PSAA_MARBO
ID PSAA_MARBO Reviewed; 720 AA.
AC Q9MUK1;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 85.
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;
DE Flags: Fragment;
GN Name=psaA;
OS Marsilea botryocarpa (Water clover).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Salviniales; Marsileaceae; Marsilea.
OX NCBI_TaxID=113539;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10779539; DOI=10.1093/oxfordjournals.molbev.a026357;
RA Sanderson M.J., Wojciechowski M.F., Hu J.-M., Sher Khan T., Brady S.G.;
RT "Error, bias, and long-branch attraction in data for two chloroplast
RT photosystem genes in seed plants.";
RL Mol. Biol. Evol. 17:782-797(2000).
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-ferredoxin oxidoreductase, converting photonic
CC excitation into a charge separation, which transfers an electron from
CC the donor P700 chlorophyll pair to the spectroscopically characterized
CC acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on
CC the lumenal side of the thylakoid membrane by plastocyanin.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000305}.
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DR EMBL; AF180014; AAF29815.1; -; Genomic_DNA.
DR PRIDE; Q9MUK1; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1130.10; -; 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; 2.
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 3: Inferred from homology;
KW 4Fe-4S; Chlorophyll; Chloroplast; Chromophore; Electron transport; Iron;
KW Iron-sulfur; Magnesium; Membrane; Metal-binding; Oxidoreductase;
KW Photosynthesis; Photosystem I; Plastid; Thylakoid; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN <1..>720
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000088558"
FT TRANSMEM 60..83
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..169
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..209
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..299
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..359
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..401
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..445
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255"
FT TRANSMEM 521..539
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255"
FT TRANSMEM 579..600
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..676
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255"
FT TRANSMEM 714..>720
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255"
FT BINDING 563
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 572
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 665
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 /evidence="ECO:0000250"
FT BINDING 673
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 681
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /evidence="ECO:0000250"
FT BINDING 682
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 720
SQ SEQUENCE 720 AA; 79952 MW; 84D63D28F27B8CC9 CRC64;
XIMVEKDPVK TSFEKWAQPG HFSKALAKGP STTTWIWNLH ADAHDFDSHT NDLEDISRKI
FSAHFGQLGI IFIWLSGMYF HGARFSNYEA WLNDPTHVKP SAQVVWPIVG QEILNGDVGG
GFQGIQITSG FFQLWRASGI TSELQLYCTA IGGLIFAGLM FFAGWFHYHK AAPKLAWFQN
VESMLNHHLA GLLGLGSLAW AGHQIHVSLP INQLLDAGVD PKEIPLPHEF ILNRELMAQT
FPSFAKGLIP FFTLDWSEYS DFLTFRGGLN PVTGGLWLTD TAHHHLAIAV LFLVAGHMYR
TXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXAHHMYA
MPPYPYLATD YATQLSLFTH HMWIGGFLIV GAAAHAAIFM VRDYDPTTQY NNLLDRVIRH
RDAIISHLNW VCIFLGFHSF GLYIHNDTMS ALGRPQDMFS DTAIQLQPVF AQWVQNTHAL
APGSTAPNAA ASTSPTWGGS DLVAVGGKVA LAPIPLGTAD FLVHHIHAFT IHVTVLILLK
GVLFARSSRL IPDKANLGFR FPCDGPGRGG TCQVSAWDHV FLGLFWMYNS ISVVIFHFSW
KMQSDVWGSI SEEGVVNHIT GGNFAQSSTT INGWLRDFLW AQASQVIQSY GSSLSAYGLL
FLGAHFVWAF SLMFLFSGRG YWQELIESIV WAHNKLKVAP VTQPRALSII QGRAVGVAHY
