PSAA_DRIWI
ID PSAA_DRIWI Reviewed; 717 AA.
AC Q9MUJ9;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 88.
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};
DE Flags: Fragment;
GN Name=psaA {ECO:0000255|HAMAP-Rule:MF_00458};
OS Drimys winteri (Winter's bark) (Drimys chilensis).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Canellales; Winteraceae; Drimys.
OX NCBI_TaxID=3419;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10779539; DOI=10.1093/oxfordjournals.molbev.a026357;
RA Sanderson M.J., Wojciechowski M.F., Hu J.-M., Sher Khan T., Brady S.G.;
RT "Error, bias, and long-branch attraction in data for two chloroplast
RT photosystem genes in seed plants.";
RL Mol. Biol. Evol. 17:782-797(2000).
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-ferredoxin oxidoreductase, converting photonic
CC excitation into a charge separation, which transfers an electron from
CC the donor P700 chlorophyll pair to the spectroscopically characterized
CC acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on
CC the lumenal side of the thylakoid membrane by plastocyanin.
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
CC {ECO:0000255|HAMAP-Rule:MF_00458}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00458}.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000255|HAMAP-
CC Rule:MF_00458}.
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DR EMBL; AF180016; AAF29817.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9MUJ9; -.
DR SMR; Q9MUJ9; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW 4Fe-4S; Chlorophyll; Chloroplast; Chromophore; Electron transport; Iron;
KW Iron-sulfur; Magnesium; Membrane; Metal-binding; Oxidoreductase;
KW Photosynthesis; Photosystem I; Plastid; Thylakoid; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN <1..>717
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000088545"
FT TRANSMEM 58..81
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 144..167
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 183..207
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 279..297
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 334..357
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 373..399
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 421..443
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 519..537
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 577..598
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 652..674
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 712..>717
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 561
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 570
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 663
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 671
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 679
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 680
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT NON_TER 1
FT NON_TER 717
SQ SEQUENCE 717 AA; 79473 MW; 83D9DBB47EBE4CD8 CRC64;
LVDRDPVKTS FEEWARPGHF SRTIAKGPET TTWIWNLHAD AHDFDSHTSD LEEISRKVFS
AHFGQLSIIF LWLSGMYFHG ARFSNYEAWL SDPTHIGPSA QVVWPIVGQE ILNGDVGGGF
RGIQITSGFF QIWRASGITS ELQLYCTAIG ALVFAGLMLF AGWFHYHKAA PKLAWFQDVE
SMLNHHLAGL LGLGSLSWAG HQVHVSLPIN QFLDAGVDPK EIPLPHEFIL NRDLLAQLYP
SFAEGATPFF TLNWSKYAEF LTFRGGLDPV TGGLWLTDIA HHHLAIAILF LIAGHMYRTN
WGIGHGLKDI LEAHKGPFTG QGHKGLYEIL TTSWHAQLSL NLAMLGSLTI VVAHHMYSMP
PYPYLAIDYG TQLSLFTHHM WIGGFLIVGA AAHAAIFMVR DYDPTTRYND LLDRVLRHRD
AIISHLNWAC IFLGFHSFGL YIHNDTMSAL GRPQDMFSDT AIQLQPIFAQ WVQNTHALAP
GATAPGATTS TSLTWGGGDL IAVGGKVALL PIPLGTADFL VHHIHAFTIH VTVLILLKGV
LFARSSRLIP DKANLGFRFP CDGPGRGGTC QVSAWDHVFL GLFWMYNAIS VVIFHFSWKM
QSDVWGSISD QGVVTHITGG NFAQSSITIN GWLRDFLWAQ ASQVIQSYGS SLSAYGLFFL
GAHFVWAFSL MFLFSGRGYW QELIESIVWA HNKLKVAPAT QPRALSIVQG RAVGVTH
