PSAA_CHLRE
ID PSAA_CHLRE Reviewed; 751 AA.
AC P12154; B7U1G1; Q9GH91;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A1;
DE EC=1.97.1.12;
DE AltName: Full=PSI-A;
DE AltName: Full=PsaA;
GN Name=psaA; Synonyms=ps1a1;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CC-406;
RX PubMed=16453785; DOI=10.1002/j.1460-2075.1987.tb02489.x;
RA Kueck U., Choquet Y., Schneider M., Dron M., Bennoun P.;
RT "Structural and transcription analysis of two homologous genes for the P700
RT chlorophyll a-apoproteins in Chlamydomonas reinhardtii: evidence for in
RT vivo trans-splicing.";
RL EMBO J. 6:2185-2195(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA Smith D.R., Lee R.W.;
RT "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT addressing the mutational-hazard hypothesis.";
RL BMC Evol. Biol. 9:120-120(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 190-686.
RC STRAIN=137c / CC-125;
RX PubMed=11083939; DOI=10.1006/mpev.2000.0831;
RA Nozaki H., Misawa K., Kajita T., Kato M., Nohara S., Watanabe M.M.;
RT "Origin and evolution of the colonial Volvocales (Chlorophyceae) as
RT inferred from multiple, chloroplast gene sequences.";
RL Mol. Phylogenet. Evol. 17:256-268(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 513-517.
RC STRAIN=137c / CC-125;
RA Redding K.;
RL Unpublished observations (APR-2001).
RN [5]
RP IDENTIFICATION, AND COMPLETE PLASTID GENOME.
RX PubMed=12417694; DOI=10.1105/tpc.006155;
RA Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H.,
RA Stern D.B.;
RT "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a
RT sea of repeats.";
RL Plant Cell 14:2659-2679(2002).
RN [6]
RP MUTAGENESIS OF CONSERVED HISTIDINES.
RC STRAIN=137c / CC-125;
RX PubMed=9427740; DOI=10.1093/emboj/17.1.50;
RA Redding K., MacMillan F., Leibl W., Brettel K., Hanley J., Rutherford A.W.,
RA Breton J., Rochaix J.-D.;
RT "A systematic survey of conserved histidines in the core subunits of
RT photosystem I by site-directed mutagenesis reveals the likely axial ligands
RT of P700.";
RL EMBO J. 17:50-60(1998).
RN [7]
RP MUTAGENESIS OF HIS-676.
RC STRAIN=CC-2696;
RX PubMed=11041867; DOI=10.1021/bi001200q;
RA Krabben L., Schlodder E., Jordan R., Carbonera D., Giacometti G., Lee H.,
RA Webber A.N., Lubitz W.;
RT "Influence of the axial ligands on the spectral properties of P700 of
RT photosystem I: a study of site-directed mutants.";
RL Biochemistry 39:13012-13025(2000).
RN [8]
RP MUTAGENESIS OF A1 PHYLLOQUINONE LIGANDS.
RC STRAIN=137c / CC-125;
RX PubMed=11274371; DOI=10.1073/pnas.081078898;
RA Guergova-Kuras M., Boudreaux B., Joliot A., Joliot P., Redding K.;
RT "Evidence for two active branches for electron transfer in photosystem I.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4437-4442(2001).
RN [9]
RP MUTAGENESIS OF A1 PHYLLOQUINONE LIGANDS.
RC STRAIN=137c / CC-125;
RX PubMed=11489879; DOI=10.1074/jbc.m102327200;
RA Boudreaux B., MacMillan F., Teutloff C., Agalarov R., Gu F., Grimaldi S.,
RA Bittl R., Brettel K., Redding K.;
RT "Mutations in both sides of the photosystem I reaction center identify the
RT phylloquinone observed by electron paramagnetic resonance spectroscopy.";
RL J. Biol. Chem. 276:37299-37306(2001).
RN [10]
RP PRESENCE OF CHLOROPHYLL A' IN PSI.
RC STRAIN=IAM C-9;
RX PubMed=12755700; DOI=10.1046/j.1432-1033.2003.03616.x;
RA Nakamura A., Akai M., Yoshida E., Taki T., Watanabe T.;
RT "Reversed-phase HPLC determination of chlorophyll a' and phylloquinone in
RT photosystem I of oxygenic photosynthetic organisms.";
RL Eur. J. Biochem. 270:2446-2458(2003).
