding;
KW Oxidoreductase; Photosynthesis; Photosystem I; Plastid; Reference proteome;
KW Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..748
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000088542"
FT TRANSMEM 69..92
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 155..178
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 194..218
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 290..308
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 345..368
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 384..410
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 432..454
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 529..547
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 587..608
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 662..684
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 722..742
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 571
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 580
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 673
FT /ligand="chlorophyll a'"
FT /ligand_id="ChEBI:CHEBI:189419"
FT /ligand_label="A1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 681
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 689
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 690
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
SQ SEQUENCE 748 AA; 82678 MW; F426053E4D84F45F CRC64;
MTLTTEKQVK VVVDRDVVPT SFEKWAKPGH FSRSLAKGPK TTTWIWNLHA DAHDFDSHTS
SLEEVSRKIF SAHFGQLAII FIWLSGMYFH GARFSNYVAW LSNPTGIKPS AQVVWPIVGQ
QILNADVGGG MQGIQITSGL FQLWRASGIV NELQLYVTAL GGLGMAGLMI FAGWFHYHKA
APKLEWFQNV ESMLNHHLAG LLGLGSLSWA GHQIHVSLPI NKLLDAGVAP SSIPLPHEFI
LNRNLMAELY PSFQQGLVPF FTLNWKQYSD ILTFKGGLSP VTGGLWLTDV AHHHLAIAVL
FLVAGHMYRT NWGIGHSIKQ ILEAHKGPLT GEGHKGLYEI LTTSWHANLA INLAMLGSLS
IIVAHHMYAM PPYPYLATDY PTQLSLFTHH MWIGGFCIVG AGAHAAIYMV RDYSPTVNFN
NVLDRMIRHR DAIISHLNWV CIFLGMHSFG LYIHNDTMRA LGRAQDMFSD TAIQLQPVFA
QWIQQIHTLA PGNTAVNALA TASYAFGADT VTVGSKIAMM PIKLGTADFM VHHIHAFTIH
VTTLILLKGV LYARNSRLIP DKANLGFRFP CDGPGRGGTC QVSAWDHVFL GLFWMYNALS
IVIFHFSWKM QSDVWGTVTS NGAISHITGG NFAQSAITIN GWLRDFLWAQ ASQVIQSYGS
SLSAYGLMFL GAHFVWAFSL MFLFSGRGYW QELIESIVWA HNKLKVAPAI APRALSITQG
RAVGVAHYLL GGIATTWAFF LARIIAVG
