ID A0A2S6CPX1_9CYAN Unreviewed; 751 AA. AC A0A2S6CPX1; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 07-NOV-2018, entry version 4. 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:PPJ61788.1}; GN ORFNames=CUN59_19010 {ECO:0000313|EMBL:PPJ61788.1}; OS Cuspidothrix issatschenkoi CHARLIE-1. OC Bacteria; Cyanobacteria; Nostocales; Aphanizomenonaceae; Cuspidothrix. OX NCBI_TaxID=2052836 {ECO:0000313|EMBL:PPJ61788.1, ECO:0000313|Proteomes:UP000239589}; RN [1] {ECO:0000313|EMBL:PPJ61788.1, ECO:0000313|Proteomes:UP000239589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CHARLIE-1 {ECO:0000313|EMBL:PPJ61788.1, RC ECO:0000313|Proteomes:UP000239589}; RA Kust A., Mares J., Jokela J., Urajova P., Hajek J., Saurav K., RA Voracova K., Fewer D.P., Haapaniemi E., Permi P., Rehakova K., RA Sivonen K., Hrouzek P.; RT "Discovery of a pederin family compound in a non-symbiotic bloom- RT forming cyanobacterium."; RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases. 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 CC FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, CC converting photonic excitation into a charge separation, which CC transfers an electron from the donor P700 chlorophyll pair to the CC spectroscopically characterized acceptors A0, A1, FX, FA and FB in CC turn. Oxidized P700 is reduced on the lumenal side of the CC thylakoid membrane by plastocyanin or cytochrome c6. CC {ECO:0000256|HAMAP-Rule:MF_00458}. 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 CC FX. {ECO:0000256|RuleBase:RU003775}. CC -!- CATALYTIC ACTIVITY: Reduced plastocyanin + oxidized ferredoxin + CC light = oxidized plastocyanin + reduced ferredoxin. CC {ECO:0000256|HAMAP-Rule:MF_00458}. CC -!- COFACTOR: CC Note=PSI electron transfer chain: 5 chlorophyll a, 1 chlorophyll CC a', 2 phylloquinones and 3 4Fe-4S clusters. PSI core antenna: 90 CC chlorophyll a, 22 carotenoids, 3 phospholipids and 1 galactolipid. CC 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 CC 4Fe-4S iron-sulfur center. {ECO:0000256|HAMAP-Rule:MF_00458}; CC -!- SUBUNIT: The PsaA/B heterodimer binds the P700 chlorophyll special CC pair and subsequent electron acceptors. PSI consists of a core CC antenna complex that captures photons, and an electron transfer CC chain that converts photonic excitation into a charge separation. CC The cyanobacterial PSI reaction center is composed of one copy CC each of PsaA,B,C,D,E,F,I,J,K,L,M and X, and forms trimeric CC complexes. {ECO:0000256|HAMAP-Rule:MF_00458}. CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane CC {ECO:0000256|HAMAP-Rule:MF_00458, ECO:0000256|RuleBase:RU003775}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00458, CC ECO:0000256|RuleBase:RU003775}. CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000256|HAMAP- CC Rule:MF_00458, ECO:0000256|RuleBase:RU003775}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:PPJ61788.1}. 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; PGEM01000171; PPJ61788.1; -; Genomic_DNA. DR Proteomes; UP000239589; Unassembled WGS sequence. 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: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 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_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 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 ECO:0000256|RuleBase:RU003775}; KW Chlorophyll {ECO:0000256|HAMAP-Rule:MF_00458, KW ECO:0000256|RuleBase:RU003775}; KW Chromophore {ECO:0000256|HAMAP-Rule:MF_00458, KW ECO:0000256|RuleBase:RU003775}; KW Complete proteome {ECO:0000313|Proteomes:UP000239589}; KW Electron transport {ECO:0000256|HAMAP-Rule:MF_00458, KW ECO:0000256|RuleBase:RU003775}; KW Iron {ECO:0000256|HAMAP-Rule:MF_00458, ECO:0000256|RuleBase:RU003775}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00458, KW ECO:0000256|RuleBase:RU003775}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00458, KW ECO:0000256|RuleBase:RU003775}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00458, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00458, KW ECO:0000256|RuleBase:RU003775}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00458}; KW Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00458, KW ECO:0000256|RuleBase:RU003775}; KW Photosystem I {ECO:0000256|HAMAP-Rule:MF_00458, KW ECO:0000256|RuleBase:RU003775}; KW Reference proteome {ECO:0000313|Proteomes:UP000239589}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_00458}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00458, KW ECO:0000256|RuleBase:RU003775, 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, KW ECO:0000256|RuleBase:RU003775}. FT TRANSMEM 73 93 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 157 181 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 294 312 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 353 373 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 393 415 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 436 457 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 538 557 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 592 612 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 665 687 Helical. {ECO:0000256|SAM:Phobius}. FT METAL 575 575 Iron-sulfur (4Fe-4S); shared with dimeric FT partner. {ECO:0000256|HAMAP-Rule: FT MF_00458}. FT METAL 584 584 Iron-sulfur (4Fe-4S); shared with dimeric FT partner. {ECO:0000256|HAMAP-Rule: FT MF_00458}. FT METAL 676 676 Magnesium (chlorophyll-a' A1 axial FT ligand; P700 special pair). FT {ECO:0000256|HAMAP-Rule:MF_00458}. FT METAL 684 684 Magnesium (chlorophyll-a A3 axial FT ligand). {ECO:0000256|HAMAP-Rule: FT MF_00458}. FT BINDING 692 692 Chlorophyll-a A3. {ECO:0000256|HAMAP- FT Rule:MF_00458}. FT BINDING 693 693 Phylloquinone A. {ECO:0000256|HAMAP-Rule: FT MF_00458}. SQ SEQUENCE 751 AA; 83008 MW; 5C704265DB9323A9 CRC64; MTISPPEREE KKARVIVDND PVPTSFEKWA KPGHFDRSLS RGPKTTTWIW NLHALAHDFD THTSDLEDIS RKIFAAHFGH LAVVAIWLSG MLFHGAKFSN YEAWLADPLG VKPSAQTVWS IVGQDILNGD MGGGFRGIQI TSGLFQVWRG WGITSSFQLY VTAIGGLVLA GLFLFAGWFH YHKRAPKLEW FQNVESMLNH HLSVLLGCGS LGWAGHLIHV SAPINKLLDA GVAAKDIPLP HELLFDTAKM AELYPGFASG LTPFFTLNWG AYADILTFKG GLNPVTGGLW MTDISHHHLA IAVLFIIAGH MYRTNWGIGH SIKDILEAHK GPFTGEGHKG LYENMTTSWH AQLATNLAFL GSLTIIIAHH MYAMPPYPYL ATDYATQLCI FTHHIWIGGF LIVGGAAHAA IFMVRDYDPV VNQNNVLDRV IRHRDAIISH LNWVCIFLGF HSFGLYIHND TMRALGRPQD MFSDAAIKLQ PVFAQWVQSL HSLAPGNTAP NALEVVSHAF GGGIVAVGGK VAMMPIALGT ADFMVHHIHA FTIHVTVLIL LKGVLYARSS RLIPDKANLG FRFPCDGPGR GGTCQVSGWD HIFLGLFWMY NSLSIVIFHF SWKMQSDVWG TIEDGTVNHI TAGNFAESAI TINGWLRDFL WAQATQVINS YGSELSAYGL MFLGAHFVWA FSLMFLFSGR GYWQELIESI VWAHNKLKVA PTIQPRALSI TQGRAVGVAH YLLGGIATTW AFFHAHILSV G //