PSAB_SYNEL
ID PSAB_SYNEL Reviewed; 741 AA.
AC P0A408; P25897;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 79.
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};
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_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.;
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_00482}.
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DR EMBL; X63768; CAA45305.1; -; Genomic_DNA.
DR AlphaFoldDB; P0A408; -.
DR SMR; P0A408; -.
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; Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..741
FT /note="Photosystem I P700 chlorophyll a apoprotein A2"
FT /id="PRO_0000088651"
FT TOPO_DOM 2..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 39..70
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TOPO_DOM 71..131
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305"
FT TRANSMEM 132..156
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TOPO_DOM 157..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 173..195
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TOPO_DOM 196..269
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305"
FT TRANSMEM 270..287
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TOPO_DOM 288..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 335..358
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TOPO_DOM 359..368
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305"
FT TRANSMEM 369..400
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TOPO_DOM 401..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 420..449
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TOPO_DOM 450..520
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305"
FT TRANSMEM 521..545
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TOPO_DOM 546..578
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 579..610
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TOPO_DOM 611..650
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305"
FT TRANSMEM 651..672
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TOPO_DOM 673..708
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 709..737
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TOPO_DOM 738..741
FT /note="Lumenal, thylakoid"
FT /evidence="ECO:0000305"
FT BINDING 566
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 575
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 661
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 669
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 677
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="B3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT BINDING 678
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
SQ SEQUENCE 741 AA; 83044 MW; 74961EF21401FB40 CRC64;
MATKFPKFSQ DLAQDPTTRR IWYAIAMAHD FESHDGMTEE NLYQKIFASH FGHLAIIFLW
VSGSLFHVAW QGNFEQWVQD PVNTRPIAHA IWDPQFGKAA VDAFTQAGAS NPVDIAYSGV
YHWWYTIGMR TNGDLYQGAI FLLILASLAL FAGWLHLQPK FRPSLSWFKN AESRLNHHLA
GLFGVSSLAW AGHLIHVAIP ESRGQHVGWD NFLSTMPHPA GLAPFFTGNW GVYAQNPDTA
SHVFGTAQGA GTAILTFLGG FHPQTESLWL TDMAHHHLAI AVLFIVAGHM YRTQFGIGHS
IKEMMDAKDF FGTKVEGPFN MPHQGIYETY NNSLHFQLGW HLACLGVITS LVAQHMYSLP
PYAFIAQDHT TMAALYTHHQ YIAGFLMVGA FAHGAIFLVR DYDPAQNKGN VLDRVLQHKE
AIISHLSWVS LFLGFHTLGL YVHNDVVVAF GTPEKQILIE PVFAQFIQAA HGKLLYGFDT
LLSNPDSIAS TAWPNYGNVW LPGWLDAINS GTNSLFLTIG PGDFLVHHAI ALGLHTTTLI
LVKGALDARG SKLMPDKKDF GYAFPCDGPG RGGTCDISAW DAFYLAMFWM LNTIGWVTFY
WHWKHLGVWE GNVAQFNESS TYLMGWLRDY LWLNSSQLIN GYNPFGTNNL SVWAWMFLFG
HLVWATGFMF LISWRGYWQE LIETLVWAHE RTPLANLVRW KDKPVALSIV QARLVGLAHF
SVGYILTYAA FLIASTAAKF G
