PSAA_TRIEI
ID PSAA_TRIEI Reviewed; 753 AA.
AC Q10VT7;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A1 {ECO:0000255|HAMAP-Rule:MF_00458};
DE EC=1.97.1.12 {ECO:0000255|HAMAP-Rule:MF_00458};
DE AltName: Full=PsaA {ECO:0000255|HAMAP-Rule:MF_00458};
GN Name=psaA {ECO:0000255|HAMAP-Rule:MF_00458}; OrderedLocusNames=Tery_4669;
OS Trichodesmium erythraeum (strain IMS101).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC Microcoleaceae; Trichodesmium.
OX NCBI_TaxID=203124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMS101;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Richardson P.;
RT "Complete sequence of Trichodesmium erythraeum IMS101.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: PsaA and PsaB bind P700, the primary electron donor of
CC photosystem I (PSI), as well as the electron acceptors A0, A1 and FX.
CC PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase,
CC converting photonic excitation into a charge separation, which
CC transfers an electron from the donor P700 chlorophyll pair to the
CC spectroscopically characterized acceptors A0, A1, FX, FA and FB in
CC turn. Oxidized P700 is reduced on the lumenal side of the thylakoid
CC membrane by plastocyanin or cytochrome c6. {ECO:0000255|HAMAP-
CC Rule:MF_00458}.
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_00458};
CC -!- COFACTOR:
CC Note=PSI electron transfer chain: 5 chlorophyll a, 1 chlorophyll a', 2
CC phylloquinones and 3 4Fe-4S clusters. PSI core antenna: 90 chlorophyll
CC a, 22 carotenoids, 3 phospholipids and 1 galactolipid. P700 is a
CC chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1
CC is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur
CC center. {ECO:0000255|HAMAP-Rule:MF_00458};
CC -!- SUBUNIT: The PsaA/B heterodimer binds the P700 chlorophyll special pair
CC and subsequent electron acceptors. PSI consists of a core antenna
CC complex that captures photons, and an electron transfer chain that
CC converts photonic excitation into a charge separation. The
CC cyanobacterial PSI reaction center is composed of one copy each of
CC PsaA,B,C,D,E,F,I,J,K,L,M and X, and forms trimeric complexes.
CC {ECO:0000255|HAMAP-Rule:MF_00458}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_00458}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00458}.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000255|HAMAP-
CC Rule:MF_00458}.
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; CP000393; ABG53637.1; -; Genomic_DNA.
DR RefSeq; WP_011613954.1; NC_008312.1.
DR AlphaFoldDB; Q10VT7; -.
DR SMR; Q10VT7; -.
DR STRING; 203124.Tery_4669; -.
DR EnsemblBacteria; ABG53637; ABG53637; Tery_4669.
DR KEGG; ter:Tery_4669; -.
DR eggNOG; COG2885; Bacteria.
DR HOGENOM; CLU_016126_1_0_3; -.
DR OMA; TWAFFHA; -.
DR OrthoDB; 32023at2; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.1130.10; -; 1.
DR HAMAP; MF_00458; PSI_PsaA; 1.
DR InterPro; IPR006243; PSI_PsaA.
DR InterPro; IPR001280; PSI_PsaA/B.
DR InterPro; IPR020586; PSI_PsaA/B_CS.
DR InterPro; IPR036408; PSI_PsaA/B_sf.
DR PANTHER; PTHR30128:SF61; PTHR30128:SF61; 1.
DR Pfam; PF00223; PsaA_PsaB; 1.
DR PIRSF; PIRSF002905; PSI_A; 1.
DR PRINTS; PR00257; PHOTSYSPSAAB.
DR SUPFAM; SSF81558; SSF81558; 1.
DR TIGRFAMs; TIGR01335; psaA; 1.
DR PROSITE; PS00419; PHOTOSYSTEM_I_PSAAB; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Chlorophyll; Chromophore; Electron transport; Iron; Iron-sulfur;
KW Magnesium; Membrane; Metal-binding; Oxidoreductase; Photosynthesis;
KW Photosystem I; Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..753
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000294212"
FT TRANSMEM 72..95
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 158..181
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 197..221
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 293..311
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 350..373
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 389..415
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 437..459
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 534..552
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 592..613
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 667..689
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 727..747
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 576
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 585
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 678
FT /ligand="chlorophyll a'"
FT /ligand_id="ChEBI:CHEBI:189419"
FT /ligand_label="A1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 686
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 694
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 695
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
SQ SEQUENCE 753 AA; 83321 MW; 7D7C35D2C01C4A3B CRC64;
MTISPPEREA KVRVTVDTDP VPTSFEKWGK PGHFSRSLAR GPKTTTWIWN LHADAHDFDS
HTSDLEDVSR KIFSAHFGHL AIIFVWLSGA YFHGAKFSNY EAWLADPTGI KPSAQVVWPV
LGQGILNGDM GGGFHGIQIT SGLFQLWRAS GITNEYQLYC TAIGGLVMAA LMMFAGWFHY
HKKAPKLEWF QNVESMMNHH LAGLLGLGCL SWAGHQIHVS LPINKLLDSG VAPEDIPLPH
EFLFNKSLMA ELYPSFAKGL TPFFTLNWGE YADFLTFKGG LNPVTGGLWL SDTAHHHLAL
AVLFIVAGHM YRTNWGIGHS MKEILEAHKD PLIIGGEGHK GLYEALTTSW HAQLAINLAM
LGSLSIIVAH HMYAMPPYPY IATDYPTQLS LFTHHMWIGG FLIVGAGAHG AIFMVRDYDP
AKNVNNVLDR VIRHRDAIIS HLNWVCIFLG FHSFGLYVHN DTLRALGRPQ DMFSDTGIQL
QPIFAQWVQN LHSLAPGNTA PNALASVSPI FGGDVLAVGG KVAMMPMTLG TADFMVHHIH
AFTIHVTALI LLKGVLYARN SRLIPDKSEL GFRFPCDGPG RGGTCQVSGW DHVFLGLFWM
YNSLSIVIFH FSWKMQSDVW GTVDPDGTVS HITYGNFAQS AVTINGWLRD FLWAQASNVI
TSYGSELSAY GLLFLGAHFI WAFSLMFLFS GRGYWQELIE SIVWAHNKLK VAPAIQPRAL
SITQGRAVGV AHYLLGGIVT TWAFFLARII AVG
