PSAC_CHLRE
ID PSAC_CHLRE Reviewed; 81 AA.
AC Q00914; B7U1K7;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
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};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=137c / CC-125;
RX PubMed=1712288; DOI=10.1002/j.1460-2075.1991.tb07733.x;
RA Takahashi Y., Goldschmidt-Clermont M., Soen S.-Y., Franzen L.-G.,
RA Rochaix J.-D.;
RT "Directed chloroplast transformation in Chlamydomonas reinhardtii:
RT insertional inactivation of the psaC gene encoding the iron sulfur protein
RT destabilizes photosystem I.";
RL EMBO J. 10:2033-2040(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8670852; DOI=10.1002/j.1460-2075.1996.tb00718.x;
RA Takahashi Y., Rahire M., Breyton C., Popot J.-L., Joliot P., Rochaix J.-D.;
RT "The chloroplast ycf7 (petL) open reading frame of Chlamydomonas
RT reinhardtii encodes a small functionally important subunit of the
RT cytochrome b6f complex.";
RL EMBO J. 15:3498-3506(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA Smith D.R., Lee R.W.;
RT "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT addressing the mutational-hazard hypothesis.";
RL BMC Evol. Biol. 9:120-120(2009).
RN [4]
RP IDENTIFICATION, AND COMPLETE PLASTID GENOME.
RX PubMed=12417694; DOI=10.1105/tpc.006155;
RA Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H.,
RA Stern D.B.;
RT "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a
RT sea of repeats.";
RL Plant Cell 14:2659-2679(2002).
RN [5]
RP MUTAGENESIS OF 52-LYS-ARG-53.
RX PubMed=8993322; DOI=10.1021/bi962244v;
RA Fischer N., Setif P., Rochaix J.-D.;
RT "Targeted mutations in the psaC gene of Chlamydomonas reinhardtii:
RT preferential reduction of FB at low temperature is not accompanied by
RT altered electron flow from photosystem I to ferredoxin.";
RL Biochemistry 36:93-102(1997).
RN [6]
RP MUTAGENESIS OF LYS-35, AND CROSS-LINKING TO FERREDOXIN.
RX PubMed=9463363; DOI=10.1093/emboj/17.4.849;
RA Fischer N., Hippler M., Setif P., Jacquot J.-P., Rochaix J.-D.;
RT "The PsaC subunit of photosystem I provides an essential lysine residue for
RT fast electron transfer to ferredoxin.";
RL EMBO J. 17:849-858(1998).
RN [7]
RP MUTAGENESIS OF ASP-9; ILE-12; 15-THR-GLN-16; GLU-46; VAL-49 AND
RP 52-LYS-ARG-53.
RC STRAIN=137c / CC-125;
RX PubMed=10438510; DOI=10.1074/jbc.274.33.23333;
RA Fischer N., Setif P., Rochaix J.-D.;
RT "Site-directed mutagenesis of the PsaC subunit of photosystem I. F(b) is
RT the cluster interacting with soluble ferredoxin.";
RL J. Biol. Chem. 274:23333-23340(1999).
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/cytochrome c6-ferredoxin oxidoreductase, converting
CC photonic excitation into a charge separation, which transfers an
CC electron from the donor P700 chlorophyll pair to the spectroscopically
CC characterized acceptors A0, A1, FX, FA and FB in turn.
CC {ECO:0000255|HAMAP-Rule:MF_01303, ECO:0000269|PubMed:1712288}.
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 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.;
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}.
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DR EMBL; X60365; CAA42917.1; -; Genomic_DNA.
DR EMBL; U43964; AAB17714.1; -; Genomic_DNA.
DR EMBL; FJ423446; ACJ50154.1; -; Genomic_DNA.
DR EMBL; BK000554; DAA00967.1; -; Genomic_DNA.
DR PIR; S16351; S16351.
DR RefSeq; NP_958423.1; NC_005353.1.
DR PDB; 6IJJ; EM; 2.89 A; C=1-81.
DR PDB; 6IJO; EM; 3.30 A; C=1-81.
DR PDB; 6JO5; EM; 2.90 A; C=1-81.
DR PDB; 6JO6; EM; 2.90 A; C=1-81.
DR PDB; 7BGI; EM; 2.54 A; C=2-81.
DR PDB; 7BLX; EM; 3.15 A; C=2-81.
DR PDB; 7D0J; EM; 3.42 A; C=2-81.
DR PDB; 7DZ7; EM; 2.84 A; C=1-81.
DR PDB; 7DZ8; EM; 3.16 A; C=1-81.
