PSAC_HORVU
ID PSAC_HORVU Reviewed; 81 AA.
AC P69416; A1E9P1; P10794;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Photosystem I iron-sulfur center;
DE EC=1.97.1.12;
DE AltName: Full=9 kDa polypeptide;
DE AltName: Full=PSI-C;
DE AltName: Full=Photosystem I subunit VII;
DE AltName: Full=PsaC;
GN Name=psaC;
OS Hordeum vulgare (Barley).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX NCBI_TaxID=4513;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Svalofs Bonus;
RA Okkels J.S., Moeller B.L.;
RT "A barley chloroplast clone encoding psaC and part of ndhD: RNA editing of
RT the ndhD initiation codon in barley?";
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Hassan; TISSUE=Leaf;
RX PubMed=10666448; DOI=10.1093/nar/28.5.1092;
RA del Campo E.M., Sabater B., Martin M.;
RT "Transcripts of the ndhH-D operon of barley plastids: possible role of
RT unedited site III in splicing of the ndhA intron.";
RL Nucleic Acids Res. 28:1092-1098(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ning S., Chen Q., Yuan Z., Zhang L., Liu D.;
RT "Sequence variation of chloroplast psaC gene region occurred in some
RT triticeae species.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Morex;
RX PubMed=17534593; DOI=10.1007/s00122-007-0567-4;
RA Saski C., Lee S.-B., Fjellheim S., Guda C., Jansen R.K., Luo H.,
RA Tomkins J., Rognli O.A., Daniell H., Clarke J.L.;
RT "Complete chloroplast genome sequences of Hordeum vulgare, Sorghum bicolor
RT and Agrostis stolonifera, and comparative analyses with other grass
RT genomes.";
RL Theor. Appl. Genet. 115:571-590(2007).
RN [5]
RP PROTEIN SEQUENCE OF 2-81.
RX PubMed=2665764; DOI=10.1007/bf02910468;
RA Scheller H.V., Svendsen I., Moeller B.L.;
RT "Amino acid sequence of the 9-kDa iron-sulfur protein of photosystem I in
RT barley.";
RL Carlsberg Res. Commun. 54:11-15(1989).
RN [6]
RP PROTEIN SEQUENCE OF 2-30.
RX PubMed=3305512; DOI=10.1016/s0021-9258(18)45260-x;
RA Hoej P.B., Svendsen I., Scheller H.V., Moeller B.L.;
RT "Identification of a chloroplast-encoded 9-kDa polypeptide as a 2[4Fe-4S]
RT protein carrying centers A and B of photosystem I.";
RL J. Biol. Chem. 262:12676-12684(1987).
RN [7]
RP MUTAGENESIS OF 27-GLU--CYS-34.
RX PubMed=8621546; DOI=10.1074/jbc.271.15.8996;
RA Naver H., Scott M.P., Golbeck J.H., Moeller B.L., Scheller H.V.;
RT "Reconstitution of barley photosystem I with modified PSI-C allows
RT identification of domains interacting with PSI-D and PSI-A/B.";
RL J. Biol. Chem. 271:8996-9001(1996).
RN [8]
RP MUTAGENESIS OF 27-GLU--CYS-34 AND 68-TYR--TYR-81.
RC STRAIN=cv. Svalofs Bonus;
RX PubMed=9668051; DOI=10.1074/jbc.273.30.18778;
RA Naver H., Scott M.P., Golbeck J.H., Olsen C.E., Scheller H.V.;
RT "The eight-amino acid internal loop of PSI-C mediates association of low
RT molecular mass iron-sulfur proteins with the P700-FX core in photosystem
RT I.";
RL J. Biol. Chem. 273:18778-18783(1998).
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;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
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:0000250};
CC -!- SUBUNIT: The eukaryotic PSI reaction center is composed of at least 11
CC subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Stromal side
CC {ECO:0000250}.
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DR EMBL; L06607; AAA32953.1; -; Genomic_DNA.
DR EMBL; AJ011848; CAA09816.1; -; Genomic_DNA.
DR EMBL; EF137813; ABL95204.1; -; Genomic_DNA.
DR EMBL; EF115541; ABK79463.1; -; Genomic_DNA.
DR PIR; A27375; A27375.
DR PIR; A32364; A32364.
DR RefSeq; YP_874703.1; NC_008590.1.
DR AlphaFoldDB; P69416; -.
DR SMR; P69416; -.
DR GeneID; 4525168; -.
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:2665764,
FT ECO:0000269|PubMed:3305512"
FT CHAIN 2..81
FT /note="Photosystem I iron-sulfur center"
FT /id="PRO_0000061984"
FT DOMAIN 2..31
FT /note="4Fe-4S ferredoxin-type 1"
FT DOMAIN 39..68
FT /note="4Fe-4S ferredoxin-type 2"
FT BINDING 11
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 17
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MUTAGEN 27..34
FT /note="Missing: In vitro PSI-C is unstably assembled into
FT PSI cores in presence of PSI-D, and not at all in its
FT absence. In vitro PSI-C is unable to bind to PSI cores even
FT in the presence of PSI-D; when associated with 67-Y--Y-80
FT deleted."
FT /evidence="ECO:0000269|PubMed:8621546,
FT ECO:0000269|PubMed:9668051"
FT MUTAGEN 68..81
FT /note="YLGPETTRSMALSY->EMIPWDGC: Removes residues 26-33 and
FT reinserts them at the C-terminus. In vitro the atypical
FT presence of residues 26-33 re-enables the protein to
FT assemble into PSI cores even in the absence of PSI-D."
FT /evidence="ECO:0000269|PubMed:9668051"
FT MUTAGEN 68..81
FT /note="Missing: In vitro PSI-C is unable to bind to PSI
FT cores even in the presence of PSI-D; when associated with
FT 27-E--C-34."
FT /evidence="ECO:0000269|PubMed:9668051"
SQ SEQUENCE 81 AA; 8899 MW; 681F63DC8FC603BF CRC64;
MSHSVKIYDT CIGCTQCVRA CPTDVLEMIP WDGCKAKQIA SAPRTEDCVG CKRCESACPT
DFLSVRVYLG PETTRSMALS Y
