PSAA_SYNY3
ID PSAA_SYNY3 Reviewed; 751 AA.
AC P29254; P73397;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 154.
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=slr1834;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1932686; DOI=10.1007/bf00037136;
RA Smart L.B., McIntosh L.;
RT "Expression of photosynthesis genes in the cyanobacterium Synechocystis sp.
RT PCC 6803: psaA-psaB and psbA transcripts accumulate in dark-grown cells.";
RL Plant Mol. Biol. 17:959-971(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP PROTEIN SEQUENCE OF 28-32, AND TOPOLOGY.
RX PubMed=9268309; DOI=10.1074/jbc.272.35.21793;
RA Sun J., Xu Q., Chitnis V.P., Jin P., Chitnis P.R.;
RT "Topography of the photosystem I core proteins of the cyanobacterium
RT Synechocystis sp. PCC 6803.";
RL J. Biol. Chem. 272:21793-21802(1997).
RN [4]
RP PRESENCE OF CHLOROPHYLL A' IN PSI.
RX PubMed=12755700; DOI=10.1046/j.1432-1033.2003.03616.x;
RA Nakamura A., Akai M., Yoshida E., Taki T., Watanabe T.;
RT "Reversed-phase HPLC determination of chlorophyll a' and phylloquinone in
RT photosystem I of oxygenic photosynthetic organisms.";
RL Eur. J. Biochem. 270:2446-2458(2003).
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; 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; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000255|HAMAP-
CC Rule:MF_00458}.
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DR EMBL; X58825; CAA41629.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA17437.1; -; Genomic_DNA.
DR PIR; S18242; S18242.
DR PDB; 4KT0; X-ray; 2.80 A; A=1-751.
DR PDB; 4L6V; X-ray; 3.80 A; 1/A/a=1-751.
DR PDB; 6HQB; X-ray; 4.00 A; A=1-751.
DR PDB; 6NWA; EM; 3.48 A; A/H/a=1-751.
DR PDB; 6UZV; EM; 3.10 A; 1/A/a=1-751.
DR PDB; 7O1V; EM; 4.31 A; A=13-751.
DR PDBsum; 4KT0; -.
DR PDBsum; 4L6V; -.
DR PDBsum; 6HQB; -.
DR PDBsum; 6NWA; -.
DR PDBsum; 6UZV; -.
DR PDBsum; 7O1V; -.
DR AlphaFoldDB; P29254; -.
DR SMR; P29254; -.
DR IntAct; P29254; 8.
DR STRING; 1148.1652516; -.
DR PaxDb; P29254; -.
DR PRIDE; P29254; -.
DR EnsemblBacteria; BAA17437; BAA17437; BAA17437.
DR KEGG; syn:slr1834; -.
DR eggNOG; COG2885; Bacteria.
DR InParanoid; P29254; -.
DR OMA; TWAFFHA; -.
DR PhylomeDB; P29254; -.
DR BioCyc; MetaCyc:PSAA-MON; -.
DR BRENDA; 1.97.1.12; 6192.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030094; C:plasma membrane-derived photosystem I; IDA:UniProtKB.
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; Direct protein sequencing;
KW Electron transport; Iron; Iron-sulfur; Magnesium; Membrane; Metal-binding;
KW Oxidoreductase; Photosynthesis; Photosystem I; Reference proteome;
KW Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..751
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000088598"
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 348..371
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 387..413
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 435..457
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 532..550
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 590..611
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 665..687
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 725..745
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 574
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 583
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 676
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 684
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 692
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 693
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT CONFLICT 604
FT /note="I -> V (in Ref. 2; BAA17437)"
FT /evidence="ECO:0000305"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 25..29
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 65..96
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 100..105
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:6UZV"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 155..181
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 193..202
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 205..218
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 220..227
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:6UZV"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 246..252
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 268..273
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 290..307
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 321..326
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 334..339
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 348..372
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 377..381
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 383..414
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 425..430
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 433..463
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 481..491
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 495..497
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 519..522
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 529..554
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 565..568
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 587..616
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 619..621
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 627..631
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 635..638
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 642..648
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 650..653
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 655..658
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 666..687
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 690..706
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 712..714
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 720..750
FT /evidence="ECO:0007829|PDB:4KT0"
SQ SEQUENCE 751 AA; 82950 MW; E4B9A4B7754AA6E7 CRC64;
MTISPPEREA KAKVSVDNNP VPTSFEKWGK PGHFDRTLAR GPKTTTWIWN LHANAHDFDS
QTSDLEDVSR KIFSAHFGHL AVVFVWLSGM YFHGAKFSNY EGWLADPTHI KPSAQVVWPI
VGQGILNGDV GGGFHGIQIT SGLFYLWRAS GFTDSYQLYC TAIGGLVMAA LMLFAGWFHY
HVKAPKLEWF QNVESMMNHH LAGLLGLGSL GWAGHQIHVS MPINKLLDAG VAPKDIPLPH
EFILEPSKMA ELYPSFAQGL TPFFTLNWGV YSDFLTFKGG LNPVTGGLWL SDTAHHHLAI
AVLFIIAGHM YRTNWGIGHS MKEILEAHKG PFTGEGHKGL YEILTTSWHA QLAINLALLG
SLTIIVAQHM YAMPPYPYQA IDYATQLSLF THHMWIGGFL IVGAGAHGAI FMVRDYDPAK
NVNNLLDRML RHRDAIISHL NWVCIFLGFH SFGLYIHNDT MRALGRPQDM FSDTAIQLQP
IFAQWVQHLH TLAPGATAPN ALATASYAFG GETIAVAGKV AMMPITLGTA DFMVHHIHAF
TIHVTALILL KGVLYARSSR LVPDKANLGF RFPCDGPGRG GTCQVSGWDH VFLGLFWMYN
SLSIVIFHFS WKMQSDVWGT VSPDGSVTHV TLGNFAQSAI TINGWLRDFL WAQAANVINS
YGSALSAYGI MFLAGHFVFA FSLMFLFSGR GYWQELIESI VWAHNKLNVA PAIQPRALSI
IQGRAVGVAH YLLGGIVTTW AFFLARSLSI G
