PSAA_PROMA
ID PSAA_PROMA Reviewed; 773 AA.
AC Q9L4N4;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 133.
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=Pro_1672;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=16228480; DOI=10.1023/a:1006445810996;
RA van der Staay G.W.M., Moon-van der Staay S.Y., Garczarek L., Partensky F.;
RT "Rapid evolutionary divergence of photosystem I core subunits PsaA and PsaB
RT in the marine prokaryote Prochlorococcus.";
RL Photosyn. Res. 65:131-139(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
RN [3]
RP REPRESSION UNDER IRON-STARVATION.
RC STRAIN=SARG / CCMP1375 / SS120;
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 divinylchlorophyll 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 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 -!- 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; AJ133192; CAB64198.2; -; Genomic_DNA.
DR EMBL; AE017126; AAQ00716.1; -; Genomic_DNA.
DR RefSeq; NP_876063.1; NC_005042.1.
DR RefSeq; WP_011125821.1; NC_005042.1.
DR AlphaFoldDB; Q9L4N4; -.
DR SMR; Q9L4N4; -.
DR STRING; 167539.Pro_1672; -.
DR EnsemblBacteria; AAQ00716; AAQ00716; Pro_1672.
DR GeneID; 54200997; -.
DR KEGG; pma:Pro_1672; -.
DR PATRIC; fig|167539.5.peg.1766; -.
DR eggNOG; COG2885; Bacteria.
DR HOGENOM; CLU_016126_1_0_3; -.
DR OMA; TWAFFHA; -.
DR OrthoDB; 32023at2; -.
DR Proteomes; UP000001420; 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..773
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000088588"
FT TRANSMEM 80..103
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 166..189
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 205..229
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 315..333
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 375..398
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 414..440
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 462..484
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 564..582
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 622..643
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 687..709
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 747..767
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 606
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 615
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 698
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 706
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 714
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 715
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT CONFLICT 252
FT /note="A -> C (in Ref. 1; CAB64198)"
FT /evidence="ECO:0000305"
FT CONFLICT 529..531
FT /note="AGN -> VVI (in Ref. 1; CAB64198)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 773 AA; 84946 MW; E67AB3F348A81638 CRC64;
MTISPPERGE KAKGAAPTPY DQPVDRDHAP IDYEKLNKPG FWSSKLSKGP KTTTWIWNLH
ADAHDFDTHL GDLEETSRKI FSAHFGHLAV VFIWMSAAFF HGARFSNYTG WLADPTNVKP
GAQVVWPVVG QEILNADLGG NYQGLQITSG IFQMWRAWGI TSEVQLMALA IGGVIMAALM
LHGGIYHYHK AAPKLEWFRK IEPMLQHHQI ALIGLGSIAW AGHLIHIGAP VAALLDAIDA
GNPLVVDGVS IASAADVTNL APRLCDPAVA SQIFPSLAGR TVENFFTLNW WAFTDILTNK
GGLNPVTGSL WMTDISHHHL AFGVFAIFGG HMWRNNVHGV GHSMKEIMDV HKGDPILFPA
PKGHQGIFEF LSNSWHGQLS INLAMVGSAS IVVAHHMYAL PPYPYIAIDY PTVLGLFTHH
MWIGGLFICG AAAHAGIAMI RDYDPAVHID NVLDRILKAR DAIISHLNWV CMWLGFHSFG
LYIHNDVMRA LGRPKDMFSD TGIQLQPFLA QWVQNLQQSA VGTGDLVGAG NLPGSVLSEV
FNGNVVEVGG KVAIAPIPLG TADLMIHHVH AFTIHVTLLI LLKGVLYARS SRLIPDKAQL
GFRFPCDGPG RGGTCQVSSW DHVFLGLFWM YNSLSVVIFH FSWKMQSDVW GLTGGNFAQS
SITINGWLRD FLWAQSSQVL TSYGQPISMY GLMFLGAHFV WAFSLMFLFS GRGYWQELFE
SIIWAHNKLK VAPTIQPRAL SITQGRAVGV AHFLLGGIAT TWAFFHARLI GLG
