PSAA_PROM9
ID PSAA_PROM9 Reviewed; 767 AA.
AC Q318L9;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=PsaA {ECO:0000255|HAMAP-Rule:MF_00458};
GN Name=psaA {ECO:0000255|HAMAP-Rule:MF_00458};
GN OrderedLocusNames=PMT9312_1616;
OS Prochlorococcus marinus (strain MIT 9312).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9312;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-
CC Rule:MF_00458}.
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=PSI electron transfer chain: 5 divinyl chlorophyll a, 1 divinyl
CC chlorophyll a', 2 phylloquinones and 3 4Fe-4S clusters. PSI core
CC antenna: 90 divinyl chlorophyll a, 22 carotenoids, 3 phospholipids and
CC 1 galactolipid. P700 is a divinyl chlorophyll a/divinyl chlorophyll a'
CC dimer, A0 is one or more divinyl chlorophyll a, A1 is one or both
CC phylloquinones and FX is a shared 4Fe-4S iron-sulfur center.
CC {ECO:0000255|HAMAP-Rule:MF_00458};
CC -!- SUBUNIT: The PsaA/B heterodimer binds the P700 divinyl chlorophyll
CC special pair and subsequent electron acceptors. PSI consists of a core
CC antenna complex that captures photons, and an electron transfer chain
CC that 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.
CC {ECO:0000255|HAMAP-Rule:MF_00458}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_00458}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00458}.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000255|HAMAP-
CC Rule:MF_00458}.
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DR EMBL; CP000111; ABB50676.1; -; Genomic_DNA.
DR RefSeq; WP_011377158.1; NC_007577.1.
DR AlphaFoldDB; Q318L9; -.
DR SMR; Q318L9; -.
DR STRING; 74546.PMT9312_1616; -.
DR EnsemblBacteria; ABB50676; ABB50676; PMT9312_1616.
DR KEGG; pmi:PMT9312_1616; -.
DR eggNOG; COG2885; Bacteria.
DR HOGENOM; CLU_016126_1_0_3; -.
DR OMA; TWAFFHA; -.
DR OrthoDB; 32023at2; -.
DR Proteomes; UP000002715; Chromosome.
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: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; Chromophore; Electron transport; Iron; Iron-sulfur;
KW Magnesium; Membrane; Metal-binding; Oxidoreductase; Photosynthesis;
KW Photosystem I; Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..767
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000294202"
FT TRANSMEM 76..99
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 162..185
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 201..225
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 309..327
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 368..391
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 407..433
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 455..477
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 558..576
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 616..637
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 681..703
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 741..761
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 600
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 609
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 692
FT /ligand="divinylchlorophyll a'"
FT /ligand_id="ChEBI:CHEBI:189420"
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 700
FT /ligand="divinyl chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:73095"
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 708
FT /ligand="divinyl chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:73095"
FT /ligand_label="A3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 709
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
SQ SEQUENCE 767 AA; 84315 MW; 6107D52EC714F54F CRC64;
MTISPPESGE KNKKVLEDPV KADPRPIDFA KLDKPGFWST KLSKGPKTTT WIWNLHADAH
DFDVHTGDAE EATRKIFSAH FGHLAIIFIW MSAAFFHGAR FSNYTGWLAD PTNVKPGAQQ
VWAVVGQEML NGNLGADYNG IQISSGIFHM WRAWGITNES ELMALAIGAV IMAALMLHGG
IYHYHKAAPK LEWFQNIESM LNHHIAGLVG LGSLAWAGHC IHIGAPTAAL LDAIDAGSPL
VINGQKIATI ADMPMPHQLC DPQIIGQIFP GLASGVGNFF SLNWFAFSDF LTFKGGLNPV
TGSLWMTDIA HHHLAFGVIA IIGGHLYRTN YGIGSSMKEI LEAHQGDPIL FPAPKGHQGL
FEFMAESRHA QLSVNLACLG SLSILISHHM YAMPPYPYIA TDYMTVLGLF THHMWIGALF
IVGAGAHAGI AMVRDYDPAK HIDNVLDRIL KARDALISHL NWVCMWLGFH SFGLYIHNDT
MRALGRPQDM FSDNAIQLQP IFAQWVQSIQ ASAVGTSILA GTPEGLPQKA LSEVFNGSLV
EVGGKVAISP IQLGTADLMI HHIHAFQIHV TVLILLKGVL YARSSRLIPD KASLGFRFPC
DGPGRGGTCQ VSSWDHVFLA LFWMYNCISI VIFHFSWKMQ SDVWGLTGGN FSQSAITING
WLRDFLWAQS SQVLTSYGEA ISMYGLMFLG AHFIWAFSLM FLFSGRGYWQ ELFESIVWAH
NKLKVAPTIQ PRALSITQGR AVGVAHFLLG GIATTWAFFH ARLFGLG
