PSAC_TOBAC
ID PSAC_TOBAC Reviewed; 81 AA.
AC P62094; P07136; P25252; Q9MRU0; Q9T2J4;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 85.
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 Nicotiana tabacum (Common tobacco).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Bright Yellow 4;
RX PubMed=16453699; DOI=10.1002/j.1460-2075.1986.tb04464.x;
RA Shinozaki K., Ohme M., Tanaka M., Wakasugi T., Hayashida N.,
RA Matsubayashi T., Zaita N., Chunwongse J., Obokata J.,
RA Yamaguchi-Shinozaki K., Ohto C., Torazawa K., Meng B.-Y., Sugita M.,
RA Deno H., Kamogashira T., Yamada K., Kusuda J., Takaiwa F., Kato A.,
RA Tohdoh N., Shimada H., Sugiura M.;
RT "The complete nucleotide sequence of the tobacco chloroplast genome: its
RT gene organization and expression.";
RL EMBO J. 5:2043-2049(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=cv. Bright Yellow 4;
RX PubMed=3329576; DOI=10.1007/bf00435285;
RA Hayashida N., Matsubayashi T., Shinozaki K., Sugiura M., Inoue K.,
RA Hiyama T.;
RT "The gene for the 9 kd polypeptide, a possible apoprotein for the iron-
RT sulfur centers A and B of the photosystem I complex, in tobacco chloroplast
RT DNA.";
RL Curr. Genet. 12:247-250(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1907869; DOI=10.1007/bf00023416;
RA Anderson S.L., McIntosh L.;
RT "Partial conservation of the 5' ndhE-psaC-ndhD 3' gene arrangement of
RT chloroplasts in the cyanobacterium Synechocystis sp. PCC 6803: implications
RT for NDH-D function in cyanobacteria and chloroplasts.";
RL Plant Mol. Biol. 16:487-499(1991).
RN [4]
RP SHOWS THAT SEQUENCE DESCRIBED IN PUBMED:1907869 ORIGINATES FROM NICOTIANA
RP TABACUM.
RX PubMed=7579183; DOI=10.1007/bf00043656;
RA Yu J., Smart L.B., Jung Y.-S., Golbeck J.H., McIntosh L.;
RT "Absence of PsaC subunit allows assembly of photosystem I core but prevents
RT the binding of PsaD and PsaE in Synechocystis sp. PCC6803.";
RL Plant Mol. Biol. 29:331-342(1995).
RN [5]
RP PROTEIN SEQUENCE OF 2-29.
RC STRAIN=cv. Bright Yellow 4;
RX PubMed=8278548; DOI=10.1104/pp.102.4.1259;
RA Obokata J., Mikami K., Hayashida N., Nakamura M., Sugiura M.;
RT "Molecular heterogeneity of photosystem I. psaD, psaE, psaF, psaH, and psaL
RT are all present in isoforms in Nicotiana spp.";
RL Plant Physiol. 102:1259-1267(1993).
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 -!- 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 -!- CAUTION: Was originally thought to originate from Synechocystis
CC PCC6803. {ECO:0000305|PubMed:1907869}.
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DR EMBL; Z00044; CAA77433.1; -; Genomic_DNA.
DR EMBL; X05881; CAA29304.1; -; Genomic_DNA.
DR EMBL; X53842; CAA37836.1; -; Genomic_DNA.
DR PIR; S07170; S07170.
DR RefSeq; NP_054558.1; NC_001879.2.
DR AlphaFoldDB; P62094; -.
DR SMR; P62094; -.
DR GeneID; 800430; -.
DR KEGG; nta:800430; -.
DR OMA; GHMSHAV; -.
DR OrthoDB; 1535519at2759; -.
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 TIGRFAMs; TIGR03048; PS_I_psaC; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; Chloroplast; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Photosynthesis;
KW Photosystem I; Plastid; Repeat; Thylakoid; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8278548"
FT CHAIN 2..81
FT /note="Photosystem I iron-sulfur center"
FT /id="PRO_0000062006"
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"
SQ SEQUENCE 81 AA; 9038 MW; 68071DB57FC603BF CRC64;
MSHSVKIYDT CIGCTQCVRA CPTDVLEMIP WDGCKAKQIA SAPRTEDCVG CKRCESACPT
DFLSVRVYLW HETTRSMGLA Y
