PSAB_PEA
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 03-AUG-2022, entry version 126.
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).
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 PRIDE; P05311; -.
DR GeneID; 9073070; -.
DR EvolutionaryTrace; P05311; -.
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 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
