PSAC_ANASL
ID PSAC_ANASL Reviewed; 9 AA.
AC P83158;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 07-APR-2021, entry version 50.
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;
DE Flags: Fragment;
GN Name=psaC;
OS Anabaena sp. (strain L31).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena;
OC unclassified Anabaena.
OX NCBI_TaxID=29412;
RN [1]
RP PROTEIN SEQUENCE OF 2-9.
RA Apte S.K., Uhlemann E., Schmid R., Altendorf K.;
RL Submitted (OCT-2001) to UniProtKB.
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 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW Membrane; Metal-binding; Oxidoreductase; Photosynthesis; Photosystem I;
KW Repeat; Thylakoid; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.1"
FT CHAIN 2..>9
FT /note="Photosystem I iron-sulfur center"
FT /id="PRO_0000262936"
FT DOMAIN 2..>9
FT /note="4Fe-4S ferredoxin-type"
FT NON_TER 9
SQ SEQUENCE 9 AA; 1093 MW; 9A82505322D1A1F5 CRC64;
MSHTVKIYD