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Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)

 M4M5T4_9ERIC            Unreviewed;       734 AA.
M4M5T4;
29-MAY-2013, integrated into UniProtKB/TrEMBL.
29-MAY-2013, sequence version 1.
25-OCT-2017, entry version 15.
RecName: Full=Photosystem I P700 chlorophyll a apoprotein A2 {ECO:0000256|HAMAP-Rule:MF_00482};
EC=1.97.1.12 {ECO:0000256|HAMAP-Rule:MF_00482};
AltName: Full=PSI-B {ECO:0000256|HAMAP-Rule:MF_00482};
AltName: Full=PsaB {ECO:0000256|HAMAP-Rule:MF_00482};
Name=psaB {ECO:0000256|HAMAP-Rule:MF_00482,
ECO:0000313|EMBL:AGG36883.1};
ORFNames=ApCp020 {ECO:0000313|EMBL:AGG36883.1};
Ardisia polysticta.
Plastid; Chloroplast {ECO:0000313|EMBL:AGG36883.1}.
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; asterids; Ericales; Primulaceae; Ardisia.
NCBI_TaxID=1265925 {ECO:0000313|EMBL:AGG36883.1};
[1] {ECO:0000313|EMBL:AGG36883.1}
NUCLEOTIDE SEQUENCE.
PubMed=23638113;
Ku C., Hu J.M., Kuo C.H.;
"Complete Plastid Genome Sequence of the Basal Asterid Ardisia
polysticta Miq. and Comparative Analyses of Asterid Plastid Genomes.";
PLoS ONE 8:E62548-E62548(2013).
-!- FUNCTION: PsaA and PsaB bind P700, the primary electron donor of
photosystem I (PSI), as well as the electron acceptors A0, A1 and
FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting
photonic excitation into a charge separation, which transfers an
electron from the donor P700 chlorophyll pair to the
spectroscopically characterized acceptors A0, A1, FX, FA and FB in
turn. Oxidized P700 is reduced on the lumenal side of the
thylakoid membrane by plastocyanin. {ECO:0000256|HAMAP-
Rule:MF_00482}.
-!- CATALYTIC ACTIVITY: Reduced plastocyanin + oxidized ferredoxin +
light = oxidized plastocyanin + reduced ferredoxin.
{ECO:0000256|HAMAP-Rule:MF_00482}.
-!- COFACTOR:
Note=P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or
more chlorophyll a, A1 is one or both phylloquinones and FX is a
shared 4Fe-4S iron-sulfur center. {ECO:0000256|HAMAP-
Rule:MF_00482};
-!- SUBUNIT: The PsaA/B heterodimer binds the P700 chlorophyll special
pair and subsequent electron acceptors. PSI consists of a core
antenna complex that captures photons, and an electron transfer
chain that converts photonic excitation into a charge separation.
The eukaryotic PSI reaction center is composed of at least 11
subunits. {ECO:0000256|HAMAP-Rule:MF_00482}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
{ECO:0000256|HAMAP-Rule:MF_00482}; Multi-pass membrane protein
{ECO:0000256|HAMAP-Rule:MF_00482}.
-!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000256|HAMAP-
Rule:MF_00482}.
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EMBL; KC465962; AGG36883.1; -; Genomic_DNA.
RefSeq; YP_007890372.1; NC_021121.1.
GeneID; 15332661; -.
GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
GO; GO:0009055; F:electron carrier activity; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
Gene3D; 1.20.1130.10; -; 1.
HAMAP; MF_00482; PSI_PsaB; 1.
InterPro; IPR001280; PSI_PsaA/B.
InterPro; IPR020586; PSI_PsaA/B_CS.
InterPro; IPR036408; PSI_PsaA/B_sf.
InterPro; IPR006244; PSI_PsaB.
Pfam; PF00223; PsaA_PsaB; 1.
PIRSF; PIRSF002905; PSI_A; 1.
PRINTS; PR00257; PHOTSYSPSAAB.
SUPFAM; SSF81558; SSF81558; 1.
TIGRFAMs; TIGR01336; psaB; 1.