CC -!- FUNCTION: PsaA and PsaB bind P700, the primary electron donor of
CC photosystem I (PSI), as well as the electron acceptors A0, A1 and FX.
CC PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase,
CC converting photonic excitation into a charge separation, which
CC transfers an electron from the donor P700 chlorophyll pair to the
CC spectroscopically characterized acceptors A0, A1, FX, FA and FB in
CC turn. Oxidized P700 is reduced on the lumenal side of the thylakoid
CC membrane by plastocyanin or cytochrome c6.
CC -!- FUNCTION: Both potential cofactor branches in PSI seem to be active;
CC however, electron transfer seems to proceed preferentially down the
CC path including the phylloquinone bound by PsaA.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced [plastocyanin]
CC = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:30407, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC Rhea:RHEA-COMP:10039, Rhea:RHEA-COMP:10040, ChEBI:CHEBI:29036,
CC ChEBI:CHEBI:30212, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:49552; EC=1.97.1.12;
CC -!- COFACTOR:
CC Note=P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more
CC chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-
CC 4S iron-sulfur center. {ECO:0000250};
CC -!- SUBUNIT: The PsaA/B heterodimer binds the P700 chlorophyll special pair
CC and subsequent electron acceptors. PSI consists of a core antenna
CC complex that captures photons, and an electron transfer chain that
CC converts photonic excitation into a charge separation. The eukaryotic
CC PSI reaction center is composed of at least 11 subunits.
CC -!- INTERACTION:
CC P12154; Q84V18: STT7; NbExp=4; IntAct=EBI-601796, EBI-15762546;
CC P12154; O20031: ycf3; NbExp=3; IntAct=EBI-601796, EBI-601871;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-
CC pass membrane protein.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000305}.
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DR EMBL; X05845; CAA29286.1; -; Genomic_DNA.
DR EMBL; X05846; CAA29286.1; JOINED; Genomic_DNA.
DR EMBL; X05847; CAA29286.1; JOINED; Genomic_DNA.
DR EMBL; FJ423446; ACJ50108.1; -; Genomic_DNA.
DR EMBL; AB044419; BAB18345.1; -; Genomic_DNA.
DR EMBL; BK000554; DAA01471.1; -; Genomic_DNA.
DR PIR; A28341; A28341.
DR RefSeq; NP_958375.1; NC_005353.1.
DR PDB; 6IJJ; EM; 2.89 A; A=1-751.
DR PDB; 6IJO; EM; 3.30 A; A=1-751.
DR PDB; 6JO5; EM; 2.90 A; A=1-751.
DR PDB; 6JO6; EM; 2.90 A; A=1-751.
DR PDB; 7BGI; EM; 2.54 A; A=11-751.
DR PDB; 7BLX; EM; 3.15 A; A=11-751.
DR PDB; 7D0J; EM; 3.42 A; A=12-751.
DR PDB; 7DZ7; EM; 2.84 A; A=1-751.
DR PDB; 7DZ8; EM; 3.16 A; A=1-751.
DR PDB; 7O01; EM; 17.10 A; A/a=11-751.
DR PDBsum; 6IJJ; -.
DR PDBsum; 6IJO; -.
DR PDBsum; 6JO5; -.
DR PDBsum; 6JO6; -.
DR PDBsum; 7BGI; -.
DR PDBsum; 7BLX; -.
DR PDBsum; 7D0J; -.
DR PDBsum; 7DZ7; -.
DR PDBsum; 7DZ8; -.
DR PDBsum; 7O01; -.
DR AlphaFoldDB; P12154; -.
DR SMR; P12154; -.
DR BioGRID; 974757; 2.
DR DIP; DIP-34985N; -.
DR IntAct; P12154; 16.
DR STRING; 3055.DAA01471; -.
DR PaxDb; P12154; -.
DR PRIDE; P12154; -.
DR GeneID; 2717000; -.
DR KEGG; cre:ChreCp019; -.
DR eggNOG; ENOG502QRYE; Eukaryota.
DR HOGENOM; CLU_370334_0_0_1; -.
