PSAA_PEA
ID PSAA_PEA Reviewed; 758 AA.
AC P05310; Q9MUB9;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 134.
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}; Synonyms=psaA1;
OS Pisum sativum (Garden pea).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX AGRICOLA=IND87003969; DOI=10.1007/BF00020126;
RA Lehmbeck J., Rasmussen O.F., Bookjans G.B., Jepsen B.R., Stummann B.M.,
RA Henningsen K.W.;
RT "Sequence of two genes in pea chloroplast DNA coding for 84 and 82 kD
RT polypeptides of the photosystem I complex.";
RL Plant Mol. Biol. 7:3-10(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-737.
RC STRAIN=cv. Wojciechowski 398;
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; X05423; CAA29003.1; -; Genomic_DNA.
DR EMBL; AF223227; AAF65219.1; -; Genomic_DNA.
DR PIR; S00703; S00703.
DR RefSeq; YP_003587538.1; NC_014057.1.
DR PDB; 2O01; X-ray; 3.40 A; A=5-758.
DR PDB; 2WSC; X-ray; 3.30 A; A=1-758.
DR PDB; 2WSE; X-ray; 3.49 A; A=1-758.
DR PDB; 2WSF; X-ray; 3.48 A; A=1-758.
DR PDB; 3LW5; X-ray; 3.30 A; A=21-758.
DR PDB; 4RKU; X-ray; 3.00 A; A=38-758.
DR PDB; 4XK8; X-ray; 2.80 A; A/a=17-758.
DR PDB; 4Y28; X-ray; 2.80 A; A=1-758.
DR PDB; 5L8R; X-ray; 2.60 A; A=1-758.
DR PDB; 7DKZ; X-ray; 2.39 A; A=1-758.
DR PDBsum; 2O01; -.
DR PDBsum; 2WSC; -.
DR PDBsum; 2WSE; -.
DR PDBsum; 2WSF; -.
DR PDBsum; 3LW5; -.
DR PDBsum; 4RKU; -.
DR PDBsum; 4XK8; -.
DR PDBsum; 4Y28; -.
DR PDBsum; 5L8R; -.
DR PDBsum; 7DKZ; -.
DR AlphaFoldDB; P05310; -.
DR SMR; P05310; -.
DR DIP; DIP-60281N; -.
DR IntAct; P05310; 3.
DR GeneID; 9073071; -.
DR EvolutionaryTrace; P05310; -.
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:SF60; PTHR30128:SF60; 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; Thylakoid;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..758
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000088568"
FT TRANSMEM 78..101
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 164..187
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 203..227
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 299..317
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 354..377
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 393..419
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 441..463
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 539..557
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 597..618
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 672..694
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 732..753
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 581
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 590
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 683
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 691
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 699
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 700
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT CONFLICT 117
FT /note="G -> R (in Ref. 1; CAA29003)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="G -> A (in Ref. 1; CAA29003)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="A -> V (in Ref. 1; CAA29003)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="R -> G (in Ref. 1; CAA29003)"
FT /evidence="ECO:0000305"
FT CONFLICT 239..253
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="G -> GPFTGQGHKGPFTGQGHKG (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 371..378
FT /note="VVAQHMYS -> IAAHHMIA (in Ref. 1; CAA29003)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="Y -> I (in Ref. 1; CAA29003)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="A -> G (in Ref. 1; CAA29003)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="A -> T (in Ref. 1; CAA29003)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="T -> I (in Ref. 1; CAA29003)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="A -> S (in Ref. 1; CAA29003)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="N -> G (in Ref. 1; CAA29003)"
FT /evidence="ECO:0000305"
FT CONFLICT 596
FT /note="D -> V (in Ref. 1; CAA29003)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="S -> A (in Ref. 1; CAA29003)"
FT /evidence="ECO:0000305"
FT CONFLICT 627
FT /note="T -> S (in Ref. 1; CAA29003)"
