ID   PSAB_HORVU              Reviewed;         734 AA.
AC   A1E9J0;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 73.
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   Hordeum vulgare (Barley).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Morex;
RX   PubMed=17534593; DOI=10.1007/s00122-007-0567-4;
RA   Saski C., Lee S.-B., Fjellheim S., Guda C., Jansen R.K., Luo H.,
RA   Tomkins J., Rognli O.A., Daniell H., Clarke J.L.;
RT   "Complete chloroplast genome sequences of Hordeum vulgare, Sorghum bicolor
RT   and Agrostis stolonifera, and comparative analyses with other grass
RT   genomes.";
RL   Theor. Appl. Genet. 115:571-590(2007).
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; EF115541; ABK79412.1; -; Genomic_DNA.
DR   RefSeq; YP_874652.1; NC_008590.1.
DR   PDB; 7EW6; EM; 3.40 A; B=1-734.
DR   PDB; 7EWK; EM; 3.88 A; B=2-734.
DR   PDBsum; 7EW6; -.
DR   PDBsum; 7EWK; -.
DR   AlphaFoldDB; A1E9J0; -.
DR   EMDB; EMD-31348; -.
DR   EMDB; EMD-31350; -.
DR   SMR; A1E9J0; -.
DR   GeneID; 4525131; -.
DR   OMA; FGHVAII; -.
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_0000300046"
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   HELIX           10..13
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           19..26
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           39..68
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           74..79
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           98..103
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   STRAND          113..115
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           120..126
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           133..155
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           165..168
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           171..180
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           183..196
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           198..201
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   TURN            202..204
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   TURN            209..214
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           224..227
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           230..232
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   TURN            263..266
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           270..287
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   STRAND          293..296
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           301..307
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   TURN            314..321
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           322..328
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           330..352
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           365..396
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   TURN            400..403
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   STRAND          404..406
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           407..410
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   TURN            411..413
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           415..445
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           458..466
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   TURN            477..479
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   STRAND          480..482
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           484..487
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   TURN            488..493
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           494..502
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   STRAND          504..506
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           514..539
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           550..552
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           563..565
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           572..602
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           606..612
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           616..622
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           624..627
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   TURN            628..631
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           632..634
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           644..665
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           668..684
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   TURN            686..688
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   STRAND          694..696
FT                   /evidence="ECO:0007829|PDB:7EW6"
FT   HELIX           702..732
FT                   /evidence="ECO:0007829|PDB:7EW6"
SQ   SEQUENCE   734 AA;  82615 MW;  86F9406F00CC9C6F CRC64;
     MELRFPRFSQ GLAQDPTTRR IWFGIATAHD FESHDDITEE RLYQNIFASH FGQLAIIFLW
     TSGNLFHVAW QGNFESWIQD PLHVRPIAHA IWDPHFGQPA VEAFTRGGAA GPVNIAYSGV
     YQWWYTIGLR TNEDLYTGAL FLLFLSTLSL IASWLHLQPK WKPSLSWFKN AESRLNHHLS
     GLFGVSSLAW TGHLVHVAIP ASRGEYVRWN NFLDVLPYPQ GLGPLLTGQW NLYAQNPDSS
     NHLFGTAQGA GTAILTLLGG FHPQTQSLWL TDMAHHHLAI AFIFLIAGHM YRTNFGIGHS
     IKDLLEAHTP PGGRLGRGHK GLYDTINNSI HFQLGLALAS LGVITSLVAQ HMYSLPPYAF
     IAQDFTTQAA LYTHHQYIAG FIMTGAFAHG AIFFIRDYNP EQNEDNVLAR MLDHKEAIIS
     HLSWASLFLG FHTLGLYVHN DVMLAFGTPE KQILIEPIFA QWIQSAHGKT TYGFDILLSS
     TNGPAFNAGR SLWLPGWLNA VNENSNSLFL TIGPGDFLVH HAIALGLHTT TLILVKGALD
     ARGSKLMPDK KDFGYSFPCD GPGRGGTCDI SAWDAFYLAV FWMLNTIGWV TFYWHWKHIT
     LWQGNVSQFN ESSTYLMGWL RDYLWLNSSQ LINGYNPFGM NSLSVWAWMF LFGHLVWATG
     FMFLISWRGY WQELIETLAW AHERTPLANL IRWRDKPVAL SIVQARLVGL AHFSVGYIFT
     YAAFLIASTS GKFG
//