ID A0A386B0M6_CODAR Unreviewed; 81 AA. AC A0A386B0M6; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 11-DEC-2019, entry version 6. DE RecName: Full=Photosystem I iron-sulfur center {ECO:0000256|HAMAP-Rule:MF_01303}; DE EC=1.97.1.12 {ECO:0000256|HAMAP-Rule:MF_01303}; DE AltName: Full=9 kDa polypeptide {ECO:0000256|HAMAP-Rule:MF_01303}; DE AltName: Full=PSI-C {ECO:0000256|HAMAP-Rule:MF_01303}; DE AltName: Full=Photosystem I subunit VII {ECO:0000256|HAMAP-Rule:MF_01303}; DE AltName: Full=PsaC {ECO:0000256|HAMAP-Rule:MF_01303}; GN Name=psaC {ECO:0000256|HAMAP-Rule:MF_01303, GN ECO:0000313|EMBL:AYC65245.1}; OS Codium arabicum (Green alga). OG Plastid; Chloroplast {ECO:0000313|EMBL:AYC65245.1}. OC Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; TCBD clade; OC Bryopsidales; Codiaceae; Codium. OX NCBI_TaxID=221038 {ECO:0000313|EMBL:AYC65245.1}; RN [1] {ECO:0000313|EMBL:AYC65245.1} RP NUCLEOTIDE SEQUENCE. RA Quirk P.G., Krulwich T.A.; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AYC65245.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=30227214; DOI=10.1016/j.ympev.2018.09.009; RA Cremen M.C., Leliaert F., West J., Lam D.W., Shimada S., RA Lopez-Bautista J.M., Verbruggen H.; RT "Reassessment of the classification of bryopsidales (chlorophyta) based on RT chloroplast phylogenomic analyses."; RL Mol. Phylogenet. Evol. 130:397-405(2019). 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. CC {ECO:0000256|HAMAP-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:0000256|HAMAP- CC Rule:MF_01303}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_01303}; CC -!- SUBUNIT: The eukaryotic PSI reaction center is composed of at least 11 CC subunits. {ECO:0000256|HAMAP-Rule:MF_01303}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000256|HAMAP-Rule:MF_01303}; Peripheral membrane protein CC {ECO:0000256|HAMAP-Rule:MF_01303}; Stromal side {ECO:0000256|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; MH591107; AYC65245.1; -; Genomic_DNA. 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 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 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01303}; KW Chloroplast {ECO:0000313|EMBL:AYC65245.1}; KW Electron transport {ECO:0000256|HAMAP-Rule:MF_01303}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01303}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01303}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01303}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01303}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01303}; KW Photosynthesis {ECO:0000256|HAMAP-Rule:MF_01303}; KW Photosystem I {ECO:0000256|HAMAP-Rule:MF_01303}; KW Plastid {ECO:0000313|EMBL:AYC65245.1}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_01303}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01303}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01303}. FT DOMAIN 1..31 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" FT DOMAIN 39..68 FT /note="4Fe-4S ferredoxin-type" FT /evidence="ECO:0000259|PROSITE:PS51379" FT METAL 11 FT /note="Iron-sulfur 1 (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01303" FT METAL 14 FT /note="Iron-sulfur 1 (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01303" FT METAL 17 FT /note="Iron-sulfur 1 (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01303" FT METAL 21 FT /note="Iron-sulfur 2 (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01303" FT METAL 48 FT /note="Iron-sulfur 2 (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01303" FT METAL 51 FT /note="Iron-sulfur 2 (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01303" FT METAL 54 FT /note="Iron-sulfur 2 (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01303" FT METAL 58 FT /note="Iron-sulfur 1 (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01303" SQ SEQUENCE 81 AA; 8911 MW; 6D25044EBFE74582 CRC64; MAHNVKIYDT CIGCTQCVRA CPTDVLEMVP WKGCKAKQIA SAPRTEDCVG CKRCETACPT DFLSVRIYLG TETTRSMGLA Y //