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HAMAP rule MF_01303

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General rule information [?]

Accession MF_01303
Dates 6-JUN-2002 (Created)
1-JUN-2023 (Last updated, Version 57)
Name PSI_PsaC
Scope(s) Bacteria
Cyanobacteriota
Plastid
Template(s) Q00914 (PSAC_CHLRE); P0A411 (PSAC_TRIV2); P0A415 (PSAC_THEVB); P0A416 (PSAC_SYNEL); P31087 (PSAC_PICP2); P31085 (PSAC_SYNP6); P32422 (PSAC_SYNY3); [ Recover all ]
Triggered by HAMAP; MF_01303 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier PSAC
Protein name RecName: Full=Photosystem I iron-sulfur center;
                 EC=1.97.1.12;
AltName: Full=9 kDa polypeptide;
AltName: Full=PSI-C;
AltName: Full=Photosystem I subunit VII;
AltName: Full=PsaC;
Gene name Name=psaC;

Comments [?]

case <OC:Cyanobacteriota> or <OG:Chloroplast> and not <OC:Streptophyta>
FUNCTIONApoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn.
end case
case <OG:Chloroplast> and <OC:Streptophyta>
FUNCTIONApoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn.
end case
CATALYTIC ACTIVITY Reaction=hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced [plastocyanin] = oxidized [plastocyanin] + reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:30407, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10039, Rhea:RHEA-COMP:10040, ChEBI:CHEBI:29036, ChEBI:CHEBI:30212, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:49552; EC=1.97.1.12;
COFACTOR Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 2 [4Fe-4S] clusters. Cluster 2 is most probably the spectroscopically characterized electron acceptor FA and cluster 1 is most probably FB.;
case <OG:Chloroplast>
SUBUNITThe eukaryotic PSI reaction center is composed of at least 11 subunits.
SUBCELLULAR LOCATIONPlastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side.
else case <OC:Gloeobacter>
SUBUNITThe cyanobacterial PSI reaction center is composed of one copy each of PsaA,B,C,D,E,F,I,J,K,L,M and X, and forms trimeric complexes.
SUBCELLULAR LOCATIONCell inner membrane; Peripheral membrane protein; Cytoplasmic side.
else
SUBUNITThe cyanobacterial PSI reaction center is composed of one copy each of PsaA,B,C,D,E,F,I,J,K,L,M and X, and forms trimeric complexes.
SUBCELLULAR LOCATIONCellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side.
end case

Keywords [?]


Gene Ontology [?]

GO:0009055; Molecular function:electron transfer activity
GO:0015979; Biological process:photosynthesis
case <OG:Chloroplast>
GO:0009535; Cellular component:chloroplast thylakoid membrane
else case <OCellular component:Gloeobacter>
GO:0005886; Cellular component:plasma membrane
else; https://www.ebi.ac.uk/QuickGO/term/else
GO:0042651; Cellular component:thylakoid membrane
end case

Cross-references [?]

Pfam PF00037; Fer4; 2;
PRINTS PR00353; 4FE4SFRDOXIN; 2;
PROSITE PS00198; 4FE4S_FER_1; 2;
PROSITE PS51379; 4FE4S_FER_2; 2;
NCBIfam TIGR03048; PS_I_psaC; 1;

Features [?]

From: PSAC_THEVB (P0A415)
Key From To Description Tag Condition FTGroup
BINDING 11 11 /ligand="[4Fe-4S] cluster"
/ligand_id="ChEBI:CHEBI:49883"
/ligand_label="1"
C
BINDING 14 14 /ligand="[4Fe-4S] cluster"
/ligand_id="ChEBI:CHEBI:49883"
/ligand_label="1"
C
BINDING 17 17 /ligand="[4Fe-4S] cluster"
/ligand_id="ChEBI:CHEBI:49883"
/ligand_label="1"
C
BINDING 21 21 /ligand="[4Fe-4S] cluster"
/ligand_id="ChEBI:CHEBI:49883"
/ligand_label="2"
C
BINDING 48 48 /ligand="[4Fe-4S] cluster"
/ligand_id="ChEBI:CHEBI:49883"
/ligand_label="2"
C
BINDING 51 51 /ligand="[4Fe-4S] cluster"
/ligand_id="ChEBI:CHEBI:49883"
/ligand_label="2"
C
BINDING 54 54 /ligand="[4Fe-4S] cluster"
/ligand_id="ChEBI:CHEBI:49883"
/ligand_label="2"
C
BINDING 58 58 /ligand="[4Fe-4S] cluster"
/ligand_id="ChEBI:CHEBI:49883"
/ligand_label="1"
C

Additional information [?]

Size range 81-93 amino acids
Related rules None
Fusion Nter: None Cter: None



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