PSAB_SYNPW
ID PSAB_SYNPW Reviewed; 738 AA.
AC Q9R6T9; A5GIQ3;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A2 {ECO:0000255|HAMAP-Rule:MF_00482};
DE EC=1.97.1.12 {ECO:0000255|HAMAP-Rule:MF_00482};
DE AltName: Full=PsaB {ECO:0000255|HAMAP-Rule:MF_00482};
GN Name=psaB {ECO:0000255|HAMAP-Rule:MF_00482};
GN OrderedLocusNames=SynWH7803_0392;
OS Synechococcus sp. (strain WH7803).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32051;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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=WH7803;
RG Genoscope;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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_00482}.
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_00482};
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_00482};
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_00482}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_00482}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00482}.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000255|HAMAP-
CC Rule:MF_00482}.
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DR EMBL; AJ133190; CAB64209.1; -; Genomic_DNA.
DR EMBL; CT971583; CAK22818.1; -; Genomic_DNA.
DR RefSeq; WP_011932315.1; NC_009481.1.
DR AlphaFoldDB; Q9R6T9; -.
DR SMR; Q9R6T9; -.
DR STRING; 32051.SynWH7803_0392; -.
DR EnsemblBacteria; CAK22818; CAK22818; SynWH7803_0392.
DR KEGG; syx:SynWH7803_0392; -.
DR eggNOG; COG2885; Bacteria.
DR HOGENOM; CLU_016126_1_0_3; -.
DR OMA; FEQWVAD; -.
DR OrthoDB; 36958at2; -.
DR Proteomes; UP000001566; 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_00482; PSI_PsaB; 1.
DR InterPro; IPR001280; PSI_PsaA/B.
DR InterPro; IPR020586; PSI_PsaA/B_CS.
DR InterPro; IPR036408; PSI_PsaA/B_sf.
DR InterPro; IPR006244; PSI_PsaB.
DR Pfam; PF00223; PsaA_PsaB; 1.
DR PIRSF; PIRSF002905; PSI_A; 1.
DR PRINTS; PR00257; PHOTSYSPSAAB.
DR SUPFAM; SSF81558; SSF81558; 1.
DR TIGRFAMs; TIGR01336; psaB; 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..738
FT /note="Photosystem I P700 chlorophyll a apoprotein A2"
FT /id="PRO_0000088656"
FT TRANSMEM 46..69
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 135..158
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 175..199
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 273..291
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 333..356
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 372..398
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 420..442
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 521..539
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 579..600
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 647..669
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 711..731
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT BINDING 563
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_00482"
FT BINDING 572
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_00482"
FT BINDING 658
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="B1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT BINDING 666
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="B3"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT BINDING 674
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="B3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT BINDING 675
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
SQ SEQUENCE 738 AA; 81818 MW; B47FEE66CE669ACF CRC64;
MATKFPSFSQ GLAQDPTTRR IWYGIATAHD FESHDGMTEE KLYQKLFSTH FGHLAIIGLW
VSGNLFHIAW QGNFEQWVAD PLHVRPIAHA IWDPHFGQGA IDAFTQAGAS SPVNIAYSGL
YHWFYTIGMT TNAELYQGSI FMMILSAWAL FAGWLHLQPK FRPSLAWFKN AESRLNHHLA
VLFGFSSIAW TGHLVHVAIP ESRGQHVGWD NFLNVMPHPA GLGPFFTGNW GVYAQNPDTM
GQVFGSAEGS GTAILTFLGG FHPQTEALWL TDIAHHHLAI GVIFVIAGHM YRTNFGIGHS
IREILEAHNP PQGTPGDLGA GHKGLYDTIN NSLHFQLGLA LASLGVVTSL VAQHMYAMPS
YAFIAKDYTT QAALYTHHQY IAIFLMCGAF AHGAIFFIRD YDPEANKDNV LARMLEHKEA
IISHLSWVSL FLGFHTLGLY VHNDVVVAFG TPEKQILVEP VFAQFVQAAS GKAIYGFDVL
LANTGGVAAN ANAAYMGGWM DAINGVRGSN DLFLPIGPGD FLVHHAIALG LHTTTLILVK
GALDARGSKL MPDKKDFGYS FPCDGPGRGG TCDISAWDAF YLAVFWALNT VGWVTFYWHW
KHLAIWQGNV AQFNESSTYL MGWFRDYLWL NSSQLINGYN PFGSNNLAVW AWMFLFGHLV
WATGFMFLIS WRGYWQELIE TIVWAHQRTP LANLVGWRDK PVALSIVQAR VVGLAHFTIG
YILTYAAFLI ASTSGKFG
