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

 Q1PJE4_PROMR            Unreviewed;       742 AA.
Q1PJE4;
16-MAY-2006, integrated into UniProtKB/TrEMBL.
16-MAY-2006, sequence version 1.
28-MAR-2018, entry version 57.
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=PsaB {ECO:0000256|HAMAP-Rule:MF_00482};
Name=psaB {ECO:0000256|HAMAP-Rule:MF_00482,
ECO:0000313|EMBL:ABE11436.1};
ORFNames=HOT0M-5C8_0002 {ECO:0000313|EMBL:ABE11436.1};
uncultured Prochlorococcus marinus clone HOT0M-5C8.
Bacteria; Cyanobacteria; Synechococcales; Prochloraceae;
Prochlorococcus.
NCBI_TaxID=379389 {ECO:0000313|EMBL:ABE11436.1};
[1] {ECO:0000313|EMBL:ABE11436.1}
NUCLEOTIDE SEQUENCE.
PubMed=16556843; DOI=10.1126/science.1122050;
Coleman M.L., Sullivan M.B., Martiny A.C., Steglich C., Barry K.,
Delong E.F., Chisholm S.W.;
"Genomic islands and the ecology and evolution of Prochlorococcus.";
Science 311:1768-1770(2006).
[2] {ECO:0000313|EMBL:ABE11436.1}
NUCLEOTIDE SEQUENCE.
US DOE Joint Genome Institute (JGI);
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
Hammon N., Israni S., Richardson P.;
"Sequencing of the draft fosmids and assembly of Prochlorococcus
marinus environmental genome fragment.";
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
-!- 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/cytochrome c6-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 or cytochrome c6.
{ECO:0000256|HAMAP-Rule:MF_00482}.
-!- FUNCTION: PsaA and psaB bind P700, the primary electron donor of
photosystem I (PSI), as well as the electron acceptors A0, A1 and
FX. {ECO:0000256|RuleBase:RU003775}.
-!- CATALYTIC ACTIVITY: Reduced plastocyanin + oxidized ferredoxin +
light = oxidized plastocyanin + reduced ferredoxin.
{ECO:0000256|HAMAP-Rule:MF_00482}.
-!- COFACTOR:
Note=PSI electron transfer chain: 5 divinyl chlorophyll a, 1
divinyl chlorophyll a', 2 phylloquinones and 3 4Fe-4S clusters.
PSI core antenna: 90 divinyl chlorophyll a, 22 carotenoids, 3
phospholipids and 1 galactolipid. P700 is a divinyl chlorophyll
a/divinyl chlorophyll a' dimer, A0 is one or more divinyl
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 divinyl 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 cyanobacterial PSI reaction center is composed of
one copy each of PsaA,B,C,D,E,F,I,J,K,L,M and X, and forms
trimeric complexes. {ECO:0000256|HAMAP-Rule:MF_00482}.
-!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
{ECO:0000256|HAMAP-Rule:MF_00482, ECO:0000256|RuleBase:RU003775};
Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00482,
ECO:0000256|RuleBase:RU003775}.
-!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000256|HAMAP-
Rule:MF_00482, ECO:0000256|RuleBase:RU003775}.
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EMBL; DQ366737; ABE11436.1; -; Genomic_DNA.
ProteinModelPortal; Q1PJE4; -.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell.
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 transfer activity; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
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,
ECO:0000256|RuleBase:RU003775};
Chlorophyll {ECO:0000256|HAMAP-Rule:MF_00482,
ECO:0000256|RuleBase:RU003775};
Chromophore {ECO:0000256|HAMAP-Rule:MF_00482,
ECO:0000256|RuleBase:RU003775};
Electron transport {ECO:0000256|HAMAP-Rule:MF_00482,
ECO:0000256|RuleBase:RU003775};
Iron {ECO:0000256|HAMAP-Rule:MF_00482, ECO:0000256|RuleBase:RU003775};
Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00482,
ECO:0000256|RuleBase:RU003775};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00482,
ECO:0000256|RuleBase:RU003775};
Membrane {ECO:0000256|HAMAP-Rule:MF_00482, ECO:0000256|SAM:Phobius};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00482,
ECO:0000256|RuleBase:RU003775};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00482};
Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00482,
ECO:0000256|RuleBase:RU003775};
Photosystem I {ECO:0000256|HAMAP-Rule:MF_00482,
ECO:0000256|RuleBase:RU003775};
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,
ECO:0000256|RuleBase:RU003775}.
TRANSMEM 51 70 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 135 157 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 178 199 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 383 402 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 423 444 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 525 543 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 583 604 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 654 673 Helical. {ECO:0000256|SAM:Phobius}.
METAL 567 567 Iron-sulfur (4Fe-4S); shared with dimeric
partner. {ECO:0000256|HAMAP-
Rule:MF_00482}.
METAL 576 576 Iron-sulfur (4Fe-4S); shared with dimeric
partner. {ECO:0000256|HAMAP-
Rule:MF_00482}.
METAL 662 662 Magnesium (divinyl chlorophyll-a B1 axial
ligand; P700 special pair).
{ECO:0000256|HAMAP-Rule:MF_00482}.
METAL 670 670 Magnesium (divinyl chlorophyll-a B3 axial
ligand). {ECO:0000256|HAMAP-
Rule:MF_00482}.
BINDING 678 678 Divinyl chlorophyll-a B3.
{ECO:0000256|HAMAP-Rule:MF_00482}.
BINDING 679 679 Phylloquinone B. {ECO:0000256|HAMAP-
Rule:MF_00482}.
SEQUENCE 742 AA; 82702 MW; 84A69A78A55996C6 CRC64;
MATKFPSFNQ GLAQDPTTRR IWYGIATAHD FESHDGMTEE KLYQKLFSTH FGHLAIIALW
VAGNLFHIAW QGNFEQFVID PTHVRPIAHA IWDPHFGSGI TEAMTQAGAS GPVNIAYSGL
YHWWYTIGMR TNEQLFQASI FMSILACWTL FAGWLHLQPK FRPSLAWFKN AEARLNHHLA
VLFGFSSIAW TGHLVHVAIP ESRGQHVGWD NWLTVLPHPA GLAPFFTLNW GAYAQNPDSL
DQVFGTAEGA GTAIFTFLGG LHPQSEALWL TDIAHHHIAI GTVFVIAGHM YRNTFGIGHS
LKEITEAHNT RHPNDPHKGS FGINHDGIYE TVNNSLHFQL GLALASLGVA TSLVAQHMGA
LPSYAFIARD YTTQSALYTH HQYIAMFLMV GAFAHGAIFF VRDYDPELNK DNVLARVLGT
KEALISHLSW VTMLLGFHTL GIYVHNDVVV AFGNPEKQIL IEPVFAQFVQ AAQGKMMYGF
DALLSDPTSS ASIAANSLPG NHYWMDLINR QDALSSFLPI GPADFLVHHA IALGLHTTAL
ILIKGALDAR GTKLIPDKKD LGYAFPCDGP GRGGTCDSSS WDAMYLAMFW ALNLIAWVTF
YWHWKHLAIW QGNVAQFNES GTYLMGWFRD YLWLNSSQLI NGYNPFGVNS LSPWAWMFLF
GHLVWATGFM FLISWRGYWQ ELIETLVWAH QRTPIANLVG WRDKPVALSI VQARLVGLAH
FTIGNILTFG AFVIASTSGK FG


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