PSAC_THEVL
ID PSAC_THEVL Reviewed; 81 AA.
AC P0A417; P18083; P20451;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Photosystem I iron-sulfur center;
DE EC=1.97.1.12;
DE AltName: Full=9 kDa polypeptide;
DE AltName: Full=PSI-C;
DE AltName: Full=Photosystem I subunit VII;
DE AltName: Full=PsaC;
GN Name=psaC;
OS Thermostichus vulcanus (Synechococcus vulcanus).
OC Bacteria; Cyanobacteria; Thermostichales; Thermostichaceae; Thermostichus.
OX NCBI_TaxID=32053;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2114016; DOI=10.1093/nar/18.12.3644;
RA Shimizu T., Hiyama T., Ikeuchi M., Koike H., Inoue Y.;
RT "Nucleotide sequence of the psaC gene of the cyanobacterium Synechococcus
RT vulcanus.";
RL Nucleic Acids Res. 18:3644-3644(1990).
RN [2]
RP PROTEIN SEQUENCE OF 2-32.
RX PubMed=2503399; DOI=10.1016/0014-5793(89)80971-8;
RA Koike H., Ikeuchi M., Hiyama T., Inoue Y.;
RT "Identification of photosystem I components from the cyanobacterium,
RT Synechococcus vulcanus by N-terminal sequencing.";
RL FEBS Lett. 253:257-263(1989).
CC -!- FUNCTION: Apoprotein for the two 4Fe-4S centers FA and FB of
CC photosystem I (PSI); essential for photochemical activity. FB is the
CC terminal electron acceptor of PSI, donating electrons to ferredoxin.
CC The C-terminus interacts with PsaA/B/D and helps assemble the protein
CC into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI
CC is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting
CC photonic excitation into a charge separation, which transfers an
CC electron from the donor P700 chlorophyll pair to the spectroscopically
CC characterized acceptors A0, A1, FX, FA and FB in turn (By similarity).
CC {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 2 [4Fe-4S] clusters. Cluster 2 is most probably the
CC spectroscopically characterized electron acceptor FA and cluster 1 is
CC most probably FB. {ECO:0000250};
CC -!- SUBUNIT: The cyanobacterial PSI reaction center is composed of one copy
CC each of PsaA,B,C,D,E,F,I,J,K,L,M and X, and forms trimeric complexes.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}.
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DR EMBL; D00590; BAA00468.1; -; Genomic_DNA.
DR PDB; 6K33; EM; 2.74 A; aC/bC/cC=2-81.
DR PDBsum; 6K33; -.
DR AlphaFoldDB; P0A417; -.
DR SMR; P0A417; -.
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:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009773; P:photosynthetic electron transport in photosystem I; IEA:InterPro.
DR HAMAP; MF_01303; PSI_PsaC; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR017491; PSI_PsaC.
DR Pfam; PF12838; Fer4_7; 1.
DR TIGRFAMs; TIGR03048; PS_I_psaC; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Photosynthesis;
KW Photosystem I; Repeat; Thylakoid; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2503399"
FT CHAIN 2..81
FT /note="Photosystem I iron-sulfur center"
FT /id="PRO_0000062020"
FT DOMAIN 2..31
FT /note="4Fe-4S ferredoxin-type 1"
FT DOMAIN 37..68
FT /note="4Fe-4S ferredoxin-type 2"
FT BINDING 11
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 17
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 81 AA; 8800 MW; ED5362F4D6E48F36 CRC64;
MAHTVKIYDT CIGCTQCVRA CPTDVLEMVP WDGCKAGQIA SSPRTEDCVG CKRCETACPT
DFLSIRVYLG AETTRSMGLA Y
