ID A0A172FJ58_ZEADI Unreviewed; 750 AA. AC A0A172FJ58; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 25-OCT-2017, entry version 9. DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A1 {ECO:0000256|HAMAP-Rule:MF_00458}; DE EC=1.97.1.12 {ECO:0000256|HAMAP-Rule:MF_00458}; DE AltName: Full=PsaA {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; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; OC 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 RT rate analysis of complete chloroplast genomes."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: Reduced plastocyanin + oxidized ferredoxin + CC light = oxidized plastocyanin + reduced ferredoxin. CC {ECO:0000256|HAMAP-Rule:MF_00458}. CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane CC {ECO:0000256|HAMAP-Rule:MF_00458}; Multi-pass membrane protein CC {ECO:0000256|HAMAP-Rule:MF_00458}. CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000256|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; KR873421; ALS45712.1; -; Genomic_DNA. DR RefSeq; YP_009259179.1; NC_030377.1. DR GeneID; 27985751; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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-SubCell. 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 carrier 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 GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW. DR Gene3D; 1.20.1130.10; -; 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 PANTHER; PTHR30128:SF8; PTHR30128:SF8; 1. DR Pfam; PF00223; PsaA_PsaB; 1. DR PIRSF; PIRSF002905; PSI_A; 1. DR PRINTS; PR00257; PHOTSYSPSAAB. DR SUPFAM; SSF81558; SSF81558; 1. DR TIGRFAMs; TIGR01335; psaA; 1. DR PROSITE; PS00419; PHOTOSYSTEM_I_PSAAB; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00458}; KW Chlorophyll {ECO:0000256|HAMAP-Rule:MF_00458}; KW Chromophore {ECO:0000256|HAMAP-Rule:MF_00458}; KW Electron transport {ECO:0000256|HAMAP-Rule:MF_00458}; KW Iron {ECO:0000256|HAMAP-Rule:MF_00458}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00458}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00458}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00458, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00458}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00458}; KW Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00458}; KW Photosystem I {ECO:0000256|HAMAP-Rule:MF_00458}; KW Plastid {ECO:0000313|EMBL:ALS45712.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_00458}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00458, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00458, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00458}. FT TRANSMEM 156 178 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 291 309 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 350 370 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 390 412 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 433 454 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 531 549 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 590 610 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 664 686 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 730 748 Helical. {ECO:0000256|SAM:Phobius}. FT METAL 573 573 Iron-sulfur (4Fe-4S); shared with dimeric FT partner. {ECO:0000256|HAMAP-Rule: FT MF_00458}. FT METAL 582 582 Iron-sulfur (4Fe-4S); shared with dimeric FT partner. {ECO:0000256|HAMAP-Rule: FT MF_00458}. FT METAL 675 675 Magnesium (chlorophyll-a' A1 axial FT ligand; P700 special pair). FT {ECO:0000256|HAMAP-Rule:MF_00458}. FT METAL 683 683 Magnesium (chlorophyll-a A3 axial FT ligand). {ECO:0000256|HAMAP-Rule: FT MF_00458}. FT BINDING 691 691 Chlorophyll-a A3. {ECO:0000256|HAMAP- FT Rule:MF_00458}. FT BINDING 692 692 Phylloquinone A. {ECO:0000256|HAMAP-Rule: FT 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 //