FT /evidence="ECO:0000305"
FT CONFLICT 639..641
FT /note="AGN -> GGR (in Ref. 1; CAA29003)"
FT /evidence="ECO:0000305"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:2WSC"
FT TURN 31..35
FT /evidence="ECO:0007829|PDB:7DKZ"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 52..59
FT /evidence="ECO:0007829|PDB:7DKZ"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 71..102
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:7DKZ"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:5L8R"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 161..187
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 199..207
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 210..224
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 252..258
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 260..264
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:7DKZ"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:7DKZ"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 296..313
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 320..325
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 327..332
FT /evidence="ECO:0007829|PDB:7DKZ"
FT TURN 337..345
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:7DKZ"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 354..378
FT /evidence="ECO:0007829|PDB:7DKZ"
FT TURN 383..387
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 389..420
FT /evidence="ECO:0007829|PDB:7DKZ"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 430..436
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 439..455
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 458..469
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:7DKZ"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:2WSC"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:3LW5"
FT HELIX 487..497
FT /evidence="ECO:0007829|PDB:7DKZ"
FT TURN 498..503
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:4RKU"
FT STRAND 508..511
FT /evidence="ECO:0007829|PDB:2O01"
FT STRAND 515..518
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 521..523
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 526..529
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 536..561
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 562..565
FT /evidence="ECO:0007829|PDB:2O01"
FT HELIX 572..575
FT /evidence="ECO:0007829|PDB:7DKZ"
FT TURN 586..588
FT /evidence="ECO:0007829|PDB:2O01"
FT HELIX 594..623
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 626..628
FT /evidence="ECO:0007829|PDB:5L8R"
FT STRAND 630..632
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 635..638
FT /evidence="ECO:0007829|PDB:7DKZ"
FT TURN 639..641
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 642..645
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 646..648
FT /evidence="ECO:0007829|PDB:4Y28"
FT HELIX 649..655
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 657..660
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 662..665
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 670..672
FT /evidence="ECO:0007829|PDB:2WSC"
FT HELIX 673..694
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 697..713
FT /evidence="ECO:0007829|PDB:7DKZ"
FT STRAND 719..721
FT /evidence="ECO:0007829|PDB:7DKZ"
FT HELIX 727..757
FT /evidence="ECO:0007829|PDB:7DKZ"
SQ SEQUENCE 758 AA; 84199 MW; 4B6CA42A585294A2 CRC64;
MIIRSPEPKV QILADPEVKI LVDRDPIKTS FEQWAKPGHF SRTIAKGPDT TTWIWNLHAD
AHDFDSHTSD LEEISRKVFS AHFGQLSIIF LWLSGMYFHG ARFSNYEAWL NDPTHIGPSA
QVVWPIVGQE ILNGDVGGGF RGIQITSGFF QIWRASGITS ELQLYCTAIG ALVFAGLMLF
AGWFHYHKAA PKLAWFQDVE SMLNHHLAGL LGLGSLSWAR HQVHVSLPIN QFLNAGVDPK
EIPLPHEFIL NRDLLAQLYP SFAEGATPFF TLNWSKYADF LTFRGGLDPL TGGLWLTDIA
HHHLAIAILF LIAGHMYRTN WGIGHGIKDI LEAHKGPFTG QGHKGLYEIL TTSWHAQLSI
NLAMLGSLTI VVAQHMYSMP PYPYLATDYA TQLSLFTHHM WIGGFLIVGA AAHAAIFMVR
DYDPTTRYND LLDRVLRHRD AIISHLNWVC IFLGFHSFGL YIHNDTMSAL GRPQDMFSDT
AIQLQPVFAQ WIQNTHALAP GTTAPGATAS TSLTWGGGDL VAVGNKVALL PIPLGTADFL
VHHIHAFTIH VTVLILLKGV LFARSSRLIP DKANLGFRFP CDGPGRGGTC QVSAWDHVFL
GLFWMYNSIS VVIFHFSWKM QSDVWGTIND QGVVTHITAG NFAQSSITIN GWLRDFLWAQ
ASQVIQSYGS SLSAYGLFFL GAHFVWAFSL MFLFSGRGYW QELIESIVWA HNKLKVAPAT
QPRALSIVQG RAVGVTHYLL GGIATTWAFF LARIIAVG
