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Photosystem I P700 chlorophyll a apoprotein A1 (EC 1.97.1.12) (PSI-A) (PsaA)

 PSAA_CHLRE              Reviewed;         751 AA.
P12154; B7U1G1; Q9GH91;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
18-OCT-2001, sequence version 3.
25-OCT-2017, entry version 130.
RecName: Full=Photosystem I P700 chlorophyll a apoprotein A1;
EC=1.97.1.12;
AltName: Full=PSI-A;
AltName: Full=PsaA;
Name=psaA; Synonyms=ps1a1;
Chlamydomonas reinhardtii (Chlamydomonas smithii).
Plastid; Chloroplast.
Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae;
Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
NCBI_TaxID=3055;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CC-406;
PubMed=16453785;
Kueck U., Choquet Y., Schneider M., Dron M., Bennoun P.;
"Structural and transcription analysis of two homologous genes for the
P700 chlorophyll a-apoproteins in Chlamydomonas reinhardtii: evidence
for in vivo trans-splicing.";
EMBO J. 6:2185-2195(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CC-503;
PubMed=19473533; DOI=10.1186/1471-2148-9-120;
Smith D.R., Lee R.W.;
"Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
addressing the mutational-hazard hypothesis.";
BMC Evol. Biol. 9:120-120(2009).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 190-686.
STRAIN=137c / CC-125;
PubMed=11083939; DOI=10.1006/mpev.2000.0831;
Nozaki H., Misawa K., Kajita T., Kato M., Nohara S., Watanabe M.M.;
"Origin and evolution of the colonial Volvocales (Chlorophyceae) as
inferred from multiple, chloroplast gene sequences.";
Mol. Phylogenet. Evol. 17:256-268(2000).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 513-517.
STRAIN=137c / CC-125;
Redding K.;
Unpublished observations (APR-2001).
[5]
IDENTIFICATION, AND COMPLETE PLASTID GENOME.
PubMed=12417694; DOI=10.1105/tpc.006155;
Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W.,
Harris E.H., Stern D.B.;
"The Chlamydomonas reinhardtii plastid chromosome: islands of genes in
a sea of repeats.";
Plant Cell 14:2659-2679(2002).
[6]
MUTAGENESIS OF CONSERVED HISTIDINES.
STRAIN=137c / CC-125;
PubMed=9427740; DOI=10.1093/emboj/17.1.50;
Redding K., MacMillan F., Leibl W., Brettel K., Hanley J.,
Rutherford A.W., Breton J., Rochaix J.-D.;
"A systematic survey of conserved histidines in the core subunits of
photosystem I by site-directed mutagenesis reveals the likely axial
ligands of P700.";
EMBO J. 17:50-60(1998).
[7]
MUTAGENESIS OF HIS-676.
STRAIN=CC-2696;
PubMed=11041867; DOI=10.1021/bi001200q;
Krabben L., Schlodder E., Jordan R., Carbonera D., Giacometti G.,
Lee H., Webber A.N., Lubitz W.;
"Influence of the axial ligands on the spectral properties of P700 of
photosystem I: a study of site-directed mutants.";
Biochemistry 39:13012-13025(2000).
[8]
MUTAGENESIS OF A1 PHYLLOQUINONE LIGANDS.
STRAIN=137c / CC-125;
PubMed=11274371; DOI=10.1073/pnas.081078898;
Guergova-Kuras M., Boudreaux B., Joliot A., Joliot P., Redding K.;
"Evidence for two active branches for electron transfer in photosystem
I.";
Proc. Natl. Acad. Sci. U.S.A. 98:4437-4442(2001).
[9]
MUTAGENESIS OF A1 PHYLLOQUINONE LIGANDS.
