ID PSAA_COFAR Reviewed; 750 AA. AC A0A335; DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 13-SEP-2023, entry version 62. 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}; OS Coffea arabica (Arabian coffee). OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Gentianales; Rubiaceae; Ixoroideae; Gardenieae complex; OC Bertiereae - Coffeeae clade; Coffeeae; Coffea. OX NCBI_TaxID=13443; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17309688; DOI=10.1111/j.1467-7652.2007.00245.x; RA Samson N., Bausher M.G., Lee S.-B., Jansen R.K., Daniell H.; RT "The complete nucleotide sequence of the coffee (Coffea arabica L.) RT chloroplast genome: organization and implications for biotechnology and RT phylogenetic relationships amongst angiosperms."; RL Plant Biotechnol. J. 5:339-353(2007). 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; EF044213; ABJ89679.1; -; Genomic_DNA. DR RefSeq; YP_817482.1; NC_008535.1. DR AlphaFoldDB; A0A335; -. DR SMR; A0A335; -. DR GeneID; 4421876; -. DR OrthoDB; 2at2759; -. DR Proteomes; UP000515148; Chloroplast Pltd. 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 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; Reference proteome; Thylakoid; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..750 FT /note="Photosystem I P700 chlorophyll a apoprotein A1" FT /id="PRO_0000275939" FT TRANSMEM 70..93 FT /note="Helical; Name=I" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT TRANSMEM 156..179 FT /note="Helical; Name=II" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT TRANSMEM 195..219 FT /note="Helical; Name=III" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT TRANSMEM 291..309 FT /note="Helical; Name=IV" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT TRANSMEM 346..369 FT /note="Helical; Name=V" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT TRANSMEM 385..411 FT /note="Helical; Name=VI" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT TRANSMEM 433..455 FT /note="Helical; Name=VII" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT TRANSMEM 531..549 FT /note="Helical; Name=VIII" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT TRANSMEM 589..610 FT /note="Helical; Name=IX" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT TRANSMEM 664..686 FT /note="Helical; Name=X" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT TRANSMEM 724..744 FT /note="Helical; Name=XI" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT BINDING 573 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 582 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 675 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 683 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 691 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="A3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" FT BINDING 692 FT /ligand="phylloquinone" FT /ligand_id="ChEBI:CHEBI:18067" FT /ligand_label="A" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458" SQ SEQUENCE 750 AA; 83059 MW; E185398CD391C305 CRC64; MIIRSPEPEV KILVDRDPVK TSFEEWAKPG HFSRTIAKGP DTTTWIWNLH ADAHDFDSHT SDLEEISRKV FSAHFGQLSI IFLWLSGMYF HGARFSNYEA WLSDPTHIGP SAQVVWPIVG QEILNGDVGG GFRGIQITSG FFQIWRASGI TNELQLYCTA IGALIFAALM LFAGWFHYHK AAPKLAWFQD VESMLNHHLA GLLGLGSLSW AGHQVHVSLP INQFLNAGVD PKEIPLPHEF ILNRDLLAQL YPSFAEGATP FFTLNWSKYA EFLTFRGGLD PVTGGLWLTD IAHHHLAIAI LFLIAGHMYR TNWGIGHGLK DILEAHKGPF TGQGHKGLYE ILTTSWHAQL SLNLAMLGSL TIVVAHHMYS MPPYPYLATD YGTQLSLFTH HMWIGGFLIV GAAAHAAIFM VRDYDPTTRY NDLLDRVLRH RDAIISHLNW ACIFLGFHSF GLYIHNDTMS ALGRPQDMFS DTAIQLQPVF AQWIQNTHAL APGATAPGAT ASTSLTWGGG DLVAVGGKVA LLPIPLGTAD FLVHHIHAFT IHVTVLILLK GVLFARSSRL IPDKANLGFR FPCDGPGRGG TCQVSAWDHV FLGLFWMYNA ISVVIFHFSW KMQSDVWGSI SDQGVVTHIT GGNFAQSSIT INGWLRDFLW AQASQVIQSY GSSLSAYGLF FLGAHFVWAF SLMFLFSGRG YWQELIESIV WAHNKLKVAP ATQPRALSIV QGRAVGVTHY LLGGIATTWA FFLARIIAVG //