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PSAA_PROMM
ID   PSAA_PROMM              Reviewed;         776 AA.
AC   Q7V510;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
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}; OrderedLocusNames=PMT_1770;
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
RN   [2]
RP   REPRESSION UNDER IRON-STARVATION.
RX   PubMed=12944966; DOI=10.1038/nature01933;
RA   Bibby T.S., Mary I., Nield J., Partensky F., Barber J.;
RT   "Low-light-adapted Prochlorococcus species possess specific antennae for
RT   each photosystem.";
RL   Nature 424:1051-1054(2003).
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 chlorophyll divinyl a, A1 is one or both
CC       phylloquinones and FX is a shared 4Fe-4S iron-sulfur center.
CC       {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.
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   -!- INDUCTION: Transcription decreases upon iron starvation.
CC       {ECO:0000269|PubMed:12944966}.
CC   -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00458}.
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DR   EMBL; BX548175; CAE21945.1; -; Genomic_DNA.
DR   RefSeq; WP_011131137.1; NC_005071.1.
DR   AlphaFoldDB; Q7V510; -.
DR   SMR; Q7V510; -.
DR   STRING; 74547.PMT_1770; -.
DR   EnsemblBacteria; CAE21945; CAE21945; PMT_1770.
DR   KEGG; pmt:PMT_1770; -.
DR   eggNOG; COG2885; Bacteria.
DR   HOGENOM; CLU_016126_1_0_3; -.
DR   OMA; TWAFFHA; -.
DR   OrthoDB; 32023at2; -.
DR   Proteomes; UP000001423; 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   2: Evidence at transcript level;
KW   4Fe-4S; Chlorophyll; Chromophore; Electron transport; Iron; Iron-sulfur;
KW   Magnesium; Membrane; Metal-binding; Oxidoreductase; Photosynthesis;
KW   Photosystem I; Reference proteome; Thylakoid; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..776
FT                   /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT                   /id="PRO_0000088589"
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        557..575
FT                   /note="Helical; Name=VIII"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        615..636
FT                   /note="Helical; Name=IX"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        690..712
FT                   /note="Helical; Name=X"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        750..770
FT                   /note="Helical; Name=XI"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   BINDING         599
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         608
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         701
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         709
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         717
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         718
FT                   /ligand="phylloquinone"
FT                   /ligand_id="ChEBI:CHEBI:18067"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
SQ   SEQUENCE   776 AA;  84981 MW;  31B48510039617D5 CRC64;
     MTISPPERGE KAKPIYDQPV DRDHVPADFE KFEQPGFFSK SLAKGPNSTT WIWNLHADAH
     DFDTHIGDLE ETSRKIFSAH FGHLAIVFIW MSGAFFHGAR FSNYSGWLAD PTHVKASAQV
     VWPIVGQEIM NADMGAGFNG IQITSGIFQM WRAWGITSET ELMALATGAL IMAALVLHGG
     IFHYHKAAPK LEWFKKIESM LQHHQIGLFG LGSLGWTGHL IHVANPTNAL LDAIDAGTPM
     VLDGKTIATA ADIPLPHELY NADLVGQIYP GLASGVGNFF SANWWAFSDF LTNNGGVNPV
     TGALWSTDVA HHHLAWAVFL MFGGHVYRSR FGIGHSMKEI MGNVKGDPLL FPAPNGHKGL
     FEFLSNSWHA QLAVNLACIG SGSIVVAHHM YSLPPYPYLA TDYPTVLGLF THHMWIGGLM
     ICGAAAHAGI AVIRDYDVSV HVDNVLDRMF KARDAIISHL NWVCMFLGFH SFGLYIHNDS
     MRALGRSQDM FSDSAIQLQP VLAQWIQSLW ASSIGTSAVV GTTTGLPGAV SDVFNGSVVA
     VGGKVALMAI PLGTADLMIH HIHAFTIHVT CLILLKGVLF ARSSRLVPDK ANLGFRFSCD
     GPGRGGTCQV SSWDHVFLGL FWMYNSLSMV IFYFSWKMQS DVWGTVNSDG SVTHLVSGNF
     AQSAITVNGW FRDFLWAQSS QVLTSYGTGL SGYGLLFLGG HFVWAFSLMF LFSGRGYWQE
     LFESIIWAHN KLKLAPTIQP RALSITQGRA VGVTHFLFGG IVTTWAFFHA RLLGLG
 
 
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