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

 PSAB_THEEB              Reviewed;         741 AA.
P0A407; P25897;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
23-MAY-2018, entry version 97.
RecName: Full=Photosystem I P700 chlorophyll a apoprotein A2;
EC=1.97.1.12 {ECO:0000269|PubMed:10066799, ECO:0000269|PubMed:10066800, ECO:0000269|PubMed:11418848, ECO:0000269|PubMed:8901876};
AltName: Full=PsaB;
Name=psaB; OrderedLocusNames=tlr0732;
Thermosynechococcus elongatus (strain BP-1).
Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
Thermosynechococcus.
NCBI_TaxID=197221;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=BP-1;
PubMed=12240834; DOI=10.1093/dnares/9.4.123;
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N.,
Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.;
"Complete genome structure of the thermophilic cyanobacterium
Thermosynechococcus elongatus BP-1.";
DNA Res. 9:123-130(2002).
[2]
PRESENCE OF CHLOROPHYLL A' IN PSI.
PubMed=12755700; DOI=10.1046/j.1432-1033.2003.03616.x;
Nakamura A., Akai M., Yoshida E., Taki T., Watanabe T.;
"Reversed-phase HPLC determination of chlorophyll a' and phylloquinone
in photosystem I of oxygenic photosynthetic organisms.";
Eur. J. Biochem. 270:2446-2458(2003).
[3]
REVIEW.
PubMed=11687205; DOI=10.1016/S0005-2728(01)00195-5;
Fromme P., Jordan P., Krauss N.;
"Structure of photosystem I.";
Biochim. Biophys. Acta 1507:5-31(2001).
[4]
X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=8901876; DOI=10.1038/nsb1196-965;
Krauss N., Schubert W.-D., Klukas O., Fromme P., Witt H.T.,
Saenger W.;
"Photosystem I at 4-A resolution represents the first structural model
of a joint photosynthetic reaction centre and core antenna system.";
Nat. Struct. Biol. 3:965-973(1996).
[5]
X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=10066799; DOI=10.1074/jbc.274.11.7351;
Klukas O., Schubert W.-D., Jordan P., Krauss N., Fromme P., Witt H.T.,
Saenger W.;
"Photosystem I, an improved model of the stromal subunits PsaC, PsaD,
and PsaE.";
J. Biol. Chem. 274:7351-7360(1999).
[6]
X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=10066800; DOI=10.1074/jbc.274.11.7361;
Klukas O., Schubert W.-D., Jordan P., Krauss N., Fromme P., Witt H.T.,
Saenger W.;
"Localization of two phylloquinones, QK and QK', in an improved
electron density map of photosystem I at 4-A resolution.";
J. Biol. Chem. 274:7361-7367(1999).
[7]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-741, FUNCTION, CATALYTIC
ACTIVITY, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=11418848; DOI=10.1038/35082000;
Jordan P., Fromme P., Witt H.T., Klukas O., Saenger W., Krauss N.;
"Three-dimensional structure of cyanobacterial photosystem I at 2.5 A
resolution.";
Nature 411:909-917(2001).
-!- 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:0000269|PubMed:10066799, ECO:0000269|PubMed:10066800,
ECO:0000269|PubMed:11418848, ECO:0000269|PubMed:8901876}.
-!- CATALYTIC ACTIVITY: Reduced plastocyanin + oxidized ferredoxin +
light = oxidized plastocyanin + reduced ferredoxin.
{ECO:0000269|PubMed:10066799, ECO:0000269|PubMed:10066800,
ECO:0000269|PubMed:11418848, ECO:0000269|PubMed:8901876}.
-!- COFACTOR:
Note=PSI electron transfer chain: 5 chlorophyll a, 1 chlorophyll
a', 2 phylloquinones and 3 4Fe-4S clusters. PSI core antenna: 90
chlorophyll a, 22 carotenoids, 3 phospholipids and 1 galactolipid.
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:0000269|PubMed:10066799,
ECO:0000269|PubMed:10066800, ECO:0000269|PubMed:11418848,
ECO:0000269|PubMed:8901876};
-!- 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 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:0000269|PubMed:10066799,
ECO:0000269|PubMed:10066800, ECO:0000269|PubMed:11418848,
ECO:0000269|PubMed:8901876}.
-!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000250};
Multi-pass membrane protein {ECO:0000269|PubMed:10066799,
ECO:0000269|PubMed:10066800, ECO:0000269|PubMed:11418848,
ECO:0000269|PubMed:8901876}.
-!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000305}.
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EMBL; BA000039; BAC08283.1; -; Genomic_DNA.
RefSeq; NP_681521.1; NC_004113.1.
RefSeq; WP_011056579.1; NC_004113.1.
PDB; 1C51; X-ray; 4.0 A; -.
PDB; 1JB0; X-ray; 2.50 A; B=2-741.
PDB; 2PPS; X-ray; 4.0 A; -.
PDB; 3PCQ; X-ray; 8.98 A; B=2-741.
PDB; 4FE1; X-ray; 4.92 A; B=2-741.
