ID L0TFZ5_TECGR Unreviewed; 81 AA. AC L0TFZ5; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 27-MAR-2024, entry version 47. DE RecName: Full=Photosystem I iron-sulfur center {ECO:0000256|ARBA:ARBA00013413, ECO:0000256|HAMAP-Rule:MF_01303}; DE EC=1.97.1.12 {ECO:0000256|ARBA:ARBA00013197, ECO:0000256|HAMAP-Rule:MF_01303}; DE AltName: Full=9 kDa polypeptide {ECO:0000256|ARBA:ARBA00032541, ECO:0000256|HAMAP-Rule:MF_01303}; DE AltName: Full=PSI-C {ECO:0000256|ARBA:ARBA00033423, ECO:0000256|HAMAP-Rule:MF_01303}; DE AltName: Full=Photosystem I subunit VII {ECO:0000256|ARBA:ARBA00030218, ECO:0000256|HAMAP-Rule:MF_01303}; DE AltName: Full=PsaC {ECO:0000256|ARBA:ARBA00031003, ECO:0000256|HAMAP-Rule:MF_01303}; GN Name=psaC {ECO:0000256|HAMAP-Rule:MF_01303, GN ECO:0000313|EMBL:CCP47184.1}; GN ORFNames=BN828_cpI1090 {ECO:0000313|EMBL:CCP47184.1}, BN828_cpII1090 GN {ECO:0000313|EMBL:CCP47273.1}, BN828_cpIII1090 GN {ECO:0000313|EMBL:CCP47362.1}; OS Tectona grandis (Teak). OG Plastid; Chloroplast {ECO:0000313|EMBL:CCP47184.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Lamiales; Lamiaceae; Tectonoideae; Tectona. OX NCBI_TaxID=41396 {ECO:0000313|EMBL:CCP47184.1}; RN [1] {ECO:0000313|EMBL:CCP47184.1} RP NUCLEOTIDE SEQUENCE. RA Volkaert H.A.; RT "Chloroplast DNA sequence of teak (Tectona grandis L. f.) and its RT diversity."; RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:QJQ74162.1} RP NUCLEOTIDE SEQUENCE. RA Liu F., Fan W., Yang J.-B., Xiang C.-L., Mower J.P., Li D.-Z., Zhu A.; RT "Punctuated rate equilibria and GC-biased gene conversion promote extreme RT mitochondrial inter- and intra-genomic synonymous divergence in subfamily RT Ajugoideae."; RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases. 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. CC {ECO:0000256|ARBA:ARBA00003402, 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; CC Evidence={ECO:0000256|ARBA:ARBA00000994, 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; HF567869; CCP47184.1; -; Genomic_DNA. DR EMBL; HF567870; CCP47273.1; -; Genomic_DNA. DR EMBL; HF567871; CCP47362.1; -; Genomic_DNA. DR EMBL; MN814870; QJQ74162.1; -; Genomic_DNA. DR RefSeq; YP_007353966.1; NC_020098.1. DR AlphaFoldDB; L0TFZ5; -. DR SMR; L0TFZ5; -. DR GeneID; 14468448; -. 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 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01303}; KW Chloroplast {ECO:0000313|EMBL:CCP47184.1}; KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP- KW Rule:MF_01303}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01303}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP- KW Rule:MF_01303}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01303}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01303}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_01303}; KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP- KW Rule:MF_01303}; KW Photosystem I {ECO:0000256|ARBA:ARBA00022836, ECO:0000256|HAMAP- KW Rule:MF_01303}; Plastid {ECO:0000313|EMBL:CCP47184.1}; KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01303}; KW Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|HAMAP-Rule:MF_01303}; KW Transport {ECO:0000256|ARBA:ARBA00022448, 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 BINDING 11 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000256|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:0000256|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:0000256|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:0000256|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:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01303" SQ SEQUENCE 81 AA; 9038 MW; 68071DB57FC603BF CRC64; MSHSVKIYDT CIGCTQCVRA CPTDVLEMIP WDGCKAKQIA SAPRTEDCVG CKRCESACPT DFLSVRVYLW HETTRSMGLA Y //