STRAIN=137c / CC-125;
PubMed=11489879; DOI=10.1074/jbc.M102327200;
Boudreaux B., MacMillan F., Teutloff C., Agalarov R., Gu F.,
Grimaldi S., Bittl R., Brettel K., Redding K.;
"Mutations in both sides of the photosystem I reaction center identify
the phylloquinone observed by electron paramagnetic resonance
spectroscopy.";
J. Biol. Chem. 276:37299-37306(2001).
[10]
PRESENCE OF CHLOROPHYLL A' IN PSI.
STRAIN=IAM C-9;
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).
-!- 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.
-!- FUNCTION: Both potential cofactor branches in PSI seem to be
active; however, electron transfer seems to proceed preferentially
down the path including the phylloquinone bound by PsaA.
-!- CATALYTIC ACTIVITY: Reduced plastocyanin + oxidized ferredoxin +
light = oxidized plastocyanin + reduced ferredoxin.
-!- 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:0000250};
-!- 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.
-!- INTERACTION:
Q84V18:STT7; NbExp=4; IntAct=EBI-601796, EBI-15762546;
O20031:ycf3; NbExp=3; IntAct=EBI-601796, EBI-601871;
-!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane;
Multi-pass membrane protein.
-!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000305}.
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EMBL; X05845; CAA29286.1; -; Genomic_DNA.
EMBL; X05846; CAA29286.1; JOINED; Genomic_DNA.
EMBL; X05847; CAA29286.1; JOINED; Genomic_DNA.
EMBL; FJ423446; ACJ50108.1; -; Genomic_DNA.
EMBL; AB044419; BAB18345.1; -; Genomic_DNA.
EMBL; BK000554; DAA01471.1; -; Genomic_DNA.
PIR; A28341; A28341.
RefSeq; NP_958375.1; NC_005353.1.
ProteinModelPortal; P12154; -.
SMR; P12154; -.
DIP; DIP-34985N; -.
IntAct; P12154; 15.
STRING; 3055.DAA01471; -.
PaxDb; P12154; -.
PRIDE; P12154; -.
GeneID; 2717000; -.
KEGG; cre:ChreCp019; -.
eggNOG; ENOG410IHST; Eukaryota.
eggNOG; ENOG410XT0I; LUCA.
InParanoid; P12154; -.
KO; K02689; -.
BioCyc; CHLAMY:CHRECP019-MONOMER; -.
BioCyc; MetaCyc:CHRECP019-MONOMER; -.
Proteomes; UP000006906; Chloroplast.
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_00458; PSI_PsaA; 1.
InterPro; IPR006243; PSI_PsaA.
InterPro; IPR001280; PSI_PsaA/B.
InterPro; IPR020586; PSI_PsaA/B_CS.
InterPro; IPR036408; PSI_PsaA/B_sf.
PANTHER; PTHR30128:SF8; PTHR30128:SF8; 1.
Pfam; PF00223; PsaA_PsaB; 1.
PIRSF; PIRSF002905; PSI_A; 1.
PRINTS; PR00257; PHOTSYSPSAAB.
SUPFAM; SSF81558; SSF81558; 1.
TIGRFAMs; TIGR01335; psaA; 1.
PROSITE; PS00419; PHOTOSYSTEM_I_PSAAB; 1.
1: Evidence at protein level;
4Fe-4S; Chlorophyll; Chloroplast; Chromophore; Complete proteome;
Electron transport; Iron; Iron-sulfur; Magnesium; Membrane;
Metal-binding; Oxidoreductase; Photosynthesis; Photosystem I; Plastid;
Reference proteome; Thylakoid; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 751 Photosystem I P700 chlorophyll a
apoprotein A1.
/FTId=PRO_0000088539.
TRANSMEM 73 96 Helical; Name=I. {ECO:0000255}.
TRANSMEM 159 182 Helical; Name=II. {ECO:0000255}.
TRANSMEM 198 222 Helical; Name=III. {ECO:0000255}.
TRANSMEM 294 312 Helical; Name=IV. {ECO:0000255}.
TRANSMEM 349 372 Helical; Name=V. {ECO:0000255}.
TRANSMEM 388 414 Helical; Name=VI. {ECO:0000255}.
