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PSAB_NEPOL
ID   PSAB_NEPOL              Reviewed;         734 AA.
AC   Q9TKW1;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Photosystem I P700 chlorophyll a apoprotein A2 {ECO:0000255|HAMAP-Rule:MF_00482};
DE            EC=1.97.1.12 {ECO:0000255|HAMAP-Rule:MF_00482};
DE   AltName: Full=PSI-B {ECO:0000255|HAMAP-Rule:MF_00482};
DE   AltName: Full=PsaB {ECO:0000255|HAMAP-Rule:MF_00482};
GN   Name=psaB {ECO:0000255|HAMAP-Rule:MF_00482};
OS   Nephroselmis olivacea (Green alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; Nephroselmidophyceae;
OC   Nephroselmidales; Nephroselmidaceae; Nephroselmis.
OX   NCBI_TaxID=31312;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-484 / S-N-5-8;
RX   PubMed=10468594; DOI=10.1073/pnas.96.18.10248;
RA   Turmel M., Otis C., Lemieux C.;
RT   "The complete chloroplast DNA sequence of the green alga Nephroselmis
RT   olivacea: insights into the architecture of ancestral chloroplast
RT   genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:10248-10253(1999).
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:0000255|HAMAP-
CC       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; Evidence={ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00482}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_00482}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_00482}.
CC   -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00482}.
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DR   EMBL; AF137379; AAD54855.1; -; Genomic_DNA.
DR   RefSeq; NP_050884.1; NC_000927.1.
DR   AlphaFoldDB; Q9TKW1; -.
DR   SMR; Q9TKW1; -.
DR   PRIDE; Q9TKW1; -.
DR   GeneID; 802034; -.
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   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; Chlorophyll; Chloroplast; Chromophore; Electron transport; Iron;
KW   Iron-sulfur; Magnesium; Membrane; Metal-binding; Oxidoreductase;
KW   Photosynthesis; Photosystem I; Plastid; Thylakoid; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..734
FT                   /note="Photosystem I P700 chlorophyll a apoprotein A2"
FT                   /id="PRO_0000088623"
FT   TRANSMEM        46..69
FT                   /note="Helical; Name=I"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   TRANSMEM        135..158
FT                   /note="Helical; Name=II"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   TRANSMEM        175..199
FT                   /note="Helical; Name=III"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   TRANSMEM        273..291
FT                   /note="Helical; Name=IV"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   TRANSMEM        330..353
FT                   /note="Helical; Name=V"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   TRANSMEM        369..395
FT                   /note="Helical; Name=VI"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   TRANSMEM        417..439
FT                   /note="Helical; Name=VII"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   TRANSMEM        517..535
FT                   /note="Helical; Name=VIII"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   TRANSMEM        575..596
FT                   /note="Helical; Name=IX"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   TRANSMEM        643..665
FT                   /note="Helical; Name=X"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   TRANSMEM        707..727
FT                   /note="Helical; Name=XI"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   BINDING         559
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   BINDING         568
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   BINDING         654
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="B1"
FT                   /ligand_part="Mg"
FT                   /ligand_part_id="ChEBI:CHEBI:25107"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   BINDING         662
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="B3"
FT                   /ligand_part="Mg"
FT                   /ligand_part_id="ChEBI:CHEBI:25107"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   BINDING         670
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="B3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   BINDING         671
FT                   /ligand="phylloquinone"
FT                   /ligand_id="ChEBI:CHEBI:18067"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
SQ   SEQUENCE   734 AA;  81748 MW;  FB1850C1E348184D CRC64;
     MATKFPKFSQ GLAEDPTTRR IWYGIATAHD FESHDGMTEE SLYQKIFASH FGQLAIIFLW
     TSGNLFHVAW QGNFEQWGQD PLHVRPIAHA IWDPHFGQPA VEAFTRGGAA GPVNISYSGV
     YQWWYTIGMR SSNDLYTGAL FLLVGAAILL FAGWLHLQPK FQPSLSWFKN AESRLNHHLA
     GLFGVSSLAW TGHLVHVAIP ESRGQHVGWD NFLTTLPHPA GLAPFFNGNW SVYAQNPDSA
     SHLFGTSTGA GTAILTFLGG FHPQTQSLWL TDMAHHHLAI AVVFILAGHM YRTNFGIGHS
     MREILEAHRA PSGRLGLGHK GLFDTVNNSL HFQLGLALAS LGVITSLVAQ HMYSLPPYAF
     MAQDFTTMSA LYTHHQYIAG FIMTGAFAHG AIFFIRDYDP IQNEGNVLAR MLEHKEALIS
     HLSWVTLFLG FHTLGLYVHN DVMLAFGTPE KQILIEPVFA QWIQASHGKA LYGFDVLLSS
     ADSPATSASQ SIWLPGWLDA INSSSNSLFL TIGPGDFLVH HAIALGLHTT TLILVKGALD
     ARGSKLMPDK KDFGYSFPCD GPGRGGTCDI SAWDAFYLAV FWMLNTIGWT TFYWHWKHLA
     LWQGNAAQFN ESSTYLMGWL RDYLWLNSSQ LINGYNPFGM NSLSVWAWMF LFGHLVWATG
     FMFLISWRGY WQELIETLAW AHERTPLANL VRWKDKPVAL SIVQARLVGL AHFSVGYVFT
     YAAFVIASTS GKFG
 
 
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