ID I1Q6F0_ORYGL Unreviewed; 81 AA.
AC I1Q6F0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=19493635 {ECO:0000313|EnsemblPlants:ORGLA06G0271300.1};
GN Synonyms=psaC {ECO:0000256|HAMAP-Rule:MF_01303,
GN ECO:0000313|EMBL:AGY93336.1};
GN ORFNames=OrsajCp089 {ECO:0000313|EMBL:AHZ60760.1};
OS Oryza glaberrima (African rice).
OG Plastid {ECO:0000313|EMBL:AGY93336.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA06G0271300.1, ECO:0000313|Proteomes:UP000007306};
RN [1] {ECO:0000313|Proteomes:UP000007306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA Zuccolo A.;
RT "The complete genome of Oryza glaberrima.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGY93336.1}
RP NUCLEOTIDE SEQUENCE.
RA Pilkington S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AHZ60760.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24690362; DOI=10.1111/1755-0998.12258;
RA Mariac C., Scarcelli N., Pouzadou J., Barnaud A., Billot C., Faye A.,
RA Kougbeadjo A., Maillol V., Martin G., Sabot F., Santoni S., Vigouroux Y.,
RA Couvreur T.L.;
RT "Cost-effective enrichment hybridization capture of chloroplast genomes at
RT deep multiplexing levels for population genetics and phylogeography
RT studies.";
RL Mol. Ecol. Resour. 14:1103-1113(2014).
RN [4] {ECO:0000313|EMBL:AJC09498.1}
RP NUCLEOTIDE SEQUENCE.
RA Chen X.-L., Norrbom A., Zhu C.-D.;
RT "A systematic study of Ichneumonosoma Meijere, Pelmatops Enderlein,
RT Pseudopelmatops Shiraki and Soita Walker (Diptera: Tephritidae).";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:AJC99802.1}
RP NUCLEOTIDE SEQUENCE.
RA Kim K.-H., Lee J.-K., Yang K.-W., Lee S.-C., Yang T.-J.;
RT "High throughput and simultaneous assembly of complete chloroplast genome
RT and nrDNA in plant.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:AJC10172.1}
RP NUCLEOTIDE SEQUENCE.
RA Kim K.-H., Kim Y.-D., Yang T.-J.;
RT "High-throughput assembly of chloroplast and ribosomal DNAs in plant
RT genomes.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000313|EMBL:AJP33996.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=101328 {ECO:0000313|EMBL:AJP34077.1}, and 104040
RC {ECO:0000313|EMBL:AJP33996.1};
RX PubMed=26355750; DOI=10.1038/srep13957;
RA Wambugu P.W., Brozynska M., Furtado A., Waters D.L., Henry R.J.;
RT "Relationships of wild and domesticated rices (Oryza AA genome species)
RT based upon whole chloroplast genome sequences.";
RL Sci. Rep. 5:13957-13957(2015).
RN [8] {ECO:0000313|EnsemblPlants:ORGLA06G0271300.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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}.
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 cyanobacterial PSI reaction center is composed of one copy
CC each of PsaA,B,C,D,E,F,I,J,K,L,M and X, and forms trimeric complexes.
CC {ECO:0000256|HAMAP-Rule:MF_01303}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC Rule:MF_01303}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01303}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01303}.
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DR EMBL; KF359903; AGY93336.1; -; Genomic_DNA.
DR EMBL; KJ513090; AHZ60760.1; -; Genomic_DNA.
DR EMBL; KM103370; AJC09498.1; -; Genomic_DNA.
DR EMBL; KM103377; AJC10172.1; -; Genomic_DNA.
DR EMBL; KM088021; AJC99802.1; -; Genomic_DNA.
DR EMBL; KM881638; AJP33996.1; -; Genomic_DNA.
DR EMBL; KM881639; AJP34077.1; -; Genomic_DNA.
DR RefSeq; YP_009034147.1; NC_024175.1.
DR AlphaFoldDB; I1Q6F0; -.
DR SMR; I1Q6F0; -.
DR STRING; 4538.I1Q6F0; -.
DR EnsemblPlants; ORGLA03G0394500.1; ORGLA03G0394500.1; ORGLA03G0394500.
DR EnsemblPlants; ORGLA06G0242500.1; ORGLA06G0242500.1; ORGLA06G0242500.
DR EnsemblPlants; ORGLA06G0259000.1; ORGLA06G0259000.1; ORGLA06G0259000.
DR EnsemblPlants; ORGLA06G0271300.1; ORGLA06G0271300.1; ORGLA06G0271300.
DR EnsemblPlants; ORGLA07G0095000.1; ORGLA07G0095000.1; ORGLA07G0095000.
DR EnsemblPlants; ORGLA08G0208200.1; ORGLA08G0208200.1; ORGLA08G0208200.
DR EnsemblPlants; ORGLA10G0159600.1; ORGLA10G0159600.1; ORGLA10G0159600.
DR EnsemblPlants; ORGLA11G0196700.1; ORGLA11G0196700.1; ORGLA11G0196700.
DR GeneID; 19493635; -.
DR Gramene; ORGLA03G0394500.1; ORGLA03G0394500.1; ORGLA03G0394500.
DR Gramene; ORGLA06G0242500.1; ORGLA06G0242500.1; ORGLA06G0242500.
DR Gramene; ORGLA06G0259000.1; ORGLA06G0259000.1; ORGLA06G0259000.
DR Gramene; ORGLA06G0271300.1; ORGLA06G0271300.1; ORGLA06G0271300.
DR Gramene; ORGLA07G0095000.1; ORGLA07G0095000.1; ORGLA07G0095000.
DR Gramene; ORGLA08G0208200.1; ORGLA08G0208200.1; ORGLA08G0208200.
DR Gramene; ORGLA10G0159600.1; ORGLA10G0159600.1; ORGLA10G0159600.
DR Gramene; ORGLA11G0196700.1; ORGLA11G0196700.1; ORGLA11G0196700.
DR KEGG; ogl:19493635; -.
DR eggNOG; ENOG502S26M; Eukaryota.
DR HOGENOM; CLU_139698_8_0_1; -.
DR OMA; GHMSHAV; -.
DR Proteomes; UP000007306; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-UniRule.
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; PF12838; Fer4_7; 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:AGY93336.1};
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:AGY93336.1};
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; 8899 MW; 681F63DC8FC603BF CRC64;
MSHSVKIYDT CIGCTQCVRA CPTDVLEMIP WDGCKAKQIA SAPRTEDCVG CKRCESACPT
DFLSVRVYLG PETTRSMALS Y
//