TRANSMEM 436 458 Helical; Name=VII. {ECO:0000255}.
TRANSMEM 533 551 Helical; Name=VIII. {ECO:0000255}.
TRANSMEM 591 612 Helical; Name=IX. {ECO:0000255}.
TRANSMEM 665 687 Helical; Name=X. {ECO:0000255}.
TRANSMEM 725 745 Helical; Name=XI. {ECO:0000255}.
METAL 575 575 Iron-sulfur (4Fe-4S); shared with dimeric
partner. {ECO:0000250}.
METAL 584 584 Iron-sulfur (4Fe-4S); shared with dimeric
partner. {ECO:0000250}.
METAL 676 676 Magnesium (chlorophyll-a' A1 axial
ligand; P700 special pair).
METAL 684 684 Magnesium (chlorophyll-a A3 axial
ligand). {ECO:0000250}.
BINDING 692 692 Chlorophyll-a A3. {ECO:0000250}.
BINDING 693 693 Phylloquinone A.
MUTAGEN 676 676 H->C: No PSI detected.
{ECO:0000269|PubMed:11041867}.
MUTAGEN 676 676 H->F,L: Loss of P700 function.
{ECO:0000269|PubMed:11041867}.
MUTAGEN 676 676 H->Q: Impairment of P700 function. More
severe; when associated with Q-656 in
psaB. {ECO:0000269|PubMed:11041867}.
MUTAGEN 676 676 H->S: Accumulates approximately 50% PSI.
{ECO:0000269|PubMed:11041867}.
MUTAGEN 693 693 W->F: Unable to photoaccumulate an
electron on A1.
CONFLICT 513 513 D -> E (in Ref. 1; CAA29286).
{ECO:0000305}.
CONFLICT 515 515 V -> G (in Ref. 1; CAA29286).
{ECO:0000305}.
CONFLICT 517 517 V -> H (in Ref. 1; CAA29286).
{ECO:0000305}.
SEQUENCE 751 AA; 83154 MW; 4D8876D1094BDCD3 CRC64;
MTISTPEREA KKVKIAVDRN PVETSFEKWA KPGHFSRTLS KGPNTTTWIW NLHADAHDFD
SHTSDLEEIS RKVFSAHFGQ LGIIFIWLSG MYFHGARFSN YEAWLSDPTH IKPSAQVVWP
IVGQEILNGD VGGGFQGIQI TSGFFQLWRA SGITSELQLY TTAIGGLVMA AAMFFAGWFH
YHKAAPKLEW FQNVESMLNH HLGGLLGLGS LAWAGHQIHV SLPVNKLLDA GVDPKEIPLP
HDLLLNRAIM ADLYPSFAKG IAPFFTLNWS EYSDFLTFKG GLNPVTGGLW LSDTAHHHVA
IAVLFLVAGH MYRTNWGIGH SMKEILEAHR GPFTGEGHVG LYEILTTSWH AQLAINLALF
GSLSIIVAHH MYAMPPYPYL ATDYGTQLSL FTHHTWIGGF CIVGAGAHAA IFMVRDYDPT
NNYNNLLDRV IRHRDAIISH LNWVCIFLGF HSFGLYIHND TMSALGRPQD MFSDTAIQLQ
PVFAQWIQNT HFLAPQLTAP NALAATSLTW GGDLVAVGGK VAMMPISLGT SDFMVHHIHA
FTIHVTVLIL LKGVLFARSS RLIPDKANLG FRFPCDGPGR GGTCQVSAWD HVFLGLFWMY
NSLSIVIFHF SWKMQSDVWG TVTASGVSHI TGGNFAQSAN TINGWLRDFL WAQSSQVIQS
YGSALSAYGL IFLGAHFVWA FSLMFLFSGR GYWQELIESI VWAHNKLKVA PAIQPRALSI
TQGRAVGVAH YLLGGIATTW SFFLARIISV G


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