PSAA_SYNS3
ID PSAA_SYNS3 Reviewed; 767 AA.
AC Q0ID48;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=sync_0393;
OS Synechococcus sp. (strain CC9311).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=64471;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9311;
RX PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA Paulsen I.T.;
RT "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT coastal environment.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
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 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: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
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; CP000435; ABI47329.1; -; Genomic_DNA.
DR RefSeq; WP_011618363.1; NC_008319.1.
DR AlphaFoldDB; Q0ID48; -.
DR SMR; Q0ID48; -.
DR STRING; 64471.sync_0393; -.
DR EnsemblBacteria; ABI47329; ABI47329; sync_0393.
DR KEGG; syg:sync_0393; -.
DR eggNOG; COG2885; Bacteria.
DR HOGENOM; CLU_016126_1_0_3; -.
DR OMA; TWAFFHA; -.
DR OrthoDB; 32023at2; -.
DR Proteomes; UP000001961; 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; Reference proteome; Thylakoid; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..767
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000294206"
FT TRANSMEM 72..95
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 158..181
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 197..221
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 305..323
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 364..387
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 403..429
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 451..473
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 548..566
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 606..627
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 BINDING 590
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 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 692
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 700
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 708
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
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; 83681 MW; 3FC4D692542E34BA CRC64;
MTISPPERGS TAKSQVEKVD NPATFELFGK PGHFDRALAK GPKTTTWVWN LHANAHDFDS
HTSDLEEVSR KIFSAHFGHL AVIFIWLSGA FFHGARFSNF SGWLADPTHV KPSAQVVWPV
FGQEILNGDM GAGFQGIQIT SGLFHVWRAW GITNETQLMS LAIGALVMAG LMLNAGVFHY
HKAAPKLEWF QNVESMLNHH LAGLLGLGSL SWTGHLLHVS LPTTKLMDAI DAGQPLVLNG
KTIASVADIP LPHEFFNQDL IAQLYPGFGA GIGAFFSGDW AAYSDFLTFK GGINPVTGSM
WMSDIAHHHL AIAVLFIVAG HMYRTNWGIG HSIKEILEGQ KGDPLLFPAT KGHDGLFEFM
TTSWHAQLGV NLAMLGSLSI IVAQHMYAMP PYPYMAIDYP TQIGLFTHHM WIGGFLIVGA
AAHAAIAMIR DYDPAKHVDN VLDRVLKARD AIISHLNWVC IWLGAHSFGL YVHNDTMRAL
GRPQDMFSDS AISIQPVFAQ WIQGIHAGAA GSTAPNALAG VSEVFNGSTI AVGGKVAAAA
IPLGTADFMV HHIHAFTIHV TVLILLKGVL YARSSRLVPD KANLGFRFPC DGPGRGGTCQ
VSAWDHVFLG LFWMYNSLSV VIFHFSWKMQ SDVWGTVNAD GSVQHITNGN FANSAITING
WLRDFLWAQA AQVINSYGSN TSAYGLMFLG AHFVWAFSLM FLFSGRGYWQ ELIESIVWAH
NKLKVAPAIQ PRALSITQGR AVGVAHYLLG GIATTWAFFH AHILVVG
