PSAB_SYNY3
ID PSAB_SYNY3 Reviewed; 731 AA.
AC P29255; P73398;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A2;
DE EC=1.97.1.12;
DE AltName: Full=PsaB;
GN Name=psaB; OrderedLocusNames=slr1835;
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 2-8; 9-13; 295-300; 304-310; 449-454; 462-467 AND
RP 498-504, 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 MUTAGENESIS OF LEU-522; LEU-536 AND CYS-565.
RX PubMed=11607363; DOI=10.1073/pnas.90.3.1132;
RA Smart L.B., Warren P.V., Golbeck J.H., McIntosh L.;
RT "Mutational analysis of the structure and biogenesis of the photosystem I
RT reaction center in the cyanobacterium Synechocystis sp. PCC 6803.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:1132-1136(1993).
RN [5]
RP MUTAGENESIS OF 595-HIS-LEU-596; 600-SER--ASN-602; 609-ASN--THR-611;
RP 614-MET--TRP-616; 622-TRP-ALA-623; 627-GLN--ILE-629; 632-TYR-ASN-633 AND
RP 638-ASN-ASN-639.
RX PubMed=10383406; DOI=10.1074/jbc.274.27.19048;
RA Sun J., Xu W., Hervas M., Navarro J.A., De La Rosa M.A., Chitnis P.R.;
RT "Oxidizing side of the cyanobacterial photosystem I. Evidence for
RT interaction between the electron donor proteins and a luminal surface helix
RT of the PsaB subunit.";
RL J. Biol. Chem. 274:19048-19054(1999).
RN [6]
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;
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000305}.
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DR EMBL; X58825; CAA41630.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA17438.1; -; Genomic_DNA.
DR PIR; S18243; S18243.
DR PDB; 4KT0; X-ray; 2.80 A; B=1-731.
DR PDB; 4L6V; X-ray; 3.80 A; 2/B/b=1-731.
DR PDB; 6HQB; X-ray; 4.00 A; B=1-731.
DR PDB; 6NWA; EM; 3.48 A; B/G/b=1-731.
DR PDB; 6UZV; EM; 3.10 A; 2/B/b=1-731.
DR PDB; 7O1V; EM; 4.31 A; B=3-731.
DR PDBsum; 4KT0; -.
DR PDBsum; 4L6V; -.
DR PDBsum; 6HQB; -.
DR PDBsum; 6NWA; -.
DR PDBsum; 6UZV; -.
DR PDBsum; 7O1V; -.
DR AlphaFoldDB; P29255; -.
DR SMR; P29255; -.
DR IntAct; P29255; 3.
DR STRING; 1148.1652517; -.
DR PaxDb; P29255; -.
DR EnsemblBacteria; BAA17438; BAA17438; BAA17438.
DR KEGG; syn:slr1835; -.
DR eggNOG; COG2885; Bacteria.
DR InParanoid; P29255; -.
DR OMA; FEQWVAD; -.
DR PhylomeDB; P29255; -.
DR BioCyc; MetaCyc:PSAB-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_00482; PSI_PsaB; 1.
DR InterPro; IPR001280; PSI_PsaA/B.
DR InterPro; IPR020586; PSI_PsaA/B_CS.
DR InterPro; IPR036408; PSI_PsaA/B_sf.
DR InterPro; IPR006244; PSI_PsaB.
DR Pfam; PF00223; PsaA_PsaB; 1.
DR PIRSF; PIRSF002905; PSI_A; 1.
DR PRINTS; PR00257; PHOTSYSPSAAB.
DR SUPFAM; SSF81558; SSF81558; 1.
DR TIGRFAMs; TIGR01336; psaB; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9268309"
FT CHAIN 2..731
FT /note="Photosystem I P700 chlorophyll a apoprotein A2"
FT /id="PRO_0000088657"
FT TRANSMEM 46..69
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..158
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..199
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..291
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..351
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..393
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..437
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255"
FT TRANSMEM 514..532
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255"
FT TRANSMEM 572..593
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255"
FT TRANSMEM 640..662
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255"
FT TRANSMEM 704..724
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255"
FT BINDING 556
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT BINDING 565
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT BINDING 651
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="B1"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 659
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="B3"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 667
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="B3"
FT /evidence="ECO:0000250"
FT BINDING 668
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT MUTAGEN 522
FT /note="L->P: No protein or PSI accumulate, unable to grow
FT photoautotrophically."
