PSAB_CYAM1
ID PSAB_CYAM1 Reviewed; 732 AA.
AC Q85FY6;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=PSI-B {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 Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC Cyanidioschyzon.
OX NCBI_TaxID=280699;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3377 / 10D;
RX PubMed=12755171; DOI=10.1093/dnares/10.2.67;
RA Ohta N., Matsuzaki M., Misumi O., Miyagishima S.-Y., Nozaki H., Tanaka K.,
RA Shin-i T., Kohara Y., Kuroiwa T.;
RT "Complete sequence and analysis of the plastid genome of the unicellular
RT red alga Cyanidioschyzon merolae.";
RL DNA Res. 10:67-77(2003).
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=P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more
CC chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-
CC 4S iron-sulfur 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 eukaryotic
CC PSI reaction center is composed of at least 11 subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00482}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-
CC pass membrane protein.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000255|HAMAP-
CC Rule:MF_00482}.
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DR EMBL; AB002583; BAC76207.1; -; Genomic_DNA.
DR RefSeq; NP_849045.1; NC_004799.1.
DR PDB; 5ZGB; EM; 3.63 A; B=1-732.
DR PDB; 5ZGH; EM; 3.82 A; B=1-732.
DR PDB; 6FOS; X-ray; 4.00 A; B=8-732.
DR PDB; 7BLZ; EM; 3.10 A; B=2-732.
DR PDBsum; 5ZGB; -.
DR PDBsum; 5ZGH; -.
DR PDBsum; 6FOS; -.
DR PDBsum; 7BLZ; -.
DR AlphaFoldDB; Q85FY6; -.
DR SMR; Q85FY6; -.
DR STRING; 45157.CMV136CT; -.
DR EnsemblPlants; CMV136CT; CMV136CT; CMV136C.
DR GeneID; 844936; -.
DR Gramene; CMV136CT; CMV136CT; CMV136C.
DR KEGG; cme:CymeCp113; -.
DR eggNOG; ENOG502QRYE; Eukaryota.
DR HOGENOM; CLU_016126_1_0_1; -.
DR Proteomes; UP000007014; Chloroplast.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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: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 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Chlorophyll; Chloroplast; Chromophore;
KW Electron transport; Iron; Iron-sulfur; Magnesium; Membrane; Metal-binding;
KW Oxidoreductase; Photosynthesis; Photosystem I; Plastid; Reference proteome;
KW Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..732
FT /note="Photosystem I P700 chlorophyll a apoprotein A2"
FT /id="PRO_0000088612"
FT TRANSMEM 46..69
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 133..156
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 173..197
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 271..289
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 328..351
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 367..393
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 415..437
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 515..533
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 573..594
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 641..663
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 705..725
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT BINDING 557
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 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 652
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 660
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 668
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="B3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT BINDING 669
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
SQ SEQUENCE 732 AA; 82027 MW; 8C1958E12CBD4705 CRC64;
MATKFPKFSQ ALASDPTTRR IWYGIATAHD FESHDGMTEE NLYQKIFASH FGHLAIIFLW
TSGNLFHVAW QGNFEQWVAN PLKTKPLAHA IWDPHFGQAA LKAFTRGDTV ANISYSGVYH
WWYTIGIRNN VELYTGALGL LVLSAVFLLA GWLHIQPKFK PSLSWFKNNE SRLNHHLAGL
FGVSSLAWTG HLVHVAIPAS RGQHVGWDNF IMTPPHPAGL QPFFTGNWSV YAQSPDSMQH
VFGTSQGAGT AILTFLGGFH PQTQSLWLTD MAHHHLAIAV IFIVAGHMYR TNFGIGHNLK
TILEAHRPPS GRLGKGHIGI YQTLTNSLHF QLGLALASLS VVTSLVAQHM YAMPPYAYMA
FDYVTQSALY THHQYIAGLL IVGAFAHGAI FFIRDYDPEQ NQDNVLARML AHKEAVISHL
SWVSLFLGFH TLGLYVHNDV VVAFGNPEKQ ILIEPIFAQW IQATSGKMLY GFQVLLSSST
SNASVAAQQL WLPGWLEAVN NESNSLFLTI GPGDFLVHHA IALGLHTTTL ILVKGALDAR
GSKLMPDKKD FGYSFPCDGP GRGGTCDISA WDAFYLAMFW MLNTIGWVTF YWHWKHLSLW
QGNVAQFNES STYLMGWLRD YLWLNSSPLI NGYNPYGMNS LAVWSWMFLF AHLVWATGFM
FLISWRGYWQ ELIETLAWAH ERTPLANLIR WKDKPVALSI VQARLVGLVH FTVGYILTYA
AFVIASTAGK FS
