PSAC_SYNY3
ID PSAC_SYNY3 Reviewed; 81 AA.
AC P32422;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 158.
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}; OrderedLocusNames=ssl0563;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1463835; DOI=10.1007/bf00027170;
RA Steinmueller K.;
RT "Identification of a second psaC gene in the cyanobacterium Synechocystis
RT sp. PCC6803.";
RL Plant Mol. Biol. 20:997-1001(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [4]
RP PROTEIN SEQUENCE OF 2-29.
RX PubMed=2105239; DOI=10.1016/0014-5793(90)80113-w;
RA Rousseau F., Lagoutte B.;
RT "Amino acid sequence of photosystem I subunit IV from the cyanobacterium
RT Synechocystis PCC 6803.";
RL FEBS Lett. 260:241-244(1990).
RN [5]
RP PROTEIN SEQUENCE OF 2-20.
RX PubMed=9298645; DOI=10.1002/elps.1150180806;
RA Sazuka T., Ohara O.;
RT "Towards a proteome project of cyanobacterium Synechocystis sp. strain
RT PCC6803: linking 130 protein spots with their respective genes.";
RL Electrophoresis 18:1252-1258(1997).
RN [6]
RP FUNCTION.
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 [7]
RP MUTAGENESIS OF CYS-14 AND CYS-51.
RX PubMed=9065476; DOI=10.1074/jbc.272.12.8032;
RA Yu J., Vassiliev I.R., Jung Y.-S., Golbeck J.H., McIntosh L.;
RT "Strains of Synechocystis sp. PCC 6803 with altered PsaC. I. Mutations
RT incorporated in the cysteine ligands of the two 4Fe-4S clusters FA and FB
RT of photosystem I.";
RL J. Biol. Chem. 272:8032-8039(1997).
RN [8]
RP MUTAGENESIS OF CYS-14 AND CYS-51.
RX PubMed=9065477; DOI=10.1074/jbc.272.12.8040;
RA Jung Y.-S., Vassiliev I.R., Yu J., McIntosh L., Golbeck J.H.;
RT "Strains of Synechocystis sp. PCC 6803 with altered PsaC. II. EPR and
RT optical spectroscopic properties of FA and FB in aspartate, serine, and
RT alanine replacements of cysteines 14 and 51.";
RL J. Biol. Chem. 272:8040-8049(1997).
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:7579183}.
CC -!- FUNCTION: Mutant proteins with a 3Fe-4S center are unable to
CC reconstitute PSI activity in vivo. {ECO:0000269|PubMed:7579183}.
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 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 -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane
CC protein; Cytoplasmic side.
CC -!- CAUTION: PubMed:1463835 originally thought that there were two genes
CC for psaC in PCC 6803. However, the first one identified did not
CC originate from PCC 6803 but from N.tabacum. The real psaC gene was
CC therefore incorrectly termed psaC2. {ECO:0000305}.
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DR EMBL; X65170; CAA46288.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA10036.1; -; Genomic_DNA.
DR PIR; S27984; S27984.
DR PDB; 4KT0; X-ray; 2.80 A; C=1-81.
DR PDB; 4L6V; X-ray; 3.80 A; 3/C/c=1-81.
DR PDB; 6HQB; X-ray; 4.00 A; C=2-81.
DR PDB; 6NWA; EM; 3.48 A; C/N/c=1-81.
DR PDB; 6UZV; EM; 3.10 A; 3/C/c=1-81.
DR PDB; 7O1V; EM; 4.31 A; C=2-81.
DR PDBsum; 4KT0; -.
DR PDBsum; 4L6V; -.
DR PDBsum; 6HQB; -.
DR PDBsum; 6NWA; -.
DR PDBsum; 6UZV; -.
DR PDBsum; 7O1V; -.
DR AlphaFoldDB; P32422; -.
DR SMR; P32422; -.
DR IntAct; P32422; 4.
DR STRING; 1148.1001414; -.
DR PaxDb; P32422; -.
DR EnsemblBacteria; BAA10036; BAA10036; BAA10036.
DR KEGG; syn:ssl0563; -.
DR eggNOG; COG1143; Bacteria.
DR InParanoid; P32422; -.
DR OMA; GHMSHAV; -.
DR PhylomeDB; P32422; -.
DR BioCyc; MetaCyc:PSAC-MON; -.
DR BRENDA; 1.97.1.12; 6192.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
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 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; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Photosynthesis;
KW Photosystem I; Reference proteome; Repeat; Thylakoid; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2105239,
FT ECO:0000269|PubMed:9298645"
FT CHAIN 2..81
FT /note="Photosystem I iron-sulfur center"
FT /id="PRO_0000062025"
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 14
FT /note="C->A: No detectable PsaC, D or E."
FT /evidence="ECO:0000269|PubMed:9065476,
FT ECO:0000269|PubMed:9065477"
FT MUTAGEN 14
FT /note="C->D,S: Considerably decreases amount of functional
FT PSI, grows mixotrophically only under very low light."
FT /evidence="ECO:0000269|PubMed:9065476,
FT ECO:0000269|PubMed:9065477"
FT MUTAGEN 14
FT /note="C->D: No detectable PsaC, D or E; when associated
FT with D-51."
FT /evidence="ECO:0000269|PubMed:9065476,
FT ECO:0000269|PubMed:9065477"
FT MUTAGEN 51
FT /note="C->A: No detectable PsaC, D or E."
FT /evidence="ECO:0000269|PubMed:9065476,
FT ECO:0000269|PubMed:9065477"
FT MUTAGEN 51
FT /note="C->D,S: Considerably decreases amount of functional
FT PSI, grows mixotrophically only under very low light."
FT /evidence="ECO:0000269|PubMed:9065476,
FT ECO:0000269|PubMed:9065477"
FT MUTAGEN 51
FT /note="C->D: No detectable PsaC, D or E; when associated
FT with D-14."
FT /evidence="ECO:0000269|PubMed:9065476,
FT ECO:0000269|PubMed:9065477"
FT CONFLICT 23
FT /note="L -> T (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 16..20
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 53..57
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 74..78
FT /evidence="ECO:0007829|PDB:4KT0"
SQ SEQUENCE 81 AA; 8828 MW; 57B7D4A330FDD485 CRC64;
MSHSVKIYDT CIGCTQCVRA CPLDVLEMVP WDGCKAAQIA SSPRTEDCVG CKRCETACPT
DFLSIRVYLG AETTRSMGLA Y
