ID E9KIP1_ORYSJ Unreviewed; 765 AA. AC E9KIP1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 02-OCT-2024, entry version 48. DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A1 {ECO:0000256|ARBA:ARBA00017774, ECO:0000256|HAMAP-Rule:MF_00458}; DE EC=1.97.1.12 {ECO:0000256|ARBA:ARBA00013197, ECO:0000256|HAMAP-Rule:MF_00458}; DE AltName: Full=PSI-A {ECO:0000256|HAMAP-Rule:MF_00458}; DE AltName: Full=PsaA {ECO:0000256|ARBA:ARBA00031004, ECO:0000256|HAMAP-Rule:MF_00458}; GN Name=psaA {ECO:0000256|HAMAP-Rule:MF_00458, GN ECO:0000313|EMBL:ADD62834.1}; OS Oryza sativa subsp. japonica (Rice). OG Plastid; Chloroplast {ECO:0000313|EMBL:ADD62834.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39947 {ECO:0000313|EMBL:ADD62834.1}; RN [1] {ECO:0000313|EMBL:ADD62834.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=317387 {ECO:0000313|EMBL:ADD62834.1}; RX PubMed=20796245; DOI=10.1111/j.1467-7652.2010.00558.x; RA Nock C.J., Waters D.L., Edwards M.A., Bowen S.G., Rice N., Cordeiro G.M., RA Henry R.J.; RT "Chloroplast genome sequences from total DNA for plant identification."; RL Plant Biotechnol. J. 9:328-333(2011). 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 {ECO:0000256|ARBA:ARBA00003162, ECO:0000256|HAMAP-Rule:MF_00458}. 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; CC Evidence={ECO:0000256|ARBA:ARBA00000994, ECO:0000256|HAMAP- CC 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:0000256|ARBA:ARBA00026002, ECO:0000256|HAMAP-Rule:MF_00458}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Plastid, CC chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_00458}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00458}. CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. CC {ECO:0000256|ARBA:ARBA00010598, ECO:0000256|HAMAP-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; GU592207; ADD62834.1; -; Genomic_DNA. DR AlphaFoldDB; E9KIP1; -. 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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. 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:SF70; 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 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00458}; KW Chlorophyll {ECO:0000256|ARBA:ARBA00022494, ECO:0000256|HAMAP- KW Rule:MF_00458}; Chloroplast {ECO:0000313|EMBL:ADD62834.1}; KW Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|HAMAP- KW Rule:MF_00458}; KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP- KW Rule:MF_00458}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00458}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP- KW Rule:MF_00458}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00458}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00458}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00458}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00458}; KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP- KW Rule:MF_00458}; KW Photosystem I {ECO:0000256|ARBA:ARBA00022836, ECO:0000256|HAMAP- KW Rule:MF_00458}; KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:ADD62834.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_00458}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_00458}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_00458}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00458}. FT TRANSMEM 169..191 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 365..385 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 405..427 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 448..469 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 546..564 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 605..625 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 679..701 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 745..763 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT BINDING 588 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00458" FT BINDING 597 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00458" FT BINDING 690 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:0000256|HAMAP-Rule:MF_00458" FT BINDING 698 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:0000256|HAMAP-Rule:MF_00458" FT BINDING 706 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="A3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00458" FT BINDING 707 FT /ligand="phylloquinone" FT /ligand_id="ChEBI:CHEBI:18067" FT /ligand_label="A" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00458" SQ SEQUENCE 765 AA; 84874 MW; E1B9AE4FF763BF61 CRC64; MAGLFVCLVR KEEDLMMIRS PEPEVKIVVD RDPVKTSFEE WARPGHFSRT IAKGPDTTTW IWNLHADAHD FDSHTGDLEE ISRKVFSAHF GQLSIIFLWL SGMYFHGARF SNYEAWLSDP THIGPSAQVV WPIVGQEILN GDVGGGFRGI QITSGFFQIW RASGITSELQ LYCTAIGALI FASLMLFAGW FHYHKAAPKL AWFQDVESML NHHLAGLLGL GSLSWAGHQI HVSLPINQFL DAGVDPKEIP LPHEFILNRD LLAQLYPSFA EGATPFFTLN WSKYAEFLSF RGGLDPITGG LWLSDIAHHH LAIAILFLIA GHMYRTNWGI GHGLKDILEA HKGPFTGQGH KGLYEILTTS WHAQLSLNLA MLGSTTIVVA HHMYSMPPYP YLATDYGTQL SLFTHHMWIG GFLIVGAAAH AAIFMVRDYD PTTRYNDLLD RVLRHRDAII SHLNWVCIFL GFHSFGLYIH NDTMSALGRP QDMFSDTAIQ LQPIFAQWVQ NLHAGAPSVT APGATTSTSL TWGGGELVAV GGKVALLPIP LGTADFLVHH IHAFTIHVTV LILLKGVLFA RSSRLIPDKA NLGFRFPCDG PGRGGTCQVS AWDHVFLGLF WMYNSISVVI FHFSWKMQSD VWGTISDQGV VTHITGGNFA QSSITINGWL RDFLWAQASQ VIQSYGSSLS AYGLFFLGAH FVWAFSLMFL FSGRGYWQEL IESIVWAHNK LKVAPATQPR ALSIIQGRAV GVTHYLLGGI ATTWAFFLAR IIAVG //