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PSAA_COFAR
ID   PSAA_COFAR              Reviewed;         750 AA.
AC   A0A335;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 59.
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   Coffea arabica (Arabian coffee).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Rubiaceae; Ixoroideae; Gardenieae complex;
OC   Bertiereae - Coffeeae clade; Coffeeae; Coffea.
OX   NCBI_TaxID=13443;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17309688; DOI=10.1111/j.1467-7652.2007.00245.x;
RA   Samson N., Bausher M.G., Lee S.-B., Jansen R.K., Daniell H.;
RT   "The complete nucleotide sequence of the coffee (Coffea arabica L.)
RT   chloroplast genome: organization and implications for biotechnology and
RT   phylogenetic relationships amongst angiosperms.";
RL   Plant Biotechnol. J. 5:339-353(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-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; EF044213; ABJ89679.1; -; Genomic_DNA.
DR   RefSeq; YP_817482.1; NC_008535.1.
DR   AlphaFoldDB; A0A335; -.
DR   SMR; A0A335; -.
DR   GeneID; 4421876; -.
DR   Proteomes; UP000515148; Chloroplast Pltd.
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; Reference proteome; Thylakoid;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..750
FT                   /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT                   /id="PRO_0000275939"
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"
SQ   SEQUENCE   750 AA;  83059 MW;  E185398CD391C305 CRC64;
     MIIRSPEPEV KILVDRDPVK TSFEEWAKPG HFSRTIAKGP DTTTWIWNLH ADAHDFDSHT
     SDLEEISRKV FSAHFGQLSI IFLWLSGMYF HGARFSNYEA WLSDPTHIGP SAQVVWPIVG
     QEILNGDVGG GFRGIQITSG FFQIWRASGI TNELQLYCTA IGALIFAALM LFAGWFHYHK
     AAPKLAWFQD VESMLNHHLA GLLGLGSLSW AGHQVHVSLP INQFLNAGVD PKEIPLPHEF
     ILNRDLLAQL YPSFAEGATP FFTLNWSKYA EFLTFRGGLD PVTGGLWLTD IAHHHLAIAI
     LFLIAGHMYR TNWGIGHGLK DILEAHKGPF TGQGHKGLYE ILTTSWHAQL SLNLAMLGSL
     TIVVAHHMYS MPPYPYLATD YGTQLSLFTH HMWIGGFLIV GAAAHAAIFM VRDYDPTTRY
     NDLLDRVLRH RDAIISHLNW ACIFLGFHSF GLYIHNDTMS ALGRPQDMFS DTAIQLQPVF
     AQWIQNTHAL APGATAPGAT ASTSLTWGGG DLVAVGGKVA LLPIPLGTAD FLVHHIHAFT
     IHVTVLILLK GVLFARSSRL IPDKANLGFR FPCDGPGRGG TCQVSAWDHV FLGLFWMYNA
     ISVVIFHFSW KMQSDVWGSI SDQGVVTHIT GGNFAQSSIT INGWLRDFLW AQASQVIQSY
     GSSLSAYGLF FLGAHFVWAF SLMFLFSGRG YWQELIESIV WAHNKLKVAP ATQPRALSIV
     QGRAVGVTHY LLGGIATTWA FFLARIIAVG
 
 
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