ID U6A4K4_9LILI Unreviewed; 81 AA.
AC U6A4K4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Photosystem I iron-sulfur center {ECO:0000256|ARBA:ARBA00013413, ECO:0000256|HAMAP-Rule:MF_01303};
DE EC=1.97.1.12 {ECO:0000256|ARBA:ARBA00013197, ECO:0000256|HAMAP-Rule:MF_01303};
DE AltName: Full=9 kDa polypeptide {ECO:0000256|ARBA:ARBA00032541, ECO:0000256|HAMAP-Rule:MF_01303};
DE AltName: Full=PSI-C {ECO:0000256|ARBA:ARBA00033423, ECO:0000256|HAMAP-Rule:MF_01303};
DE AltName: Full=Photosystem I subunit VII {ECO:0000256|ARBA:ARBA00030218, ECO:0000256|HAMAP-Rule:MF_01303};
DE AltName: Full=PsaC {ECO:0000256|ARBA:ARBA00031003, ECO:0000256|HAMAP-Rule:MF_01303};
GN Name=psaC {ECO:0000256|HAMAP-Rule:MF_01303,
GN ECO:0000313|EMBL:AHA12649.1};
OS Ravenala madagascariensis.
OG Plastid {ECO:0000313|EMBL:AHA12649.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zingiberales; Strelitziaceae;
OC Ravenala.
OX NCBI_TaxID=4664 {ECO:0000313|EMBL:AHA12649.1};
RN [1] {ECO:0000313|EMBL:AHA12649.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24280362; DOI=10.1093/aob/mct264;
RA Barrett C.F., Specht C.D., Leebens-Mack J., Stevenson D.W., Zomlefer W.B.,
RA Davis J.I.;
RT "Resolving ancient radiations: can complete plastid gene sets elucidate
RT deep relationships among the tropical gingers (Zingiberales)?";
RL Ann. Bot. 113:119-133(2014).
RN [2] {ECO:0000313|EMBL:AYP34542.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P.1395G {ECO:0000313|EMBL:AYP34542.1};
RX PubMed=30368769; DOI=.1002/ajb2.1178;
RA Givnish T.J., Zuluaga A., Spalink D., Soto Gomez M., Lam V.K.Y.,
RA Saarela J.M., Sass C., Iles W.J.D., de Sousa D.J.L., Leebens-Mack J.,
RA Chris Pires J., Zomlefer W.B., Gandolfo M.A., Davis J.I., Stevenson D.W.,
RA dePamphilis C., Specht C.D., Graham S.W., Barrett C.F., Ane C.;
RT "Monocot plastid phylogenomics, timeline, net rates of species
RT diversification, the power of multi-gene analyses, and a functional model
RT for the origin of monocots.";
RL Am. J. Bot. 105:1888-1910(2018).
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 {ECO:0000256|ARBA:ARBA00003402}.
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 Evidence={ECO:0000256|ARBA:ARBA00000994, ECO:0000256|HAMAP-
CC Rule:MF_01303};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|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:0000256|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 trimeric complexes.
CC {ECO:0000256|HAMAP-Rule:MF_01303}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC Rule:MF_01303}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01303}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01303}.
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DR EMBL; KF601568; AHA12649.1; -; Genomic_DNA.
DR EMBL; MH603437; AYP34542.1; -; Genomic_DNA.
DR RefSeq; YP_008854560.1; NC_022927.1.
DR AlphaFoldDB; U6A4K4; -.
DR SMR; U6A4K4; -.
DR GeneID; 17728155; -.
DR GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
DR GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-UniRule.
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 Gene3D; 3.30.70.20; -; 1.
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 NCBIfam; TIGR03048; PS_I_psaC; 1.
DR PANTHER; PTHR24960:SF88; PHOTOSYSTEM I IRON-SULFUR CENTER; 1.
DR PANTHER; PTHR24960; PHOTOSYSTEM I IRON-SULFUR CENTER-RELATED; 1.
DR Pfam; PF14697; Fer4_21; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01303};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW Rule:MF_01303};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01303};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01303};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01303};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01303};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01303};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531, ECO:0000256|HAMAP-
KW Rule:MF_01303};
KW Photosystem I {ECO:0000256|ARBA:ARBA00022836, ECO:0000256|HAMAP-
KW Rule:MF_01303}; Plastid {ECO:0000313|EMBL:AHA12649.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01303};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|HAMAP-Rule:MF_01303};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01303}.
FT DOMAIN 1..31
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 39..68
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 11
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|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:0000256|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:0000256|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:0000256|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:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01303"
SQ SEQUENCE 81 AA; 9054 MW; 681F7DB57FC603BF CRC64;
MSHSVKIYDT CIGCTQCVRA CPTDVLEMIP WDGCKAKQIA SAPRTEDCVG CKRCESACPT
DFLSVRVYLW HETTRSMGLS Y
//
