PSAA_SYNEL
ID PSAA_SYNEL Reviewed; 755 AA.
AC P0A406; P25896;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
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};
OS Synechococcus elongatus.
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=32046;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8486290; DOI=10.1016/0378-1119(93)90618-d;
RA Muehlenhoff U., Haehnel W., Witt H.T., Herrmann R.G.;
RT "Genes encoding eleven subunits of photosystem I from the thermophilic
RT cyanobacterium Synechococcus sp.";
RL Gene 127:71-78(1993).
RN [2]
RP REVIEW.
RX PubMed=11687205; DOI=10.1016/s0005-2728(01)00195-5;
RA Fromme P., Jordan P., Krauss N.;
RT "Structure of photosystem I.";
RL Biochim. Biophys. Acta 1507:5-31(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.
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.;
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 -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000255|HAMAP-
CC Rule:MF_00458}.
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DR EMBL; X63768; CAA45304.1; -; Genomic_DNA.
DR AlphaFoldDB; P0A406; -.
DR SMR; P0A406; -.
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..755
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000088592"
FT TOPO_DOM 1..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 65..96
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TOPO_DOM 97..155
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305"
FT TRANSMEM 156..179
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TOPO_DOM 180..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 193..217
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TOPO_DOM 218..293
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305"
FT TRANSMEM 294..311
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TOPO_DOM 312..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 353..376
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TOPO_DOM 377..386
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305"
FT TRANSMEM 387..418
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TOPO_DOM 419..436
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 437..468
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TOPO_DOM 469..532
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305"
FT TRANSMEM 533..558
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TOPO_DOM 559..590
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 591..619
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TOPO_DOM 620..668
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305"
FT TRANSMEM 669..690
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TOPO_DOM 691..723
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 724..753
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 578
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 587
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 680
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 688
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 696
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 697
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
SQ SEQUENCE 755 AA; 83183 MW; 36A39CCE5D119AEA CRC64;
MTISPPEREP KVRVVVDNDP VPTSFEKWAK PGHFDRTLAR GPQTTTWIWN LHALAHDFDT
HTSDLEDISR KIFSAHFGHL AVVFIWLSGM YFHGAKFSNY EAWLADPTGI KPSAQVVWPI
VGQGILNGDV GGGFHGIQIT SGLFQLWRAS GITNEFQLYC TAIGGLVMAG LMLFAGWFHY
HKRAPKLEWF QNVESMLNHH LAGLLGLGSL AWAGHQIHVS LPINKLLDAG VAAKDIPLPH
EFILNPSLMA ELYPKVDWGF FSGVIPFFTF NWAAYSDFLT FNGGLNPVTG GLWLSDTAHH
HLAIAVLFII AGHMYRTNWG IGHSLKEILE AHKGPFTGAG HKGLYEVLTT SWHAQLAINL
AMMGSLSIIV AQHMYAMPPY PYLATDYPTQ LSLFTHHMWI GGFLVVGGAA HGAIFMVRDY
DPAMNQNNVL DRVLRHRDAI ISHLNWVCIF LGFHSFGLYV HNDTMRAFGR PQDMFSDTGI
QLQPVFAQWV QNLHTLAPGG TAPNAAATAS VAFGGDVVAV GGKVAMMPIV LGTADFMVHH
IHAFTIHVTV LILLKGVLFA RSSRLIPDKA NLGFRFPCDG PGRGGTCQVS GWDHVFLGLF
WMYNCISVVI FHFSWKMQSD VWGTVAPDGT VSHITGGNFA QSAITINGWL RDFLWAQASQ
VIGSYGSALS AYGLLFLGAH FIWAFSLMFL FSGRGYWQEL IESIVWAHNK LKVAPAIQPR
ALSIIQGRAV GVAHYLLGGI ATTWAFFLAR IISVG
