PSAA_PROHO
ID PSAA_PROHO Reviewed; 699 AA.
AC Q9AL93;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A1;
DE EC=1.97.1.12;
DE AltName: Full=PsaA;
DE Flags: Fragment;
GN Name=psaA;
OS Prochlorothrix hollandica.
OC Bacteria; Cyanobacteria; Pseudanabaenales; Prochlorotrichaceae;
OC Prochlorothrix.
OX NCBI_TaxID=1223;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Mychkin E., Bullerjahn G.S.;
RT "Structural variability in the psaA/psaB proteins of Prochlorothrix.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE REVISION TO 624.
RA Bullerjahn G.S.;
RL Unpublished observations (OCT-2001).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=PSI electron transfer chain: 5 chlorophyll a, 1 chlorophyll a', 2
CC phylloquinones and 3 4Fe-4S clusters. PSI core antenna: 90 chlorophyll
CC a, 22 carotenoids, 3 phospholipids and 1 galactolipid. P700 is a
CC chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1
CC is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur
CC 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
CC cyanobacterial PSI reaction center is composed of one copy each of
CC PsaA,B,C,D,E,F,I,J,K,L,M and X, and forms trimeric complexes (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000305}.
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DR EMBL; AY026898; AAK08970.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q9AL93; -.
DR SMR; Q9AL93; -.
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:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
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; 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; Chromophore; Electron transport; Iron; Iron-sulfur;
KW Magnesium; Membrane; Metal-binding; Oxidoreductase; Photosynthesis;
KW Photosystem I; Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT CHAIN <1..699
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000088587"
FT TRANSMEM 15..38
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..127
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..167
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..256
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..318
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..360
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..404
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255"
FT TRANSMEM 480..498
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255"
FT TRANSMEM 538..559
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255"
FT TRANSMEM 613..635
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255"
FT TRANSMEM 673..693
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255"
FT BINDING 522
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 531
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 624
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 632
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 640
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /evidence="ECO:0000250"
FT BINDING 641
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 699 AA; 76532 MW; A3737E9E66878BD9 CRC64;
FDSHTSDLED VSRKIFSAHF GHLAVIFIWL SGAYFHGARF SNYTAWLSDP ISIKPSAQVV
WPFRSIFGQE ILNGDVGGGF HGIQITSGLF HLWRACGITH SSELYATAIG ALVMAGLMLF
AGWFHYHKAA PKLEWFQNVE SMLNHHLSVL LGCGSLGWAG HLIHISLPVN ALLDAGVSPA
DIPLAKDYVL DAGYMAKFSQ LCRGLNPFFT LNWGVYSDFL TFKGGLNPQT GSLWLTDIAH
HQLAIAVLFI IAGHMYRTNW GIGHDMKALL DGHKGPVGEV GTGHAGLYEI LTTSWHAQLA
INLALLGSLS IIVAHHMYAM PPYPYLAIDY PTQLSLFTHH VWIGGFLIVG AGAHAAIFMI
RDYDPAKNVD NLLDRVIRHR DAIISHLNWV CIWLGFHSFG LYIHNDTMRA LGRPQDMFSD
SAIQLQPIFA QGIQSIQAAV AGSAQAPWVG AATSPVWGGD TIAVGGKVAM SAIPLGTADF
MVHHIHAFTI HVTVLILLKG VLYARNSRLV PDKAELGFAF PCDGPGRGGT CQVSAWDHVF
LGLFWMYNSL SIVIFHFSWK MQSDVWGTVY PDGSVLNITV GNFAESALTI NGRLRDFLWA
QAASVINSYG SALSAYGLMF LAAHFVWAFS LMFLFSGRGY WQELIESIVW AHNKLKVAPA
IQPRALSITQ GRAVGVAHYL LGGIATTWAF FLARIISVG
