ID A0A172FJ58_ZEADI Unreviewed; 750 AA. AC A0A172FJ58; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 24-JAN-2024, entry version 27. 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=PsaA {ECO:0000256|ARBA:ARBA00031004, ECO:0000256|HAMAP-Rule:MF_00458}; GN Name=psaA {ECO:0000256|HAMAP-Rule:MF_00458, GN ECO:0000313|EMBL:ALS45712.1}; GN ORFNames=ZDIP_g21 {ECO:0000313|EMBL:ALS45712.1}; OS Zea diploperennis (Diploperennial teosinte). OG Plastid {ECO:0000313|EMBL:ALS45712.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea. OX NCBI_TaxID=4576 {ECO:0000313|EMBL:ALS45712.1}; RN [1] {ECO:0000313|EMBL:ALS45712.1} RP NUCLEOTIDE SEQUENCE. RA Orton L.M., Duvall M.R.; RT "Phylogenomic study of selected species within the genus Zea: mutation rate RT analysis of complete chloroplast genomes."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:QVO55269.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=TK043 {ECO:0000313|EMBL:QVO55269.1}; RA Welker C.A.D., McKain M.R., Estep M.C., Pasquet R.S., Chipabika G., RA Pallangyo B., Kellogg E.A.; RT "Phylogenomics enables biogeographic analysis and a new subtribal RT classification of Andropogoneae (Poaceae#Panicoideae)."; RL J Syst Evol 58:1003-1030(2020). 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_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}. CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP- CC Rule:MF_00458}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_00458}. 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_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; KR873421; ALS45712.1; -; Genomic_DNA. DR EMBL; MT610091; QVO55269.1; -; Genomic_DNA. DR RefSeq; YP_009259179.1; NC_030377.1. DR AlphaFoldDB; A0A172FJ58; -. DR SMR; A0A172FJ58; -. DR GeneID; 27985751; -. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW. DR GO; GO:0009522; C:photosystem I; 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: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}; KW Chloroplast {ECO:0000256|ARBA:ARBA00022528, ECO:0000313|EMBL:QVO55269.1}; 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}; Plastid {ECO:0000313|EMBL:ALS45712.1}; KW Thylakoid {ECO:0000256|ARBA:ARBA00023078, 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 156..178 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 291..309 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 350..370 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 390..412 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 433..454 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 531..549 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 590..610 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 664..686 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 730..748 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" 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:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00458" FT BINDING 691 FT /ligand="chlorophyll a" FT /ligand_id="ChEBI:CHEBI:58416" FT /ligand_label="A3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00458" FT BINDING 692 FT /ligand="phylloquinone" FT /ligand_id="ChEBI:CHEBI:18067" FT /ligand_label="A" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00458" SQ SEQUENCE 750 AA; 83139 MW; FC597E745F3243C7 CRC64; MIIRSSEPEV KIAVDRDPIK TSFEEWARPG HFSRTIAKGP DTTTWIWNLH ADAHDFDSHT GDLEEISRKV FSAHFGQLSI IFLWLSGMYF HGARFSNYEA WLSDPTHIGP SAQVVWPIVG QEILNGDVGG GFRGIQITSG FFQIWRASGI TSELQLYCTA IGALIFASLM LFAGWFHYHK AAPKLAWFQD VESMLNHHLA GLLGLGSLSW AGHQIHVSLP INQFLDAGVD PKEIPLPHEF ILNRDLLAQL YPSFAEGATP FFTLNWSKYA EFLSFRGGLD PITGGLWLSD IAHHHLAIAI LFLIAGHMYR TNWGIGHGLK DILEAHKGPF TGQGHKGLYE ILTTSWHAQL SLNLAMLGST TIVVAHHMYS MPPYPYLATD YGTQLSLFTH HMWIGGFLIV GAAAHAAIFM VRDYDPTTRY NDLLDRVLRH RDAIISHLNW VCIFLGFHSF GLYIHNDTMS ALGRPQDMFS DTAIQLQPIF AQWIQNIHAG APGVTAPGAT TSTSLTWGGG ELVAIGGKVA LLPIPLGTAD FLVHHIHAFT IHVTVLILLK GVLFARSSRL IPDKANLGFR FPCDGPGRGG TCQVSAWDHV FLGLFWMYNS ISVVIFHFSW KMQSDVWGTI SDQGIVTHIT GGNFAQSSIT INGWLRDFLW AQASQVIQSY GSSLSAYGLF FLGAHFVWAF SLMFLFSGRG YWQELIESIV WAHNKLKVAP ATQPRALSII QGRAVGVTHY LLGGIATTWA FFLARIIAVG //