PSAC_TRIV2
ID PSAC_TRIV2 Reviewed; 81 AA.
AC P0A411; P23392; P31086; Q3M7E5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 111.
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=Ava_3484;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16668719; DOI=10.1104/pp.98.2.798;
RA Mannan R.M., Pakrasi H.B.;
RT "Molecular analysis of the psaC gene encoding the FA/FB apoprotein of
RT photosystem I in the filamentous cyanobacterium Anabaena sp. ATCC 29413.";
RL Plant Physiol. 98:798-800(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
RN [3]
RP PROTEIN SEQUENCE OF 2-39.
RX PubMed=1618755; DOI=10.1016/s0021-9258(18)42303-4;
RA Nyhus K.J., Ikeuchi M., Inoue Y., Whitmarsh J., Pakrasi H.B.;
RT "Purification and characterization of the photosystem I complex from the
RT filamentous cyanobacterium Anabaena variabilis ATCC 29413.";
RL J. Biol. Chem. 267:12489-12495(1992).
RN [4]
RP FUNCTION.
RX PubMed=7979407; DOI=10.1006/abbi.1994.1472;
RA Mannan R.M., Pakrasi H.B., Sonoike K.;
RT "The PsaC protein is necessary for the stable association of the PsaD,
RT PsaE, and PsaL proteins in the photosystem I complex: analysis of a
RT cyanobacterial mutant strain.";
RL Arch. Biochem. Biophys. 315:68-73(1994).
RN [5]
RP MUTAGENESIS OF CYS-14 AND CYS-51.
RX PubMed=8617228; DOI=10.1002/j.1460-2075.1996.tb00532.x;
RA Mannan R.M., He W.-Z., Metzger S.U., Whitmarsh J., Malkin R., Pakrasi H.B.;
RT "Active photosynthesis in cyanobacterial mutants with directed
RT modifications in the ligands for two iron-sulfur clusters on the PsaC
RT protein of photosystem I.";
RL EMBO J. 15:1826-1833(1996).
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:7979407}.
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.
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DR EMBL; X57153; CAA40443.1; -; Genomic_DNA.
DR EMBL; CP000117; ABA23091.1; -; Genomic_DNA.
DR PIR; S14475; FEAICV.
DR RefSeq; WP_010997613.1; NC_007413.1.
DR AlphaFoldDB; P0A411; -.
DR SMR; P0A411; -.
DR STRING; 240292.Ava_3484; -.
DR EnsemblBacteria; ABA23091; ABA23091; Ava_3484.
DR GeneID; 58726273; -.
DR KEGG; ava:Ava_3484; -.
DR eggNOG; COG1143; Bacteria.
DR HOGENOM; CLU_139698_8_0_3; -.
DR OMA; GHMSHAV; -.
DR Proteomes; UP000002533; 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 4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW Membrane; Metal-binding; Oxidoreductase; Photosynthesis; Photosystem I;
KW Repeat; Thylakoid; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1618755"
FT CHAIN 2..81
FT /note="Photosystem I iron-sulfur center"
FT /id="PRO_0000062009"
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->D: Loss of FB, mutant is capable of growth,
FT although with reduced rate and quantum efficiency."
FT /evidence="ECO:0000269|PubMed:8617228"
FT MUTAGEN 51
FT /note="C->D: Generates a modified FA (not 3Fe-4S), mutant
FT is capable of normal growth."
FT /evidence="ECO:0000269|PubMed:8617228"
SQ SEQUENCE 81 AA; 8816 MW; 52B285C39270115E CRC64;
MSHTVKIYDT CIGCTQCVRA CPTDVLEMVP WDGCKAAQVA SSPRTEDCVG CKRCETACPT
DFLSIRVYLG AETTRSMGLA Y