DR PDB; 7O01; EM; 17.10 A; C/c=2-81.
DR PDBsum; 6IJJ; -.
DR PDBsum; 6IJO; -.
DR PDBsum; 6JO5; -.
DR PDBsum; 6JO6; -.
DR PDBsum; 7BGI; -.
DR PDBsum; 7BLX; -.
DR PDBsum; 7D0J; -.
DR PDBsum; 7DZ7; -.
DR PDBsum; 7DZ8; -.
DR PDBsum; 7O01; -.
DR AlphaFoldDB; Q00914; -.
DR SMR; Q00914; -.
DR IntAct; Q00914; 6.
DR STRING; 3055.DAA00967; -.
DR PaxDb; Q00914; -.
DR PRIDE; Q00914; -.
DR GeneID; 2717046; -.
DR KEGG; cre:ChreCp067; -.
DR eggNOG; ENOG502S26M; Eukaryota.
DR HOGENOM; CLU_139698_8_0_1; -.
DR InParanoid; Q00914; -.
DR OrthoDB; 1535519at2759; -.
DR BioCyc; MetaCyc:CHRECP067-MON; -.
DR BRENDA; 1.97.1.12; 1318.
DR Proteomes; UP000006906; Chloroplast.
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:0015979; P:photosynthesis; IBA:GO_Central.
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 Pfam; PF12838; Fer4_7; 1.
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 3D-structure; 4Fe-4S; Chloroplast; Electron transport; Iron; Iron-sulfur;
KW Membrane; Metal-binding; Oxidoreductase; Photosynthesis; Photosystem I;
KW Plastid; Reference proteome; Repeat; Thylakoid; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..81
FT /note="Photosystem I iron-sulfur center"
FT /id="PRO_0000061974"
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 BINDING 14
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT BINDING 17
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT BINDING 48
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT BINDING 58
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT MUTAGEN 9
FT /note="D->K,N: No effect."
FT /evidence="ECO:0000269|PubMed:10438510"
FT MUTAGEN 12
FT /note="I->V: 60-fold increase in affinity of PSI for
FT ferredoxin; when associated with 15-KR-16. Unable to grow
FT photoautotrophically."
FT /evidence="ECO:0000269|PubMed:10438510"
FT MUTAGEN 15..16
FT /note="TQ->KR: 60-fold increase in affinity of PSI for
FT ferredoxin; when associated with V-12. Unable to grow
FT photoautotrophically."
FT /evidence="ECO:0000269|PubMed:10438510"
FT MUTAGEN 35
FT /note="K->D,E: Drastically decreases affinity of PSI for
FT ferredoxin, limits photoautotrophic growth at medium and
FT greater light. Decreases cross-linking of ferredoxin to
FT PSI-D and PSI-E."
FT /evidence="ECO:0000269|PubMed:9463363"
FT MUTAGEN 35
FT /note="K->T: Drastically decreases affinity of PSI for
FT ferredoxin. Decreases cross-linking of ferredoxin to PSI-D
FT and PSI-E."
FT /evidence="ECO:0000269|PubMed:9463363"
FT MUTAGEN 46
FT /note="E->K,Q: No effect."
FT /evidence="ECO:0000269|PubMed:10438510"
FT MUTAGEN 49
FT /note="V->I: Leads to partial destabilization of PSI; when
FT associated with 52-TQ-53, alters the FA center. Unable to
FT grow photoautotrophically."
FT /evidence="ECO:0000269|PubMed:10438510"
FT MUTAGEN 52..53
FT /note="KR->SA: Preferentially reduces FB, accumulates 20-
FT 30% PSI, 25% of which is damaged. Grows
FT photoautotrophically under low light."
FT /evidence="ECO:0000269|PubMed:10438510,
FT ECO:0000269|PubMed:8993322"
FT MUTAGEN 52..53
FT /note="KR->TQ: Leads to partial destabilization of PSI;
FT when associated with I-49. Alters the FA center. Unable to
FT grow photoautotrophically."
FT /evidence="ECO:0000269|PubMed:10438510,
FT ECO:0000269|PubMed:8993322"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 16..20
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:7BLX"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:7BGI"
FT HELIX 53..57
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:7BGI"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:7BGI"
FT TURN 74..78
FT /evidence="ECO:0007829|PDB:7BGI"
SQ SEQUENCE 81 AA; 8860 MW; 6EE84943D2E3E102 CRC64;
MAHIVKIYDT CIGCTQCVRA CPLDVLEMVP WDGCKASQMA SAPRTEDCVG CKRCETACPT
DFLSVRVYLG SESTRSMGLS Y