PROSITE; PS00419; PHOTOSYSTEM_I_PSAAB; 1.
3: Inferred from homology;
4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00482};
Chlorophyll {ECO:0000256|HAMAP-Rule:MF_00482};
Chloroplast {ECO:0000313|EMBL:AGG36883.1};
Chromophore {ECO:0000256|HAMAP-Rule:MF_00482};
Electron transport {ECO:0000256|HAMAP-Rule:MF_00482};
Iron {ECO:0000256|HAMAP-Rule:MF_00482};
Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00482};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00482};
Membrane {ECO:0000256|HAMAP-Rule:MF_00482, ECO:0000256|SAM:Phobius};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00482};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00482};
Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00482};
Photosystem I {ECO:0000256|HAMAP-Rule:MF_00482};
Plastid {ECO:0000313|EMBL:AGG36883.1};
Thylakoid {ECO:0000256|HAMAP-Rule:MF_00482};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_00482,
ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00482,
ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|HAMAP-Rule:MF_00482}.
TRANSMEM 135 157 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 178 199 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 330 349 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 377 396 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 417 438 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 517 539 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 575 596 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 645 665 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 707 727 Helical. {ECO:0000256|SAM:Phobius}.
METAL 559 559 Iron-sulfur (4Fe-4S); shared with dimeric
partner. {ECO:0000256|HAMAP-
Rule:MF_00482}.
METAL 568 568 Iron-sulfur (4Fe-4S); shared with dimeric
partner. {ECO:0000256|HAMAP-
Rule:MF_00482}.
METAL 654 654 Magnesium (chlorophyll-a B1 axial ligand;
P700 special pair). {ECO:0000256|HAMAP-
Rule:MF_00482}.
METAL 662 662 Magnesium (chlorophyll-a B3 axial
ligand). {ECO:0000256|HAMAP-
Rule:MF_00482}.
BINDING 670 670 Chlorophyll-a B3. {ECO:0000256|HAMAP-
Rule:MF_00482}.
BINDING 671 671 Phylloquinone B. {ECO:0000256|HAMAP-
Rule:MF_00482}.
SEQUENCE 734 AA; 82497 MW; 2D26E40A80BA8BB7 CRC64;
MELRFPRFSQ GLAQDPTTRR IWFGIATAHD FESHDDITEE RLYQNIFASH FGQLAIIFLW
TSGNLFHVAW QGNFESWVQD PLHVRPIAHA IWDPHFGQPA VEAFTRGGAL GPVNIAYSGV
YQWWYTIGLR TNEDLYTGAL FLLFLSAISL IAGWLHLQPK WKPSVSWFKN AESRLNHHLS
GLFGVSSLAW TGHLVHVAIP ASRGEYVRWN NFLNVLPHPQ GLGPLFTGQW NLYAQNPDSS
SHLFGTSQGA GTAILTLLGG FHSQTQSLWL TDIAHHHLAI AFIFLVAGHM YRTNFGIGHS
MKDLLDAHVP PGGRLGRGHK GLYDTINNSI HFQLGLALAS LGVITSLVAQ HMYSLPAYAF
IAQDFTTQAA LYTHHQYIAG FIMTGAFAHG AIFFIRDYNP EQNEDNVLAR MLDHKEAIIS
HLSWASLFLG FHTLGLYVHN DVMLAFGTPE KQILIEPIFA QWIQSAHGKT SYGFDVLLSS
TSGPAFNAGR SIWLPGWLNA VNENNNSLFL TIGPGDFLVH HAIALGLHTT TLILVKGALD
ARGSKLMPDK KDFGYSFPCD GPGRGGTCDI SAWDAFYLAV FWMLNTIGWV TFYWHWKHIT
LWQGNVSQFN ESSTYLMGWL RDYLWLNSSQ LINGYNPFGM NSLSVWAWMF LFGHLIWAIG
FMFLISWRGY WQELIETLAW AHERTPLANL IRWRDKPVAL SIVQARLVGL AHFSVGYIFT
YAAFLIASTS GKFG


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