ID A0A193D349_IMPCY Unreviewed; 734 AA. AC A0A193D349; DT 05-OCT-2016, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 1. DT 29-SEP-2021, entry version 21. 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=PSI-B {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:ANN36025.1}; GN ORFNames=IMCY_g020 {ECO:0000313|EMBL:ANN36025.1}; OS Imperata cylindrica (Cogon grass). OG Plastid; Chloroplast {ECO:0000313|EMBL:ANN36025.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Andropogoneae; Germainiinae; Imperata. OX NCBI_TaxID=80369 {ECO:0000313|EMBL:ANN36025.1}; RN [1] {ECO:0000313|EMBL:ANN36025.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=27316745; DOI=10.1186/s12870-016-0823-3; RA Burke S.V., Wysocki W.P., Zuloaga F.O., Craine J.M., Pires J.C., RA Edger P.P., Mayfield-Jones D., Clark L.G., Kelchner S.A., Duvall M.R.; RT "Evolutionary relationships in Panicoid grasses based on plastome RT phylogenomics (Panicoideae; Poaceae)."; RL BMC Plant Biol. 16:140-140(2016). 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_00482}. 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 -!- 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:0000256|HAMAP-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|HAMAP-Rule:MF_00482}. 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_00482}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00482}. 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; KU291466; ANN36025.1; -; Genomic_DNA. DR RefSeq; YP_009260068.1; NC_030487.1. DR SMR; A0A193D349; -. DR GeneID; 32983949; -. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. 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: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 GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW. DR Gene3D; 1.20.1130.10; -; 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 Pfam; PF00223; PsaA_PsaB; 1. DR PIRSF; PIRSF002905; PSI_A; 1. DR PRINTS; PR00257; PHOTSYSPSAAB. DR SUPFAM; SSF81558; SSF81558; 1. DR TIGRFAMs; TIGR01336; 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}; Chloroplast {ECO:0000313|EMBL:ANN36025.1}; 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:ANN36025.1}; 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 METAL 559 FT /note="Iron-sulfur (4Fe-4S); shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00482" FT METAL 568 FT /note="Iron-sulfur (4Fe-4S); shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00482" FT METAL 654 FT /note="Magnesium (chlorophyll-a B1 axial ligand; P700 FT special pair)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00482" FT METAL 662 FT /note="Magnesium (chlorophyll-a B3 axial ligand)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00482" FT BINDING 670 FT /note="Chlorophyll-a B3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00482" FT BINDING 671 FT /note="Phylloquinone B" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00482" SQ SEQUENCE 734 AA; 82570 MW; 1D8165BBEDBA608F CRC64; MELRFPRFSQ GLAQDPTTRR IWFGIATAHD FESHDDITEE RLYQNIFASH FGQLAIIFLW TSGNLFHVAW QGNFESWIQD PLHVRPIAHA IWDPHFGQPA VEAFTRGGAA GPVNIAYSGV YQWWYTIGLR TNEDLYTGAL FLLFLSTLSL IGGWLHLQPK WKPSLSWFKN AESRLNHHLS GLFGVSSLAW TGHLVHVAIP GSRGEYVRWN NFLDVLPYPQ GLGPLLTGQW NLYAQNPDSS NHLFGTTQGA GTAILTLLGG FHPQTQSLWL TDIAHHHLAI AFIFLIAGHM YRTNFGIGHS IKDLLEAHTP PGGRLGRGHK GLYDTINNSI HFQLGLALAS LGVITSLVAQ HMYSLPAYAF IAQDFTTQAA LYTHHQYIAG FIMTGAFAHG AIFFIRDYNP EQNEDNVLAR MLDHKEAIIS HLSWASLFLG FHTLGLYVHN DVMLAFGTPE KQILIEPIFA QWIQSAHGKT TYGFDILLSS TNGPAFNAGR NIWLPGWLNA VNENSNSLFL TIGPGDFLVH HAIALGLHTT TLILVKGALD ARGSKLMPDK KDFGYSFPCD GPGRGGTCDI SAWDAFYLAV FWMLNTIGWV TFYWHWKHIT LWQGNVSQFN ESSTYLMGWL RDYLWLNSSQ LINGYNPFGM NSLSVWAWMF LFGHLVWATG FMFLISWRGY WQELIETLAW AHERTPLANL IRWRDKPVAL SIVQARLVGL AHFSVGYIFT YAAFLIASTS GKFG //