ID A0A0K1Z9H1_9ASTE Unreviewed; 734 AA. AC A0A0K1Z9H1; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 29-MAY-2024, entry version 24. DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A2 {ECO:0000256|HAMAP-Rule:MF_00482}; DE EC=1.97.1.12 {ECO:0000256|HAMAP-Rule:MF_00482}; DE AltName: Full=PsaB {ECO:0000256|HAMAP-Rule:MF_00482}; GN Name=psaB {ECO:0000256|HAMAP-Rule:MF_00482, GN ECO:0000313|EMBL:AKZ22659.1}; OS Ellisia nyctelea. OG Plastid {ECO:0000313|EMBL:AKZ22659.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Boraginales; Hydrophyllaceae; Ellisia. OX NCBI_TaxID=79343 {ECO:0000313|EMBL:AKZ22659.1}; RN [1] {ECO:0000313|EMBL:AKZ22659.1} RP NUCLEOTIDE SEQUENCE. RA Aust S.K., Ahrendsen D.L., Kellar P.R.; RT "Biodiversity assessment among two Nebraska prairies: a comparison between RT traditional and phylogenetic diversity indices."; RL Biodivers Data J 3:e5403-e5403(2015). 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}. 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_00482}; 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}. CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP- CC Rule:MF_00482}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00482}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass CC membrane protein {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. CC {ECO:0000256|ARBA:ARBA00010598, ECO:0000256|HAMAP-Rule:MF_00482}. 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; KT177359; AKZ22659.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0K1Z9H1; -. DR GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW. DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW. DR GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-UniRule. 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_00482; PSI_PsaB; 1. DR InterPro; IPR001280; PSI_PsaA/B. DR InterPro; IPR020586; PSI_PsaA/B_CS. DR InterPro; IPR036408; PSI_PsaA/B_sf. DR InterPro; IPR006244; PSI_PsaB. DR NCBIfam; TIGR01336; psaB; 1. DR PANTHER; PTHR30128; OUTER MEMBRANE PROTEIN, OMPA-RELATED; 1. DR PANTHER; PTHR30128:SF75; PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A2; 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_00482}; KW Chlorophyll {ECO:0000256|ARBA:ARBA00022494, ECO:0000256|HAMAP- KW Rule:MF_00482}; KW Chromophore {ECO:0000256|ARBA:ARBA00022991, ECO:0000256|HAMAP- KW Rule:MF_00482}; KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP- KW Rule:MF_00482}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00482}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP- KW Rule:MF_00482}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00482}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00482}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00482}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00482}; KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP- KW Rule:MF_00482}; KW Photosystem I {ECO:0000256|ARBA:ARBA00022836, ECO:0000256|HAMAP- KW Rule:MF_00482}; KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:AKZ22659.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_00482}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_00482}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_00482}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00482}. FT TRANSMEM 135..157 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 178..199 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 330..349 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 377..396 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 417..438 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 517..539 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 575..596 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 645..665 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 707..727 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT BINDING 559 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_00482" FT BINDING 568 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_00482" FT BINDING 654 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="B1" FT /ligand_part="Mg" FT /ligand_part_id="ChEBI:CHEBI:25107" FT /note="axial binding residue" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00482" FT BINDING 662 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="B3" FT /ligand_part="Mg" FT /ligand_part_id="ChEBI:CHEBI:25107" FT /note="axial binding residue" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00482" FT BINDING 670 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="B3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00482" FT BINDING 671 FT /ligand="phylloquinone" FT /ligand_id="ChEBI:CHEBI:18067" FT /ligand_label="B" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00482" SQ SEQUENCE 734 AA; 82390 MW; 0D14E9BB2CED3A5A CRC64; MALRFPRFSQ GLAQDPTTRR IWFGIATAHD FESHDDITEE RLYQNIFASH FGQLAIIFLW TSGNLFHVAW QGNFESWVQD PLHVRPIAHA IWDPHFGQPA VEAYTRGGAL GPVNIAYSGV YQWWYTIGLR TNEDLYTGAL FLLFLSALFL IAGWLHLQPK WKPSVSWFKN AESRLNHHLS GLFGVSSLAW TGHLVHVAIP GSRGESVRWN NFLDVLPHPQ GLGPLFTGQW NLYAQNPDSS SHLFGTSQGA GTAILTLLGG FHPQTQSLWL TDMAHHHLAI AILFLIAGHM YRTNFGIGHS IKDLLNAHIP PGGRLGRGHK GLYDTINNSL HFQLGLALAS LGVITSLVAQ HMYSLPAYAF IAQDFTTQAA LYTHHQYIAG FIMTGAFAHG AIFFIRDYNP EQNEDNVLAR MLEHKEAIIS HLSWASLFLG FHTLGLYVHN DVMLAFGTPE KQILIEPIFA QWIQSAHGKT SYGFDVLLSS TSGPAFNAGR SIWLPGWLNA VNENSNSLFL TIGPGDFLVH HAIALGLHTT TLILVKGALD ARGSKLMPDK KDFGYSFPCD GPGRGGTCDI SAWDAFYLAV FWMLNTIGWV TFYWHWKHIT LWQGNVSQFN ESSTYLMGWL RDYLWLNSSQ LINGYNPFGM NSLSVWAWMF LFGHLVWATG FMFLISWRGY WQELIETLAW AHERTPLANL IRWRDKPVAL SIVQARLVGL AHFSVGYIFT YAAFLIASTS GKFG //