ID PSAC_PEA Reviewed; 81 AA. AC P10793; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 139. DE RecName: Full=Photosystem I iron-sulfur center {ECO:0000255|HAMAP-Rule:MF_01303}; DE EC=1.97.1.12 {ECO:0000255|HAMAP-Rule:MF_01303}; DE AltName: Full=9 kDa polypeptide {ECO:0000255|HAMAP-Rule:MF_01303}; DE AltName: Full=PSI-C {ECO:0000255|HAMAP-Rule:MF_01303}; DE AltName: Full=Photosystem I subunit VII {ECO:0000255|HAMAP-Rule:MF_01303}; DE AltName: Full=PsaC {ECO:0000255|HAMAP-Rule:MF_01303}; GN Name=psaC {ECO:0000255|HAMAP-Rule:MF_01303}; Synonyms=frxA; OS Pisum sativum (Garden pea) (Lathyrus oleraceus). OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum. OX NCBI_TaxID=3888; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX AGRICOLA=IND92000055; DOI=10.1007/BF00027388; RA Dunn P.P.J., Gray J.C.; RT "Localization and nucleotide sequence of the gene for the 8 kDa subunit of RT photosystem I in pea and wheat chloroplast DNA."; RL Plant Mol. Biol. 11:311-319(1988). RN [2] RP PROTEIN SEQUENCE OF 2-49. RX PubMed=3277857; DOI=10.1016/0014-5793(88)80607-0; RA Dunn P.P.J., Packman L.C., Pappin D., Gray J.C.; RT "N-terminal amino acid sequence analysis of the subunits of pea photosystem RT I."; RL FEBS Lett. 228:157-161(1988). 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-ferredoxin oxidoreductase, converting photonic CC excitation into a charge separation, which transfers an electron from CC the donor P700 chlorophyll pair to the spectroscopically characterized CC acceptors A0, A1, FX, FA and FB in turn. {ECO:0000255|HAMAP- CC Rule:MF_01303}. 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_01303}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01303}; 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:0000255|HAMAP-Rule:MF_01303}; CC -!- SUBUNIT: The eukaryotic PSI reaction center is composed of at least 11 CC subunits. {ECO:0000255|HAMAP-Rule:MF_01303}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000255|HAMAP-Rule:MF_01303}; Peripheral membrane protein CC {ECO:0000255|HAMAP-Rule:MF_01303}; Stromal side {ECO:0000255|HAMAP- CC Rule:MF_01303}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X13157; CAA31554.1; -; Genomic_DNA. DR PIR; S04033; FEPM1S. DR RefSeq; YP_003587533.1; NC_014057.1. DR PDB; 2O01; X-ray; 3.40 A; C=2-81. DR PDB; 2WSC; X-ray; 3.30 A; C=1-81. DR PDB; 2WSE; X-ray; 3.49 A; C=1-81. DR PDB; 2WSF; X-ray; 3.48 A; C=1-81. DR PDB; 3LW5; X-ray; 3.30 A; C=1-81. DR PDB; 4RKU; X-ray; 3.00 A; C=2-81. DR PDB; 4XK8; X-ray; 2.80 A; C/c=2-81. DR PDB; 4Y28; X-ray; 2.80 A; C=1-81. DR PDB; 5L8R; X-ray; 2.60 A; C=1-81. DR PDB; 6LY5; EM; 2.38 A; c=2-81. DR PDB; 6YAC; EM; 2.50 A; C=2-81. DR PDB; 6YEZ; EM; 2.70 A; C=2-81. DR PDB; 6ZOO; EM; 2.74 A; C=2-81. DR PDB; 6ZXS; X-ray; 3.00 A; C=2-81. DR PDB; 7DKZ; X-ray; 2.39 A; C=1-81. DR PDBsum; 2O01; -. DR PDBsum; 2WSC; -. DR PDBsum; 2WSE; -. DR PDBsum; 2WSF; -. DR PDBsum; 3LW5; -. DR PDBsum; 4RKU; -. DR PDBsum; 4XK8; -. DR PDBsum; 4Y28; -. DR PDBsum; 5L8R; -. DR PDBsum; 6LY5; -. DR PDBsum; 6YAC; -. DR PDBsum; 6YEZ; -. DR PDBsum; 6ZOO; -. DR PDBsum; 6ZXS; -. DR PDBsum; 7DKZ; -. DR AlphaFoldDB; P10793; -. DR EMDB; EMD-10746; -. DR EMDB; EMD-10798; -. DR EMDB; EMD-11326; -. DR EMDB; EMD-30012; -. DR SMR; P10793; -. DR DIP; DIP-60283N; -. DR IntAct; P10793; 3. DR GeneID; 9073063; -. DR EvolutionaryTrace; P10793; -. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. 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: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 Gene3D; 3.30.70.20; -; 1. 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 NCBIfam; TIGR03048; PS_I_psaC; 1. DR PANTHER; PTHR24960:SF88; PHOTOSYSTEM I IRON-SULFUR CENTER; 1. DR PANTHER; PTHR24960; PHOTOSYSTEM I IRON-SULFUR CENTER-RELATED; 1. DR Pfam; PF14697; Fer4_21; 1. DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 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; Chloroplast; Direct protein sequencing; KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; KW Oxidoreductase; Photosynthesis; Photosystem I; Plastid; Repeat; Thylakoid; KW Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:3277857" FT CHAIN 2..81 FT /note="Photosystem I iron-sulfur center" FT /id="PRO_0000061996" FT DOMAIN 2..31 FT /note="4Fe-4S ferredoxin-type 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01303" FT DOMAIN 39..68 FT /note="4Fe-4S ferredoxin-type 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01303" FT BINDING 11 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01303" FT BINDING 14 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01303" FT BINDING 17 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01303" FT BINDING 21 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01303" FT BINDING 48 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01303" FT BINDING 51 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01303" FT BINDING 54 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01303" FT BINDING 58 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01303" FT STRAND 4..7 FT /evidence="ECO:0007829|PDB:6LY5" FT HELIX 16..20 FT /evidence="ECO:0007829|PDB:6LY5" FT TURN 22..24 FT /evidence="ECO:0007829|PDB:2WSC" FT STRAND 27..30 FT /evidence="ECO:0007829|PDB:6LY5" FT STRAND 32..34 FT /evidence="ECO:0007829|PDB:6LY5" FT TURN 35..37 FT /evidence="ECO:0007829|PDB:2WSC" FT STRAND 38..41 FT /evidence="ECO:0007829|PDB:6LY5" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:6LY5" FT HELIX 53..57 FT /evidence="ECO:0007829|PDB:6LY5" FT STRAND 60..62 FT /evidence="ECO:0007829|PDB:6LY5" FT STRAND 64..68 FT /evidence="ECO:0007829|PDB:6LY5" FT HELIX 74..77 FT /evidence="ECO:0007829|PDB:6LY5" SQ SEQUENCE 81 AA; 8980 MW; 680556D8CB5603BF CRC64; MSHSVKIYDT CIGCTQCVRA CPTDVLEMIP WGGCKAKQIA SAPRTEDCVG CKRCESACPT DFLSVRVYLW HETTRSMGLA Y //