ID A0A0K1Z9H1_9ASTE Unreviewed; 734 AA. AC A0A0K1Z9H1; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 31-JUL-2019, entry version 10. 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=PsaB {ECO:0000256|HAMAP-Rule:MF_00482}; GN Name=psaB {ECO:0000256|HAMAP-Rule:MF_00482, GN ECO:0000313|EMBL:AKZ22659.1}; OS Ellisia nyctelea. OG Plastid {ECO:0000313|EMBL:AKZ22659.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; OC Pentapetalae; asterids; lamiids; Boraginales; Hydrophyllaceae; OC Ellisia. OX NCBI_TaxID=79343 {ECO:0000313|EMBL:AKZ22659.1}; RN [1] {ECO:0000313|EMBL:AKZ22659.1} RP NUCLEOTIDE SEQUENCE. RA Aust S.K., Ahrendsen D.L., Kellar P.R.; RT "Biodiversity assessment among two Nebraska prairies: a comparison RT between traditional and phylogenetic diversity indices."; RL Biodivers Data J 3:e5403-e5403(2015). CC -!- CATALYTIC ACTIVITY: CC Reaction=hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced CC [plastocyanin] = oxidized [plastocyanin] + reduced [2Fe-2S]- CC [ferredoxin]; Xref=Rhea:RHEA:30407, Rhea:RHEA-COMP:10000, CC Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10039, Rhea:RHEA- CC COMP:10040, ChEBI:CHEBI:29036, ChEBI:CHEBI:30212, CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:49552; CC EC=1.97.1.12; Evidence={ECO:0000256|HAMAP-Rule:MF_00482}; CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane CC {ECO:0000256|HAMAP-Rule:MF_00482}; Multi-pass membrane protein CC {ECO:0000256|HAMAP-Rule:MF_00482}. CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000256|HAMAP- CC 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; KT177359; AKZ22659.1; -; Genomic_DNA. 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 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|HAMAP-Rule:MF_00482}; KW Chlorophyll {ECO:0000256|HAMAP-Rule:MF_00482}; KW Chromophore {ECO:0000256|HAMAP-Rule:MF_00482}; KW Electron transport {ECO:0000256|HAMAP-Rule:MF_00482}; KW Iron {ECO:0000256|HAMAP-Rule:MF_00482}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00482}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00482}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_00482, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00482}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00482}; KW Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00482}; KW Photosystem I {ECO:0000256|HAMAP-Rule:MF_00482}; KW Plastid {ECO:0000313|EMBL:AKZ22659.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_00482}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00482, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00482, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|HAMAP-Rule:MF_00482}. FT TRANSMEM 135 157 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 178 199 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 330 349 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 377 396 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 417 438 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 517 539 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 575 596 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 645 665 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 707 727 Helical. {ECO:0000256|SAM:Phobius}. FT METAL 559 559 Iron-sulfur (4Fe-4S); shared with dimeric FT partner. {ECO:0000256|HAMAP-Rule: FT MF_00482}. FT METAL 568 568 Iron-sulfur (4Fe-4S); shared with dimeric FT partner. {ECO:0000256|HAMAP-Rule: FT MF_00482}. FT METAL 654 654 Magnesium (chlorophyll-a B1 axial ligand; FT P700 special pair). {ECO:0000256|HAMAP- FT Rule:MF_00482}. FT METAL 662 662 Magnesium (chlorophyll-a B3 axial FT ligand). {ECO:0000256|HAMAP-Rule: FT MF_00482}. FT BINDING 670 670 Chlorophyll-a B3. {ECO:0000256|HAMAP- FT Rule:MF_00482}. FT BINDING 671 671 Phylloquinone B. {ECO:0000256|HAMAP-Rule: FT MF_00482}. SQ SEQUENCE 734 AA; 82390 MW; 0D14E9BB2CED3A5A CRC64; MALRFPRFSQ GLAQDPTTRR IWFGIATAHD FESHDDITEE RLYQNIFASH FGQLAIIFLW TSGNLFHVAW QGNFESWVQD PLHVRPIAHA IWDPHFGQPA VEAYTRGGAL GPVNIAYSGV YQWWYTIGLR TNEDLYTGAL FLLFLSALFL IAGWLHLQPK WKPSVSWFKN AESRLNHHLS GLFGVSSLAW TGHLVHVAIP GSRGESVRWN NFLDVLPHPQ GLGPLFTGQW NLYAQNPDSS SHLFGTSQGA GTAILTLLGG FHPQTQSLWL TDMAHHHLAI AILFLIAGHM YRTNFGIGHS IKDLLNAHIP PGGRLGRGHK GLYDTINNSL HFQLGLALAS LGVITSLVAQ HMYSLPAYAF IAQDFTTQAA LYTHHQYIAG FIMTGAFAHG AIFFIRDYNP EQNEDNVLAR MLEHKEAIIS HLSWASLFLG FHTLGLYVHN DVMLAFGTPE KQILIEPIFA QWIQSAHGKT SYGFDVLLSS TSGPAFNAGR SIWLPGWLNA VNENSNSLFL TIGPGDFLVH HAIALGLHTT TLILVKGALD ARGSKLMPDK KDFGYSFPCD GPGRGGTCDI SAWDAFYLAV FWMLNTIGWV TFYWHWKHIT LWQGNVSQFN ESSTYLMGWL RDYLWLNSSQ LINGYNPFGM NSLSVWAWMF LFGHLVWATG FMFLISWRGY WQELIETLAW AHERTPLANL IRWRDKPVAL SIVQARLVGL AHFSVGYIFT YAAFLIASTS GKFG //