PSAA_NOSS1
ID PSAA_NOSS1 Reviewed; 752 AA.
AC P58576;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=alr5154;
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 [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).
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; BA000019; BAB76853.1; -; Genomic_DNA.
DR PIR; AB2450; AB2450.
DR RefSeq; WP_010999280.1; NZ_RSCN01000052.1.
DR PDB; 6JEO; EM; 3.30 A; aA/bA/cA/dA=1-752.
DR PDB; 6K61; EM; 2.37 A; A/a=1-752.
DR PDB; 6TCL; EM; 3.20 A; A/A1/A2/AA=12-751.
DR PDBsum; 6JEO; -.
DR PDBsum; 6K61; -.
DR PDBsum; 6TCL; -.
DR AlphaFoldDB; P58576; -.
DR SMR; P58576; -.
DR STRING; 103690.17134292; -.
DR EnsemblBacteria; BAB76853; BAB76853; BAB76853.
DR KEGG; ana:alr5154; -.
DR eggNOG; COG2885; Bacteria.
DR OMA; TWAFFHA; -.
DR OrthoDB; 32023at2; -.
DR Proteomes; UP000002483; 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 3D-structure; 4Fe-4S; Chlorophyll; Chromophore; Electron transport; Iron;
KW Iron-sulfur; Magnesium; Membrane; Metal-binding; Oxidoreductase;
KW Photosynthesis; Photosystem I; Reference proteome; Thylakoid;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..752
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000088583"
FT TRANSMEM 73..96
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 159..182
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 198..222
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 294..312
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 349..372
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 388..414
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 436..458
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 533..551
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 591..612
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 666..688
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 726..746
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
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:0000255|HAMAP-Rule:MF_00458"
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:0000255|HAMAP-Rule:MF_00458"
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:0000255|HAMAP-Rule:MF_00458"
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:0000255|HAMAP-Rule:MF_00458"
FT BINDING 693
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 694
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:6K61"
FT TURN 37..41
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 66..97
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 101..106
FT /evidence="ECO:0007829|PDB:6K61"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 144..150
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 156..182
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:6K61"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 207..219
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 248..253
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 255..259
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 269..274
FT /evidence="ECO:0007829|PDB:6K61"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 291..308
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 322..328
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:6K61"
FT TURN 335..340
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 341..347
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 349..373
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 384..415
FT /evidence="ECO:0007829|PDB:6K61"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 426..431
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 434..464
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 468..470
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 482..492
FT /evidence="ECO:0007829|PDB:6K61"
FT TURN 496..498
FT /evidence="ECO:0007829|PDB:6K61"
FT TURN 508..510
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 515..517
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 520..523
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 530..555
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 566..569
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 588..617
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 620..622
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 624..626
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 628..632
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 636..639
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 643..654
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 656..659
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 667..688
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 691..707
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 713..715
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 721..751
FT /evidence="ECO:0007829|PDB:6K61"
SQ SEQUENCE 752 AA; 83200 MW; 042E243BB01A55DA CRC64;
MTISPPEREE KKARVIVDKD PVPTSFEKWA QPGHFDRTLA RGPKTTTWIW NLHALAHDFD
THTSDLEDIS RKIFAAHFGH LAVVTIWLSG MIFHGAKFSN YEAWLSDPLN VRPSAQVVWP
IVGQDILNGD VGGGFHGIQI TSGLFQVWRG WGITNSFQLY CTAIGGLVLA GLFLFAGWFH
YHKRAPKLEW FQNVESMLNH HLQVLLGCGS LGWAGHLIHV SAPINKLMDA GVAVKDIPLP
HEFILNKSLL IDLFPGFAAG LTPFFTLNWG QYADFLTFKG GLNPVTGGLW MTDIAHHHLA
IAVVFIIAGH 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
