PSAB_AMPCA
ID PSAB_AMPCA Reviewed; 644 AA.
AC P58383;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A2;
DE EC=1.97.1.12;
DE AltName: Full=PSI-B;
DE AltName: Full=PsaB;
GN Name=psaB;
OS Amphidinium carterae (Dinoflagellate).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Alveolata; Dinophyceae; Amphidiniales; Amphidiniaceae;
OC Amphidinium.
OX NCBI_TaxID=2961;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CS21;
RX PubMed=11576546; DOI=10.1016/s0014-5793(01)02871-x;
RA Hiller R.G.;
RT "'Empty' minicircles and petB/atpA and psbD/psbE (cytb559 alpha) genes in
RT tandem in Amphidinium carterae plastid DNA.";
RL FEBS Lett. 505:449-452(2001).
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 (By similarity).
CC {ECO:0000250}.
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; AJ311629; CAC34542.2; -; Genomic_DNA.
DR AlphaFoldDB; P58383; -.
DR SMR; P58383; -.
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; -; 3.
DR InterPro; IPR001280; PSI_PsaA/B.
DR InterPro; IPR020586; PSI_PsaA/B_CS.
DR InterPro; IPR036408; PSI_PsaA/B_sf.
DR Pfam; PF00223; PsaA_PsaB; 3.
DR SUPFAM; SSF81558; SSF81558; 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..644
FT /note="Photosystem I P700 chlorophyll a apoprotein A2"
FT /id="PRO_0000088601"
FT TRANSMEM 58..81
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..190
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..249
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..287
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..329
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..370
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..447
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..508
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255"
FT TRANSMEM 555..577
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255"
FT TRANSMEM 621..641
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255"
FT BINDING 471
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 480
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 566
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="B1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 574
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="B3"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 582
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="B3"
FT /evidence="ECO:0000250"
FT BINDING 583
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
SQ SEQUENCE 644 AA; 70711 MW; 140796C76EBA65D6 CRC64;
MGTVFSRLFQ SVLLVCPIKR VSIRLGSYGR CATQRYFQVL GNIHDIELNE SLNSPQAIQA
LSFGQLSVIL LWLAAYTFHI GWSGNFEAFI DNPLGVQPIN HFVLDPHYSQ YKVDTTIAAL
ANHPIYHWLM TVGFTSNAQI YRFTLGLEIT AAVMLVLSLA PSVGLLSMGG LEVVSWISIC
WAGHLVNFAP GAANLTNVVM EGPGSLGNLM NVLTFNGGIQ LDTQALAVSD VAHHHVAIGI
VGLWISALLR VSKYAWNFNT QSSYHLDLSL SLTVGGILTS LLAQQAYVYP ALSYLPYDYL
ATTSLYVHHQ YIGAFLATGG FVHGGIFLVR DYTLSNDLVG KLLATKATVI STLSWITLFL
GFHATGLYMH NDAMAAFGVP QKQIIIEPVF AEFIQQVFFL GTPVYGLGSA AVSSTPTLSF
LPIISGGDFL VHHAIALGLH TTVLVLIKGA LDSQGSYLFP DKQSFGYGFA CDGPGRGGTC
DISTWDSFYL AFFWVNNTVA WFTYYFHWKV LSLWQSSTAV SDEDSLYLMG WFRDYLWQNC
AALLSGYDSL GSNDLAVWAW AFLLAHLAWA TGFMFLISWR GYWQELIDTV IYMHLKAQAR
FIGLAADVVT PVALSIVQAR FIGLAHYVAG FILTYHAFVV GATS
