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

 PSAB_PHAVU              Reviewed;         734 AA.
A4GG98; A8W819;
11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
17-APR-2007, sequence version 1.
25-OCT-2017, entry version 51.
RecName: Full=Photosystem I P700 chlorophyll a apoprotein A2 {ECO:0000255|HAMAP-Rule:MF_00482};
EC=1.97.1.12 {ECO:0000255|HAMAP-Rule:MF_00482};
AltName: Full=PSI-B {ECO:0000255|HAMAP-Rule:MF_00482};
AltName: Full=PsaB {ECO:0000255|HAMAP-Rule:MF_00482};
Name=psaB {ECO:0000255|HAMAP-Rule:MF_00482};
Phaseolus vulgaris (Kidney bean) (French bean).
Plastid; Chloroplast.
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Phaseoleae; Phaseolus.
NCBI_TaxID=3885;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Negro Jamapa;
PubMed=17623083; DOI=10.1186/1471-2164-8-228;
Guo X., Castillo-Ramirez S., Gonzalez V., Bustos P.,
Fernandez-Vazquez J.L., Santamaria R.I., Arellano J., Cevallos M.A.,
Davila G.;
"Rapid evolutionary change of common bean (Phaseolus vulgaris L)
plastome, and the genomic diversification of legume chloroplasts.";
BMC Genomics 8:228-228(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Moore M.J., Triplett E.W., Broughton W.J., Soltis P.S., Soltis D.E.;
"Complete nucleotide sequence of the plastid genome of the common
bean, Phaseolus vulgaris.";
Submitted (OCT-2007) 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-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:0000255|HAMAP-
Rule:MF_00482}.
-!- CATALYTIC ACTIVITY: Reduced plastocyanin + oxidized ferredoxin +
light = oxidized plastocyanin + reduced ferredoxin.
{ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00482}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
{ECO:0000255|HAMAP-Rule:MF_00482}; Multi-pass membrane protein
{ECO:0000255|HAMAP-Rule:MF_00482}.
-!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000255|HAMAP-
Rule:MF_00482}.
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EMBL; DQ886273; ABH88079.1; -; Genomic_DNA.
EMBL; EU196765; ABW22789.1; -; Genomic_DNA.
RefSeq; YP_001122799.1; NC_009259.1.
ProteinModelPortal; A4GG98; -.
SMR; A4GG98; -.
PRIDE; A4GG98; -.
GeneID; 4961769; -.
KEGG; pvu:PhvuCp15; -.
KO; K02690; -.
PhylomeDB; A4GG98; -.
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: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.
3: Inferred from homology;
4Fe-4S; Chlorophyll; Chloroplast; Chromophore; Electron transport;
Iron; Iron-sulfur; Magnesium; Membrane; Metal-binding; Oxidoreductase;
Photosynthesis; Photosystem I; Plastid; Thylakoid; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 734 Photosystem I P700 chlorophyll a
apoprotein A2.
/FTId=PRO_0000300053.
TRANSMEM 46 69 Helical; Name=I. {ECO:0000255|HAMAP-
Rule:MF_00482}.
TRANSMEM 135 158 Helical; Name=II. {ECO:0000255|HAMAP-
Rule:MF_00482}.
TRANSMEM 175 199 Helical; Name=III. {ECO:0000255|HAMAP-
Rule:MF_00482}.
TRANSMEM 273 291 Helical; Name=IV. {ECO:0000255|HAMAP-
Rule:MF_00482}.
TRANSMEM 330 353 Helical; Name=V. {ECO:0000255|HAMAP-
Rule:MF_00482}.
TRANSMEM 369 395 Helical; Name=VI. {ECO:0000255|HAMAP-
Rule:MF_00482}.
TRANSMEM 417 439 Helical; Name=VII. {ECO:0000255|HAMAP-
Rule:MF_00482}.
TRANSMEM 517 535 Helical; Name=VIII. {ECO:0000255|HAMAP-
Rule:MF_00482}.
TRANSMEM 575 596 Helical; Name=IX. {ECO:0000255|HAMAP-
Rule:MF_00482}.
TRANSMEM 643 665 Helical; Name=X. {ECO:0000255|HAMAP-
Rule:MF_00482}.
TRANSMEM 707 727 Helical; Name=XI. {ECO:0000255|HAMAP-
Rule:MF_00482}.
METAL 559 559 Iron-sulfur (4Fe-4S); shared with dimeric
partner. {ECO:0000255|HAMAP-
Rule:MF_00482}.
METAL 568 568 Iron-sulfur (4Fe-4S); shared with dimeric
partner. {ECO:0000255|HAMAP-
Rule:MF_00482}.
METAL 654 654 Magnesium (chlorophyll-a B1 axial ligand;
P700 special pair). {ECO:0000255|HAMAP-
Rule:MF_00482}.
METAL 662 662 Magnesium (chlorophyll-a B3 axial
ligand). {ECO:0000255|HAMAP-
Rule:MF_00482}.
BINDING 670 670 Chlorophyll-a B3. {ECO:0000255|HAMAP-
Rule:MF_00482}.
BINDING 671 671 Phylloquinone B. {ECO:0000255|HAMAP-
Rule:MF_00482}.
SEQUENCE 734 AA; 82383 MW; D17ABF0FCAB4EBB7 CRC64;
MALRFPSFSQ GLAQDPTTRR IWFGIATAHD FESHDDITEE RLYQNIFASH FGQLAIIFLW
TSGNLFHVAW QGNFETWVQD PLHVRPIAHA IWDPHFGQPA VEAFTRGGAL GPVNIAYSGV
YQWWYTIGLR TNGDLYTGAI FLLILSTISL IAGWLHLQPK WKPSVSWFKN AESRLNHHLS
GLFGVSSLAW TGHLVHVAIP GSRGEYVRWN NLLGILPHPE GLGPFFTGQW NLYAQNPDSN
NHIFGTPQGA GTAILTLLGG FHPQTQSLWL TDIAHHHLAI AFIFLVAGHM YRTNFGIGHS
IKDLLEVHTP PGGRLGRGHK GLYDTINNSI HFQLGLALAS LGVITSLVAQ HMYSLPAYAF
IAQDFTTQAA LYTHHQYIAG FIMTGAFAHG AIFFIRDYNP EQNKDNVLAR MLDHKEAIIS
HLSWASLFLG FHTLGLYVHN DVMLAFGTPE KQILIEPIFA QWIQSAHGKT SYGFDILLSS
TNSPAFNAGR SIWLPGWLNA VNENSNSLFL TIGPGDFLVH HAIALGLHTT TLILVKGALD
ARGSKLMPDK KDFGYSFPCD GPGRGGTCDI SAWDAFYLAV FWMLNTIGWV TFYWHWKHIT
LWQGNISQFN ESSTYLMGWL RDYLWLNSSQ LINGYNPFGM NSLSVWAWMF LFGHLVWATG
FMFLISWRGY WQELIETLAW AHERTPLANL IRWRDKPVAL SIVQARLVGL AHFSVGYIFT
YAAFLIASTS GKFG


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