PSAA_SYNP6
ID PSAA_SYNP6 Reviewed; 763 AA.
AC Q5N0D6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=syc2044_d;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
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; AP008231; BAD80234.1; -; Genomic_DNA.
DR RefSeq; WP_011244354.1; NC_006576.1.
DR AlphaFoldDB; Q5N0D6; -.
DR SMR; Q5N0D6; -.
DR STRING; 269084.syc2044_d; -.
DR EnsemblBacteria; BAD80234; BAD80234; syc2044_d.
DR KEGG; syc:syc2044_d; -.
DR eggNOG; COG2885; Bacteria.
DR OMA; TWAFFHA; -.
DR Proteomes; UP000001175; 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..763
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000088593"
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 360..383
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 399..425
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 447..469
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 544..562
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 602..623
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 677..699
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 737..757
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 586
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 595
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 688
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 696
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 704
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 705
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
SQ SEQUENCE 763 AA; 83905 MW; 076F1B1242B941D4 CRC64;
MTISPPEREA KVKATVDKNP VPTSFEKWGK PGHFDRTLAK GPKTTTWIWN LHANAHDFDS
HTSDLEDISR KIFSAHFGHL AVIFIWLSGA YFHGARFSNF SGWLADPTHV KPSAQVVWPI
FGQEILNGDV GGGFHGIQIT SGLFQLWRAS GYTNEFQLYV TAIGALVMAG LMLFAGWFHY
HKAAPKLEWF QNVESMLNHH LAGLLGLGSL SWAGHQIHVS LPVNKLLDAI DAGEPLVLNG
KTIASAADIP LPHEFLDVSL ISQLFPGFEA GVKAFFTLNW SAYADFLTFK GGLNPVTGGL
WLTDTAHHHL AIAVLFIVAG HMYRTNWGIG HSLKEILEAH KGPFTGQGHK GLYEILTTSW
HAQLSINLAI LGSISIIVAH HMYAMPPYPY LATDYPTMLS LFTHHIWIGG FLIVGAGAHA
AIFMVRDYDP AKNVDNLLDR VLRHRDAIIS HLNWVCIWLG FHSFGLYIHN DTMRALGRPQ
DMFSDSAIQL QPIFAQWIQN IHALAPGNTA PNALASVSQV FGGDVVAVGG KVAAAPIVLG
TADFMVHHIH AFTIHVTALI LLKGVLYARS SRLVPDKANL GFRFPCDGPG RGGTCQVSGW
DHVFLGLFWM YNSLSIVIFH YSWKMQSDVW GSVLPDGSVA HIANGNFAQS ALTINGWLRD
FLWAQASQVI TSYGSSTSAY GLLFLGAHFV WAFSLMFLFS GRGYWQELIE SIVWAHNKLK
VAPAIQPRAL SIIQGRAVGV AHYLLGGIVT TWSFFLARII AVG
