PSAA_TRIV2
ID PSAA_TRIV2 Reviewed; 752 AA.
AC Q44550; Q3MAG4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A1;
DE EC=1.97.1.12;
DE AltName: Full=PsaA;
GN Name=psaA; OrderedLocusNames=Ava_2405;
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=8167140; DOI=10.1016/0005-2728(94)90217-8;
RA Nyhus K.J., Sonoike K., Pakrasi H.B.;
RT "Nucleotide sequences of the psaA and the psaB genes encoding the reaction
RT center proteins of photosystem I in Anabaena variabilis ATCC 29413.";
RL Biochim. Biophys. Acta 1185:247-251(1994).
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 CHARACTERIZATION, AND BLOCKAGE OF N-TERMINUS.
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).
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.
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 -!- 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:0000250};
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 -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane
CC protein.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000305}.
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DR EMBL; L26326; AAA18488.1; -; Unassigned_DNA.
DR EMBL; CP000117; ABA22022.1; -; Genomic_DNA.
DR PIR; I39615; I39615.
DR AlphaFoldDB; Q44550; -.
DR SMR; Q44550; -.
DR STRING; 240292.Ava_2405; -.
DR EnsemblBacteria; ABA22022; ABA22022; Ava_2405.
DR KEGG; ava:Ava_2405; -.
DR eggNOG; COG2885; Bacteria.
DR HOGENOM; CLU_016126_1_0_3; -.
DR OMA; TWAFFHA; -.
DR Proteomes; UP000002533; Chromosome.
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 1: Evidence at protein level;
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..752
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000088584"
FT TRANSMEM 73..96
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..182
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..222
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..312
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..372
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..414
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..458
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255"
FT TRANSMEM 533..551
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255"
FT TRANSMEM 591..612
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255"
FT TRANSMEM 666..688
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255"
FT TRANSMEM 726..746
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255"
FT BINDING 575
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 584
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 677
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:0000250"
FT BINDING 685
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:0000250"
FT BINDING 693
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /evidence="ECO:0000250"
FT BINDING 694
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
SQ SEQUENCE 752 AA; 83180 MW; D558AEF88F674E9F CRC64;
MTISPPEREE KKARVIVDKD PVPTSFEKWA QPGHFDRTLA RGPKTTTWIW NLHALAHDFD
THTSDLEDIS RKIFAAHFGH LAVVTIWLSG MIFHGAKFSN YEAWLSDPLN VRPSAQVVWP
IVGQDILNGD VGGGFHGIQI TSGLFQVWRG WGITNSFQLY CTAIGGLVLA GLFLFAGWFH
YHKRAPKLEW FQNVESMLNH HLQVLLGCGS LGWAGHLIHV SAPINKLLDA GVAVKDIPLP
HEFILNKSVL IDLFPGFAAG LTPFFTLNWG QYADFLTFKG GLNPVTGGLW LTDISHHHLA
IAVLFIIAGH QYRTNWGIGH SIKEILENHK GPFTGEGHKG LYENLTTSWH AQLATNLAFL
GSLTIIIAHH MYAMPPYPYL ATDYATQLCI FTHHIWIGGF LIVGGAAHAA IFMVRDYDPV
VNQNNVLDRV IRHRDAIISH LNWVCIFLGF HSFGLYIHND TMRALGRPQD MFSDTAIQLQ
PVFAQWVQNL HTLAPGGTAP NALEPVSYAF GGGVLAVGGK VAMMPIALGT ADFLIHHIHA
FTIHVTVLIL LKGVLFARSS RLIPDKANLG FRFPCDGPGR GGTCQVSGWD HVFLGLFWMY
NSLSIVIFHF SWKMQSDVWG TVDAAGNVSH ITGGNFAQSA ITINGWLRDF LWAQASQVIN
SYGSALSAYG LMFLGAHFVW AFSLMFLFSG RGYWQELIES IVWAHNKLKV APAIQPRALS
ITQGRAVGVA HYLLGGIATT WAFFHAHILS VG
