ID   L0TFZ5_TECGR            Unreviewed;        81 AA.
AC   L0TFZ5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   07-SEP-2016, entry version 23.
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: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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; asterids; lamiids; Lamiales; Lamiaceae;
OC   Lamiaceae incertae sedis; 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.
CC   -!- FUNCTION: Apoprotein for the two 4Fe-4S centers FA and FB of
CC       photosystem I (PSI); essential for photochemical activity. FB is
CC       the terminal electron acceptor of PSI, donating electrons to
CC       ferredoxin. The C-terminus interacts with PsaA/B/D and helps
CC       assemble the protein into the PSI complex. Required for binding of
CC       PsaD and PsaE to PSI. PSI is a plastocyanin-ferredoxin
CC       oxidoreductase, converting photonic excitation into a charge
CC       separation, which transfers an electron from the donor P700
CC       chlorophyll pair to the spectroscopically characterized acceptors
CC       A0, A1, FX, FA and FB in turn. {ECO:0000256|HAMAP-Rule:MF_01303}.
CC   -!- CATALYTIC ACTIVITY: Reduced plastocyanin + oxidized ferredoxin +
CC       light = oxidized plastocyanin + reduced ferredoxin.
CC       {ECO:0000256|HAMAP-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
CC       is most probably FB. {ECO:0000256|HAMAP-Rule:MF_01303};
CC   -!- SUBUNIT: The eukaryotic PSI reaction center is composed of at
CC       least 11 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
CC       {ECO:0000256|HAMAP-Rule:MF_01303}.
CC   -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.
CC       {ECO:0000256|HAMAP-Rule:MF_01303}.
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DR   EMBL; HF567869; CCP47184.1; -; Genomic_DNA.
DR   EMBL; HF567870; CCP47273.1; -; Genomic_DNA.
DR   EMBL; HF567871; CCP47362.1; -; Genomic_DNA.
DR   RefSeq; YP_007353966.1; NC_020098.1.
DR   SMR; L0TFZ5; 2-81.
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 carrier activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; 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   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:CCP47184.1};
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:CCP47184.1};
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       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   DOMAIN       39     68       4Fe-4S ferredoxin-type.
FT                                {ECO:0000259|PROSITE:PS51379}.
FT   METAL        11     11       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_01303}.
FT   METAL        14     14       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_01303}.
FT   METAL        17     17       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_01303}.
FT   METAL        21     21       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_01303}.
FT   METAL        48     48       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_01303}.
FT   METAL        51     51       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_01303}.
FT   METAL        54     54       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_01303}.
FT   METAL        58     58       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000256|HAMAP-Rule:MF_01303}.
SQ   SEQUENCE   81 AA;  9038 MW;  68071DB57FC603BF CRC64;
     MSHSVKIYDT CIGCTQCVRA CPTDVLEMIP WDGCKAKQIA SAPRTEDCVG CKRCESACPT
     DFLSVRVYLW HETTRSMGLA Y
//