ID A0A2S6CPX1_9CYAN Unreviewed; 751 AA. AC A0A2S6CPX1; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 17-JUN-2020, entry version 10. 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., Voracova K., RA Fewer D.P., Haapaniemi E., Permi P., Rehakova K., Sivonen K., Hrouzek P.; RT "Discovery of a pederin family compound in a non-symbiotic bloom-forming RT 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 FX. CC 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 thylakoid CC membrane by plastocyanin or cytochrome c6. {ECO:0000256|HAMAP- CC 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 FX. CC {ECO:0000256|RuleBase:RU003775}. 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:0000256|HAMAP- CC Rule:MF_00458}; CC -!- COFACTOR: CC Note=PSI electron transfer chain: 5 chlorophyll a, 1 chlorophyll a', 2 CC phylloquinones and 3 4Fe-4S clusters. PSI core antenna: 90 chlorophyll CC a, 22 carotenoids, 3 phospholipids and 1 galactolipid. P700 is a CC chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 CC is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur CC center. {ECO:0000256|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 CC cyanobacterial PSI reaction center is composed of one copy each of CC PsaA,B,C,D,E,F,I,J,K,L,M and X, and forms trimeric complexes. CC {ECO:0000256|HAMAP-Rule:MF_00458}. CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP- CC Rule:MF_00458, ECO:0000256|RuleBase:RU003775}; Multi-pass membrane CC 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 EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 PANTHER; PTHR30128:SF43; PTHR30128:SF43; 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, 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 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, 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, ECO:0000256|RuleBase:RU003775}. FT TRANSMEM 73..93 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 157..181 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 294..312 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 353..373 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 393..415 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 436..457 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 538..557 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 592..612 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 665..687 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT METAL 575 FT /note="Iron-sulfur (4Fe-4S); shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00458" FT METAL 584 FT /note="Iron-sulfur (4Fe-4S); shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00458" FT METAL 676 FT /note="Magnesium (chlorophyll-a' A1 axial ligand; P700 FT special pair)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00458" FT METAL 684 FT /note="Magnesium (chlorophyll-a A3 axial ligand)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00458" FT BINDING 692 FT /note="Chlorophyll-a A3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00458" FT BINDING 693 FT /note="Phylloquinone A" FT /evidence="ECO:0000256|HAMAP-Rule: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 //