PSAA_ANGEV
ID PSAA_ANGEV Reviewed; 750 AA.
AC Q9MUJ5; A2T333;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 97.
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 {ECO:0000255|HAMAP-Rule:MF_00458};
OS Angiopteris evecta (Mule's foot fern) (Polypodium evectum).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Marattiidae; Marattiales; Marattiaceae; Angiopteris.
OX NCBI_TaxID=13825;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Roper J.M., Hansen S.K., Wolf P.G., Karol K.G., Mandoli D.F.,
RA Everett K.D.E., Kuehl J.V., Boore J.L.;
RT "The complete plastid genome sequence of Angiopteris evecta (G. Forst.)
RT Hoffm. (Marattiaceae).";
RL Am. Fern J. 97:95-106(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-730.
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; 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; DQ821119; ABG79600.1; -; Genomic_DNA.
DR EMBL; AF180020; AAF29821.1; -; Genomic_DNA.
DR RefSeq; YP_001023701.1; NC_008829.1.
DR AlphaFoldDB; Q9MUJ5; -.
DR SMR; Q9MUJ5; -.
DR GeneID; 4788250; -.
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..750
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000088531"
FT TRANSMEM 70..93
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 156..179
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 195..219
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 291..309
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 346..369
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 385..411
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 433..455
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 531..549
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 589..610
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 664..686
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 724..744
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 573
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 582
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 675
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 683
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 691
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 692
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT CONFLICT 28
FT /note="Q -> K (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="D -> E (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="H -> R (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="Q -> R (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="L -> I (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="N -> S (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="G -> A (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="R -> W (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="G -> S (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="L -> S (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="L -> V (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 263..264
FT /note="TS -> AL (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 270..271
FT /note="AD -> SE (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 299..300
FT /note="GV -> AI (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="V -> I (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="I -> L (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="L -> I (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="I -> V (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="T -> I (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="G -> R (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="V -> I (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="T -> I (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="I -> V (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="V -> A (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="F -> S (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="L -> S (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 498..500
FT /note="NAT -> GAA (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="I -> L (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="S -> A (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="I -> V (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="Q -> R (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 627
FT /note="S -> T (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 638..639
FT /note="AT -> SI (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
FT CONFLICT 670
FT /note="L -> F (in Ref. 2; AAF29821)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 750 AA; 83076 MW; 9EAEF93CFC5A9438 CRC64;
MTIRSPEPEV KIVVERDPIK TSFEKWAQPG HFSRTLAKGP NTTTWIWNLH ADAHDFDSHT
NDLEDISRKV FSAHFGQLAI ILIWLSGMYF HGARFSNYEA WLSDPTHIKP SAQVVWPIVG
QEILNGDVGG GFQGIQITSG FFQLWRASGI TNELQLYCTA IGALIFAGLM LFAGWFHYHK
AAPKLARFQD VESMLNHHLA GLLGLGSLGW AGHQVHVSLP INQLLDAGVD PKEIPLPHEF
ILNRDLLAQL YPSFAKGLTP FFTSNWSEYA DFLTFRGGLN PVTGGLWLTD TAHHHLAIGV
LFLVAGHMYR TNWGIGHSIK EILEAHKGPF TGEGHKGLYE ILTTSWHAQL ALNLAMLGSL
TIIVAHHMYS MPPYPYLATD YGTQLSLFTH HMWIGGFLVV GAAAHAAIFM VRDYDPTTQY
NNLLDRVLRH RDAIISHLNW VCIFLGFHSF GLYIHNDTMS ALGRPQDMFS DTAIQLQPIF
AQWIQNTHAF APSLTAPNAT ASTSLTWGGG DLIAVGGKVA LLPIPLGTAD FLVHHIHAFT
IHVTVLILLK GVLFARSSRL IPDKANLGFR FPCDGPGRGG TCQVSAWDHV FLGLFWMYNS
ISIVIFHFSW KMQSDVWGSI SDQGVVSHIT GGNFAQSATT INGWLRDFLW AQASQVIQSY
GSSLSAYGLL FLGAHFVWAF SLMFLFSGRG YWQELIESIV WAHNKLKVAP AIQPRALSIV
QGRAVGVAHY LLGGIATTWA FFLARIISVG