PDB; 5ZF0; X-ray; 4.20 A; B1/B2/B3/B4/B5/B6=2-741.
PDBsum; 1C51; -.
PDBsum; 1JB0; -.
PDBsum; 2PPS; -.
PDBsum; 3PCQ; -.
PDBsum; 4FE1; -.
PDBsum; 5ZF0; -.
ProteinModelPortal; P0A407; -.
SMR; P0A407; -.
STRING; 197221.tlr0732; -.
EnsemblBacteria; BAC08283; BAC08283; BAC08283.
GeneID; 1011917; -.
KEGG; tel:tlr0732; -.
PATRIC; fig|197221.4.peg.772; -.
eggNOG; ENOG4105F37; Bacteria.
eggNOG; ENOG410Y2QV; LUCA.
HOGENOM; HOG000276868; -.
KO; K02690; -.
OMA; AQFNESS; -.
OrthoDB; POG091H09L9; -.
BioCyc; TELO197221:G1G3I-748-MONOMER; -.
EvolutionaryTrace; P0A407; -.
Proteomes; UP000000440; Chromosome.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
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.
1: Evidence at protein level;
3D-structure; 4Fe-4S; Chlorophyll; Chromophore; Complete proteome;
Electron transport; Iron; Iron-sulfur; Magnesium; Membrane;
Metal-binding; Oxidoreductase; Photosynthesis; Photosystem I;
Reference proteome; Thylakoid; Transmembrane; Transmembrane helix;
Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:11418848}.
CHAIN 2 741 Photosystem I P700 chlorophyll a
apoprotein A2.
/FTId=PRO_0000088650.
TOPO_DOM 2 38 Cytoplasmic. {ECO:0000305}.
TRANSMEM 39 70 Helical; Name=I.
TOPO_DOM 71 131 Lumenal, thylakoid. {ECO:0000305}.
TRANSMEM 132 156 Helical; Name=II.
TOPO_DOM 157 172 Cytoplasmic. {ECO:0000305}.
TRANSMEM 173 195 Helical; Name=III.
TOPO_DOM 196 269 Lumenal, thylakoid. {ECO:0000305}.
TRANSMEM 270 287 Helical; Name=IV.
TOPO_DOM 288 334 Cytoplasmic. {ECO:0000305}.
TRANSMEM 335 358 Helical; Name=V.
TOPO_DOM 359 368 Lumenal, thylakoid. {ECO:0000305}.
TRANSMEM 369 400 Helical; Name=VI.
TOPO_DOM 401 419 Cytoplasmic. {ECO:0000305}.
TRANSMEM 420 449 Helical; Name=VII.
TOPO_DOM 450 520 Lumenal, thylakoid. {ECO:0000305}.
TRANSMEM 521 545 Helical; Name=VIII.
TOPO_DOM 546 578 Cytoplasmic. {ECO:0000305}.
TRANSMEM 579 610 Helical; Name=IX.
TOPO_DOM 611 650 Lumenal, thylakoid. {ECO:0000305}.
TRANSMEM 651 672 Helical; Name=X.
TOPO_DOM 673 708 Cytoplasmic. {ECO:0000305}.
TRANSMEM 709 737 Helical; Name=XI.
TOPO_DOM 738 741 Lumenal, thylakoid. {ECO:0000305}.
METAL 566 566 Iron-sulfur (4Fe-4S); shared with dimeric
partner. {ECO:0000269|PubMed:11418848}.
METAL 575 575 Iron-sulfur (4Fe-4S); shared with dimeric
partner. {ECO:0000269|PubMed:11418848}.
METAL 661 661 Magnesium (chlorophyll-a B1 axial ligand;
P700 special pair); via tele nitrogen.
{ECO:0000269|PubMed:11418848}.
METAL 669 669 Magnesium (chlorophyll-a B3 axial
ligand). {ECO:0000269|PubMed:11418848}.
BINDING 677 677 Chlorophyll-a B3.
{ECO:0000269|PubMed:10066800,
ECO:0000269|PubMed:11418848}.
BINDING 678 678 Phylloquinone B.
{ECO:0000269|PubMed:10066800,
ECO:0000269|PubMed:11418848}.
HELIX 10 13 {ECO:0000244|PDB:1JB0}.
HELIX 19 27 {ECO:0000244|PDB:1JB0}.
HELIX 31 33 {ECO:0000244|PDB:1JB0}.
HELIX 39 71 {ECO:0000244|PDB:1JB0}.
HELIX 74 79 {ECO:0000244|PDB:1JB0}.
TURN 81 83 {ECO:0000244|PDB:1JB0}.
STRAND 87 90 {ECO:0000244|PDB:1JB0}.
HELIX 98 104 {ECO:0000244|PDB:1JB0}.
STRAND 113 115 {ECO:0000244|PDB:1JB0}.
HELIX 120 126 {ECO:0000244|PDB:1JB0}.
HELIX 132 155 {ECO:0000244|PDB:1JB0}.
HELIX 159 161 {ECO:0000244|PDB:1JB0}.