DR InParanoid; P12154; -.
DR OrthoDB; 209831at2759; -.
DR BioCyc; MetaCyc:CHRECP019-MON; -.
DR BRENDA; 1.97.1.12; 1318.
DR Proteomes; UP000006906; Chloroplast.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.1130.10; -; 1.
DR HAMAP; MF_00458; PSI_PsaA; 1.
DR InterPro; IPR006243; PSI_PsaA.
DR InterPro; IPR001280; PSI_PsaA/B.
DR InterPro; IPR020586; PSI_PsaA/B_CS.
DR InterPro; IPR036408; PSI_PsaA/B_sf.
DR PANTHER; PTHR30128:SF61; PTHR30128:SF61; 1.
DR Pfam; PF00223; PsaA_PsaB; 1.
DR PIRSF; PIRSF002905; PSI_A; 1.
DR PRINTS; PR00257; PHOTSYSPSAAB.
DR SUPFAM; SSF81558; SSF81558; 1.
DR TIGRFAMs; TIGR01335; psaA; 1.
DR PROSITE; PS00419; PHOTOSYSTEM_I_PSAAB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Chlorophyll; Chloroplast; Chromophore;
KW Electron transport; Iron; Iron-sulfur; Magnesium; Membrane; Metal-binding;
KW Oxidoreductase; Photosynthesis; Photosystem I; Plastid; Reference proteome;
KW Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..751
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000088539"
FT TRANSMEM 73..96
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..182
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..222
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..312
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..372
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..414
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..458
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255"
FT TRANSMEM 533..551
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255"
FT TRANSMEM 591..612
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255"
FT TRANSMEM 665..687
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255"
FT TRANSMEM 725..745
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255"
FT BINDING 575
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 584
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 676
FT /ligand="chlorophyll a'"
FT /ligand_id="ChEBI:CHEBI:189419"
FT /ligand_label="A1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT BINDING 684
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 692
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /evidence="ECO:0000250"
FT BINDING 693
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="A"
FT MUTAGEN 676
FT /note="H->C: No PSI detected."
FT /evidence="ECO:0000269|PubMed:11041867"
FT MUTAGEN 676
FT /note="H->F,L: Loss of P700 function."
FT /evidence="ECO:0000269|PubMed:11041867"
FT MUTAGEN 676
FT /note="H->Q: Impairment of P700 function. More severe; when
FT associated with 'Q-656' in PsaB."
FT /evidence="ECO:0000269|PubMed:11041867"
FT MUTAGEN 676
FT /note="H->S: Accumulates approximately 50% PSI."
FT /evidence="ECO:0000269|PubMed:11041867"
FT MUTAGEN 693
FT /note="W->F: Unable to photoaccumulate an electron on A1."
FT CONFLICT 513
FT /note="D -> E (in Ref. 1; CAA29286)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="V -> G (in Ref. 1; CAA29286)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="V -> H (in Ref. 1; CAA29286)"
FT /evidence="ECO:0000305"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:7BGI"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 66..97
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 101..106
FT /evidence="ECO:0007829|PDB:7BGI"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:7DZ7"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 156..182
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 194..202
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 204..219
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 221..229
FT /evidence="ECO:0007829|PDB:7BGI"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 240..245
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 255..259
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 269..274
FT /evidence="ECO:0007829|PDB:7BGI"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 291..308
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 314..320
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 322..328
FT /evidence="ECO:0007829|PDB:7BGI"
FT TURN 332..336
FT /evidence="ECO:0007829|PDB:7DZ7"
FT HELIX 341..345
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 349..373
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 384..415
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 426..432
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 434..464
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 468..470
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 471..477
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 482..493
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 494..496
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 508..512
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 515..517
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 520..523
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 530..555
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 566..569
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 574..576
FT /evidence="ECO:0007829|PDB:7BLX"
FT HELIX 588..617
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 620..623
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 626..631
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 635..638
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 642..647
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 650..653
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 655..658
FT /evidence="ECO:0007829|PDB:7BGI"
FT TURN 661..665
FT /evidence="ECO:0007829|PDB:7D0J"
FT HELIX 666..687
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 690..706
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 712..714
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 720..750
FT /evidence="ECO:0007829|PDB:7BGI"
SQ 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
