PSAA_BIGNA
ID PSAA_BIGNA Reviewed; 751 AA.
AC Q06J42;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A1 {ECO:0000255|HAMAP-Rule:MF_00458};
DE EC=1.97.1.12 {ECO:0000255|HAMAP-Rule:MF_00458};
DE AltName: Full=PSI-A {ECO:0000255|HAMAP-Rule:MF_00458};
DE AltName: Full=PsaA {ECO:0000255|HAMAP-Rule:MF_00458};
GN Name=psaA-A {ECO:0000255|HAMAP-Rule:MF_00458};
GN and
GN Name=psaA-B {ECO:0000255|HAMAP-Rule:MF_00458};
OS Bigelowiella natans (Pedinomonas minutissima) (Chlorarachnion sp. (strain
OS CCMP621)).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Rhizaria; Cercozoa; Chlorarachniophyceae; Bigelowiella.
OX NCBI_TaxID=227086;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16990439; DOI=10.1093/molbev/msl129;
RA Rogers M.B., Gilson P.R., Su V., McFadden G.I., Keeling P.J.;
RT "The complete chloroplast genome of the chlorarachniophyte Bigelowiella
RT natans: evidence for independent origins of chlorarachniophyte and euglenid
RT secondary endosymbionts.";
RL Mol. Biol. Evol. 24:54-62(2007).
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 -!- 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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00458};
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:0000255|HAMAP-Rule:MF_00458};
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 {ECO:0000255|HAMAP-Rule:MF_00458}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_00458}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00458}.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000255|HAMAP-
CC Rule:MF_00458}.
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DR EMBL; DQ851108; ABG91408.1; -; Genomic_DNA.
DR EMBL; DQ851108; ABG91417.1; -; Genomic_DNA.
DR RefSeq; YP_778576.1; NC_008408.1.
DR RefSeq; YP_778585.1; NC_008408.1.
DR AlphaFoldDB; Q06J42; -.
DR SMR; Q06J42; -.
DR GeneID; 4352993; -.
DR GeneID; 4353002; -.
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 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..751
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000294231"
FT TRANSMEM 73..96
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 159..182
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 198..222
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 294..312
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 349..372
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 388..414
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 436..458
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 533..551
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 591..612
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 665..687
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 725..745
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
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:0000255|HAMAP-Rule:MF_00458"
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:0000255|HAMAP-Rule:MF_00458"
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 /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
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:0000255|HAMAP-Rule:MF_00458"
FT BINDING 692
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 693
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
SQ SEQUENCE 751 AA; 83932 MW; 80A4F4A40597F03A CRC64;
MAIDVSNQND DLVKVVVDVD PVPTDFERWA KPGHFSRSLS KGPLTTTWIW NLHADVHDFD
GYSTNLQDIS RKIFSAHFGQ LGIIFIWLSG MYFHGARFSN YEAWLSNPAK IKPSAQVVWP
IVGQDILNGD VGDGFRGVQI TSGLFHVWRA SGITNELELF STAIGGLVMA FLMFFAGWFH
YHKAAPKLQW FQNAESMLNH HLSGLLGLGS LSWAGHQIHI AIPINKLLDK GVSASEIPLP
HEFLVDKTQM INIFPSFEKG LTPFFTLNWK EYSDFLTFQG GLDPQTGSLW LTDIAHHHLA
IAVLFIVAGH MYKTNWSIGH RLKEILEGHK VLSVSKGHSG LYEIFTTSWH AQLSLNLAML
GSLSIIVAHH MYAMPPYPYI SVDYATQLSL FTHHMWIGGF CIVGAGAHAS IFMVRDYNPA
DNYNNLLDRI ICQRDAIISH LNWACIFLGL HSFGLYIHND TMSALGRSDD MFSDTAIQLQ
PIFSQFIQRI HYMTIESTAP YVSHGTSPAW GGDIVAINGK IAMMPISLGT SDFMVHHIHA
FTIHVTVLIL LKGVLFSRNS RLIPDKSNLG FRFPCDGPGR GGTCQVSAWD HVFLGLFWMY
NSLSIVIFHF SWKLQSDVWG NVNSSVVSHI TRGNFAQSAN TINGWLRDFL WSQSSQVIQS
YGSSLSAYGL IFLGAHFVWA FSLMFLFSGR GYWQELIESI VWAHNKLKVA PAIAPRALSI
TQGRAVGVAH YLLGGIGTTW SFFLARIISV N