HELIX 165 168 {ECO:0000244|PDB:1JB0}.
HELIX 171 180 {ECO:0000244|PDB:1JB0}.
TURN 181 183 {ECO:0000244|PDB:1JB0}.
HELIX 184 196 {ECO:0000244|PDB:1JB0}.
HELIX 198 202 {ECO:0000244|PDB:1JB0}.
TURN 209 211 {ECO:0000244|PDB:1JB0}.
HELIX 212 214 {ECO:0000244|PDB:1JB0}.
HELIX 223 226 {ECO:0000244|PDB:1JB0}.
HELIX 230 234 {ECO:0000244|PDB:1JB0}.
TURN 263 265 {ECO:0000244|PDB:1JB0}.
HELIX 270 287 {ECO:0000244|PDB:1JB0}.
HELIX 301 306 {ECO:0000244|PDB:1JB0}.
HELIX 318 320 {ECO:0000244|PDB:1JB0}.
HELIX 326 332 {ECO:0000244|PDB:1JB0}.
HELIX 334 358 {ECO:0000244|PDB:1JB0}.
HELIX 365 367 {ECO:0000244|PDB:1JB0}.
HELIX 369 400 {ECO:0000244|PDB:1JB0}.
HELIX 405 407 {ECO:0000244|PDB:1JB0}.
HELIX 411 417 {ECO:0000244|PDB:1JB0}.
HELIX 419 449 {ECO:0000244|PDB:1JB0}.
HELIX 453 455 {ECO:0000244|PDB:1JB0}.
HELIX 462 470 {ECO:0000244|PDB:1JB0}.
HELIX 474 476 {ECO:0000244|PDB:1JB0}.
HELIX 488 491 {ECO:0000244|PDB:1JB0}.
TURN 492 495 {ECO:0000244|PDB:1JB0}.
HELIX 501 509 {ECO:0000244|PDB:1JB0}.
STRAND 510 513 {ECO:0000244|PDB:1JB0}.
HELIX 521 546 {ECO:0000244|PDB:1JB0}.
HELIX 557 560 {ECO:0000244|PDB:1JB0}.
HELIX 570 572 {ECO:0000244|PDB:1JB0}.
HELIX 579 610 {ECO:0000244|PDB:1JB0}.
HELIX 614 619 {ECO:0000244|PDB:1JB0}.
HELIX 623 629 {ECO:0000244|PDB:1JB0}.
HELIX 631 634 {ECO:0000244|PDB:1JB0}.
TURN 635 637 {ECO:0000244|PDB:1JB0}.
HELIX 638 640 {ECO:0000244|PDB:1JB0}.
STRAND 641 643 {ECO:0000244|PDB:1JB0}.
HELIX 651 672 {ECO:0000244|PDB:1JB0}.
HELIX 675 690 {ECO:0000244|PDB:1JB0}.
HELIX 695 697 {ECO:0000244|PDB:1JB0}.
STRAND 701 703 {ECO:0000244|PDB:1JB0}.
HELIX 709 737 {ECO:0000244|PDB:1JB0}.
SEQUENCE 741 AA; 83044 MW; 74961EF21401FB40 CRC64;
MATKFPKFSQ DLAQDPTTRR IWYAIAMAHD FESHDGMTEE NLYQKIFASH FGHLAIIFLW
VSGSLFHVAW QGNFEQWVQD PVNTRPIAHA IWDPQFGKAA VDAFTQAGAS NPVDIAYSGV
YHWWYTIGMR TNGDLYQGAI FLLILASLAL FAGWLHLQPK FRPSLSWFKN AESRLNHHLA
GLFGVSSLAW AGHLIHVAIP ESRGQHVGWD NFLSTMPHPA GLAPFFTGNW GVYAQNPDTA
SHVFGTAQGA GTAILTFLGG FHPQTESLWL TDMAHHHLAI AVLFIVAGHM YRTQFGIGHS
IKEMMDAKDF FGTKVEGPFN MPHQGIYETY NNSLHFQLGW HLACLGVITS LVAQHMYSLP
PYAFIAQDHT TMAALYTHHQ YIAGFLMVGA FAHGAIFLVR DYDPAQNKGN VLDRVLQHKE
AIISHLSWVS LFLGFHTLGL YVHNDVVVAF GTPEKQILIE PVFAQFIQAA HGKLLYGFDT
LLSNPDSIAS TAWPNYGNVW LPGWLDAINS GTNSLFLTIG PGDFLVHHAI ALGLHTTTLI
LVKGALDARG SKLMPDKKDF GYAFPCDGPG RGGTCDISAW DAFYLAMFWM LNTIGWVTFY
WHWKHLGVWE GNVAQFNESS TYLMGWLRDY LWLNSSQLIN GYNPFGTNNL SVWAWMFLFG
HLVWATGFMF LISWRGYWQE LIETLVWAHE RTPLANLVRW KDKPVALSIV QARLVGLAHF
SVGYILTYAA FLIASTAAKF G


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