PSAB_SPIOL
ID PSAB_SPIOL Reviewed; 734 AA.
AC P06512;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 125.
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 Spinacia oleracea (Spinach).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver, and cv. Monatol;
RA Kirsch W., Seyer P., Herrmann R.G.;
RT "Nucleotide sequence of the clustered genes for two P700 chlorophyll a
RT apoproteins of the photosystem I reaction center and the ribosomal protein
RT S14 of the spinach plastid chromosome.";
RL Curr. Genet. 10:843-855(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX PubMed=11292076; DOI=10.1023/a:1006478403810;
RA Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA Mache R.;
RT "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT sequence and gene organization.";
RL Plant Mol. Biol. 45:307-315(2001).
RN [3]
RP 3D-STRUCTURE MODELING.
RX PubMed=9792668; DOI=10.1074/jbc.273.45.29592;
RA Kitmitto A., Mustafa A.O., Holzenburg A., Ford R.C.;
RT "Three-dimensional structure of higher plant photosystem I determined by
RT electron crystallography.";
RL J. Biol. Chem. 273:29592-29599(1998).
RN [4]
RP PRESENCE OF CHLOROPHYLL A' IN PSI.
RX PubMed=12755700; DOI=10.1046/j.1432-1033.2003.03616.x;
RA Nakamura A., Akai M., Yoshida E., Taki T., Watanabe T.;
RT "Reversed-phase HPLC determination of chlorophyll a' and phylloquinone in
RT photosystem I of oxygenic photosynthetic organisms.";
RL Eur. J. Biochem. 270:2446-2458(2003).
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:0000255|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; 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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-
CC pass membrane protein.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000255|HAMAP-
CC Rule:MF_00482}.
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DR EMBL; AJ400848; CAB88725.1; -; Genomic_DNA.
DR PIR; S00445; S00445.
DR RefSeq; NP_054932.1; NC_002202.1.
DR AlphaFoldDB; P06512; -.
DR SMR; P06512; -.
DR STRING; 3562.P06512; -.
DR GeneID; 2715603; -.
DR KEGG; soe:2715603; -.
DR OrthoDB; 209831at2759; -.
DR BRENDA; 1.97.1.12; 5812.
DR Proteomes; UP000054095; Chloroplast.
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; Reference proteome; Thylakoid;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..734
FT /note="Photosystem I P700 chlorophyll a apoprotein A2"
FT /id="PRO_0000088638"
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; 82429 MW; 9C4B83803338C12F CRC64;
MALRFPRFSQ GLAQDPTTRR IWFGIATAHD FESHDDITEE RLYQNIFASH FGQLAIIFLW
TSGNLFHVAW QGNFESWVQD PLHVRPIAHA IWDPHFGQPA VEAFTRGGAL GPVNIAYSGV
YQWWYTIGLR TNEDLYTGAL FLLFLSVISL LGGWLHLQPK WKPSVSWFKN AESRLNHHLS
GLFGVSSLAW TGHLVHVAIP GSRGEYVRWN NFLDVLPHPQ GLGPLFTGQW NLYAQNPDSS
SHLFGTSQGA GTAILTLLGG FHPQTQSLWL TDMAHHHLAI AFVFLVAGHM YRTNFGIGHS
MKDLLEAHIP PGGRLGRGHK GLYDTINNSL HFQLGLALAS LGVITSLVAQ HMYSLPAYAF
IAQDFTTQAA LYTHHQYIAG FIMTGAFAHG AIFFIRDYNP EQNEDNVLAR MLDHKEAIIS
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
