ID   PSAB_PEA                Reviewed;         734 AA.
AC   P05311;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   24-JAN-2024, entry version 131.
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}; Synonyms=psaA2;
OS   Pisum sativum (Garden pea) (Lathyrus oleraceus).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   AGRICOLA=IND87003969; DOI=10.1007/BF00020126;
RA   Lehmbeck J., Rasmussen O.F., Bookjans G.B., Jepsen B.R., Stummann B.M.,
RA   Henningsen K.W.;
RT   "Sequence of two genes in pea chloroplast DNA coding for 84 and 82 kD
RT   polypeptides of the photosystem I complex.";
RL   Plant Mol. Biol. 7:3-10(1986).
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       {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; X05423; CAA29004.1; -; Genomic_DNA.
DR   PIR; S00704; S00704.
DR   RefSeq; YP_003587537.1; NC_014057.1.
DR   PDB; 2O01; X-ray; 3.40 A; B=2-733.
DR   PDB; 2WSC; X-ray; 3.30 A; B=1-734.
DR   PDB; 2WSE; X-ray; 3.49 A; B=1-734.
DR   PDB; 2WSF; X-ray; 3.48 A; B=1-734.
DR   PDB; 3LW5; X-ray; 3.30 A; B=2-734.
DR   PDB; 4RKU; X-ray; 3.00 A; B=3-733.
DR   PDB; 4XK8; X-ray; 2.80 A; B/b=2-734.
DR   PDB; 4Y28; X-ray; 2.80 A; B=1-733.
DR   PDBsum; 2O01; -.
DR   PDBsum; 2WSC; -.
DR   PDBsum; 2WSE; -.
DR   PDBsum; 2WSF; -.
DR   PDBsum; 3LW5; -.
DR   PDBsum; 4RKU; -.
DR   PDBsum; 4XK8; -.
DR   PDBsum; 4Y28; -.
DR   AlphaFoldDB; P05311; -.
DR   SMR; P05311; -.
DR   DIP; DIP-60282N; -.
DR   IntAct; P05311; 2.
DR   GeneID; 9073070; -.
DR   EvolutionaryTrace; P05311; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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; Photosystem I PsaA/PsaB; 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   NCBIfam; TIGR01336; psaB; 1.
DR   PANTHER; PTHR30128; OUTER MEMBRANE PROTEIN, OMPA-RELATED; 1.
DR   PANTHER; PTHR30128:SF75; PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A2; 1.
DR   Pfam; PF00223; PsaA_PsaB; 1.
DR   PIRSF; PIRSF002905; PSI_A; 1.
DR   PRINTS; PR00257; PHOTSYSPSAAB.
DR   SUPFAM; SSF81558; Photosystem I subunits PsaA/PsaB; 1.
DR   PROSITE; PS00419; PHOTOSYSTEM_I_PSAAB; 1.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Chlorophyll; Chloroplast; Chromophore;
KW   Electron transport; Iron; Iron-sulfur; Magnesium; Membrane; Metal-binding;
KW   Oxidoreductase; Photosynthesis; Photosystem I; Plastid; Thylakoid;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..734
FT                   /note="Photosystem I P700 chlorophyll a apoprotein A2"
FT                   /id="PRO_0000088630"
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"
FT   STRAND          4..6
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           10..13
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           19..26
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   TURN            27..29
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           31..33
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   STRAND          34..36
FT                   /evidence="ECO:0007829|PDB:2O01"
FT   HELIX           39..71
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           74..79
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   STRAND          81..84
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           98..103
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   STRAND          109..111
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   STRAND          113..115
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           120..127
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           132..157
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   TURN            159..161
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           165..168
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           171..180
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   TURN            181..183
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           184..196
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           198..202
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   TURN            209..214
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   TURN            219..222
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           223..227
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           230..234
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   STRAND          244..249
FT                   /evidence="ECO:0007829|PDB:2O01"
FT   STRAND          260..262
FT                   /evidence="ECO:0007829|PDB:4Y28"
FT   TURN            263..266
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           270..287
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   STRAND          288..291
FT                   /evidence="ECO:0007829|PDB:3LW5"
FT   STRAND          294..296
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           301..307
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   TURN            314..321
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           322..327
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           330..354
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   STRAND          358..360
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   STRAND          362..364
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   HELIX           365..396
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           401..403
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           407..413
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           415..445
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           449..451
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           458..466
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           477..479
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           484..488
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   TURN            490..493
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           494..501
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   STRAND          504..506
FT                   /evidence="ECO:0007829|PDB:4Y28"
FT   HELIX           514..539
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   TURN            540..542
FT                   /evidence="ECO:0007829|PDB:4Y28"
FT   STRAND          547..549
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   HELIX           550..552
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           563..565
FT                   /evidence="ECO:0007829|PDB:4Y28"
FT   HELIX           572..603
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           606..612
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           616..622
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   TURN            623..625
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           626..628
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           629..632
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   TURN            633..635
FT                   /evidence="ECO:0007829|PDB:2WSC"
FT   HELIX           636..638
FT                   /evidence="ECO:0007829|PDB:2O01"
FT   HELIX           644..665
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           668..683
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           688..690
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   STRAND          694..696
FT                   /evidence="ECO:0007829|PDB:4XK8"
FT   HELIX           702..730
FT                   /evidence="ECO:0007829|PDB:4XK8"
SQ   SEQUENCE   734 AA;  82412 MW;  2ACF1F77D46FA8E7 CRC64;
     MALRIPRFSQ GIAQDPTTRR IWFGIATAHD FESHDDITEG RLYQNIFASH FGQLAIIFLW
     TSGNLFHVAW QGNFEAWVQD PFHVRPIAHA IWDPHFGQPA VEAFTRGGAL GPVNNAYSGV
     YQWWYTIGLR TNEDLYTGAI FLLFLSFISL LAGWLHLQPK WKPSVSWFKN AESRLNHHLS
     GLFGVSSLAW AGHLVHVAIP GSRGEYVRWN NFLDVLPYPQ GLGPLLTGQW NLYAQNPSSS
     NHLFGTTQGA GTAILTILGG FHPQTQSLWL TDVAHHHLAI AFLFLIGGLM YRTNFGIGHS
     IKYILEAHIP PGGRLGRGHK GLYDTINNSI HFQLGLALAS LGVITSLVAQ HMYSLPAYAF
     IAQDFTTQAA LYTHHQYIAG FIMTGAFAHG PIFFIRDYNP EQNADNVLAR MLEHKEAIIS
     HLSWASLFLG FHTLGLYVHN DVMLAFGTPE KQILIEPIFA QWIQSAHGKT TYGFDIPLSS
     TNGPALNAGR NIWLPGWLNA INENSNSLFL TIGPGDFLVH HAIALGLHTT TLILVKGALD
     ARGSKLMPDK KDFGYSFPCD GPGRGGTCDI SAWDDFYLAV FWMLNTIGWV TFYWHWKHIT
     LWRGNVSQFN ESSTYLMGWL RDYLWLNSSQ LINGITPLVC NSLSVWAWMF LFGHLVWATG
     FMFLISWRGY WQELIETLAW AHERTPLANL IRWRDKPVAL SIVQARLVGL VHFSVGYIFT
     YAAFLIASTS GKFG
//