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 24-JAN-2024, entry version 138. 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) (Lathyrus oleraceus). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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: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; Photosystem I PsaA/PsaB; 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 NCBIfam; TIGR01335; psaA; 1. DR PANTHER; PTHR30128; OUTER MEMBRANE PROTEIN, OMPA-RELATED; 1. DR PANTHER; PTHR30128:SF77; PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A1; 1. DR Pfam; PF00223; PsaA_PsaB; 1. DR PIRSF; PIRSF002905; PSI_A; 1. DR PRINTS; PR00257; PHOTSYSPSAAB. DR SUPFAM; SSF81558; Photosystem I subunits PsaA/PsaB; 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 //