PSAC_NOSS1
ID PSAC_NOSS1 Reviewed; 81 AA.
AC P0A410; P23392; P31086;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 108.
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=asr3463;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1558954; DOI=10.1007/bf00020024;
RA Mulligan M.E., Jackman D.M.;
RT "Nucleotide sequence and expression of the gene for the 9 kDa FA/FB
RT component of photosystem I from the cyanobacterium Anabaena sp. PCC7120.";
RL Plant Mol. Biol. 18:803-808(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [3]
RP PROTEIN SEQUENCE OF 2-16, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=24550276; DOI=10.1073/pnas.1320599111;
RA Watanabe M., Semchonok D.A., Webber-Birungi M.T., Ehira S., Kondo K.,
RA Narikawa R., Ohmori M., Boekema E.J., Ikeuchi M.;
RT "Attachment of phycobilisomes in an antenna-photosystem I supercomplex of
RT cyanobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:2512-2517(2014).
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}.
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 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 dimeric and
CC tetrameric complexes. {ECO:0000269|PubMed:24550276}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_01303, ECO:0000269|PubMed:24550276}; Peripheral membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01303}; Cytoplasmic side
CC {ECO:0000255|HAMAP-Rule:MF_01303}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X61369; CAA43645.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB75162.1; -; Genomic_DNA.
DR PIR; AH2238; AH2238.
DR PIR; S20851; FEAI1C.
DR RefSeq; WP_010997613.1; NZ_RSCN01000015.1.
DR PDB; 6JEO; EM; 3.30 A; aC/bC/cC/dC=1-81.
DR PDB; 6K61; EM; 2.37 A; C/c=1-81.
DR PDB; 6TCL; EM; 3.20 A; C/C1/C2/CC=2-81.
DR PDBsum; 6JEO; -.
DR PDBsum; 6K61; -.
DR PDBsum; 6TCL; -.
DR AlphaFoldDB; P0A410; -.
DR SMR; P0A410; -.
DR STRING; 103690.17132596; -.
DR EnsemblBacteria; BAB75162; BAB75162; BAB75162.
DR GeneID; 58726273; -.
DR KEGG; ana:asr3463; -.
DR eggNOG; COG1143; Bacteria.
DR OMA; GHMSHAV; -.
DR Proteomes; UP000002483; 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 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:24550276"
FT CHAIN 2..81
FT /note="Photosystem I iron-sulfur center"
FT /id="PRO_0000062008"
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"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 16..20
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 53..57
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:6K61"
FT TURN 74..78
FT /evidence="ECO:0007829|PDB:6K61"
SQ SEQUENCE 81 AA; 8816 MW; 52B285C39270115E CRC64;
MSHTVKIYDT CIGCTQCVRA CPTDVLEMVP WDGCKAAQVA SSPRTEDCVG CKRCETACPT
DFLSIRVYLG AETTRSMGLA Y