FT /evidence="ECO:0000269|PubMed:11607363"
FT MUTAGEN 522
FT /note="L->V: No effect."
FT /evidence="ECO:0000269|PubMed:11607363"
FT MUTAGEN 536
FT /note="L->M: No effect."
FT /evidence="ECO:0000269|PubMed:11607363"
FT MUTAGEN 565
FT /note="C->D,H: Almost no protein accumulates. No PSI
FT activity is present, unable to grow photoautotrophically."
FT /evidence="ECO:0000269|PubMed:11607363"
FT MUTAGEN 565
FT /note="C->S: Accumulates some protein and PSI, still does
FT not grow photoautotrophically."
FT /evidence="ECO:0000269|PubMed:11607363"
FT MUTAGEN 595..596
FT /note="HL->CI: PSI less stably assembled than wild-type,
FT possible decrease in ability to accept electrons from
FT cytochrome c6. C-594 is exposed on complex surface."
FT /evidence="ECO:0000269|PubMed:10383406"
FT MUTAGEN 600..602
FT /note="SGN->RCI: No protein or PSI accumulate, unable to
FT grow photoautotrophically."
FT /evidence="ECO:0000269|PubMed:10383406"
FT MUTAGEN 609..611
FT /note="NST->KCI: No protein or PSI accumulate, unable to
FT grow photoautotrophically."
FT /evidence="ECO:0000269|PubMed:10383406"
FT MUTAGEN 614..616
FT /note="MGW->ICA: No protein or PSI accumulate, unable to
FT grow photoautotrophically."
FT /evidence="ECO:0000269|PubMed:10383406"
FT MUTAGEN 622..623
FT /note="WA->CR: Decreases PSI levels, has slow autotrophic
FT growth, unable to accept electrons in vitro from cytochrome
FT c6. C-621 is exposed on complex surface."
FT /evidence="ECO:0000269|PubMed:10383406"
FT MUTAGEN 627..629
FT /note="QLI->HCS: Decreases PSI levels but no change in
FT ability of complex to accept electrons from cytochrome c6.
FT C-627 is exposed on complex surface."
FT /evidence="ECO:0000269|PubMed:10383406"
FT MUTAGEN 632..633
FT /note="YN->CI: Greatly decreases levels of PSI, cells do
FT not grow photoautotrophically. Unable to accept electrons
FT from cytochrome c6 in vitro. C-631 is exposed on complex
FT surface."
FT /evidence="ECO:0000269|PubMed:10383406"
FT MUTAGEN 638..639
FT /note="NN->CS: PSI assembles less stably than in wild-type
FT but no change in ability of complex to accept electrons
FT from cytochrome c6. C-637 is exposed on complex surface."
FT /evidence="ECO:0000269|PubMed:10383406"
FT CONFLICT 502
FT /note="T -> I (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 537..538
FT /note="DA -> ES (in Ref. 1; CAA41630)"
FT /evidence="ECO:0000305"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 19..26
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 39..71
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 132..155
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 223..228
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 230..234
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 270..285
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 301..305
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:6UZV"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:6UZV"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 320..326
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 328..350
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:6UZV"
FT HELIX 363..394
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 398..403
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 405..411
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 413..443
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 456..463
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 464..466
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 475..477
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 482..487
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 491..499
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 503..506
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 511..536
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 547..549
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 569..600
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 604..609
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 610..612
FT /evidence="ECO:0007829|PDB:6UZV"
FT HELIX 613..619
FT /evidence="ECO:0007829|PDB:4KT0"
FT TURN 620..627
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 628..630
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 641..662
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 665..681
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 682..684
FT /evidence="ECO:0007829|PDB:4KT0"
FT STRAND 685..688
FT /evidence="ECO:0007829|PDB:6UZV"
FT STRAND 691..693
FT /evidence="ECO:0007829|PDB:4KT0"
FT HELIX 699..729
FT /evidence="ECO:0007829|PDB:4KT0"
SQ SEQUENCE 731 AA; 81292 MW; BEED6B43CC5B3DD9 CRC64;
MATKFPKFSQ DLAQDPTTRR IWYGIATAHD FETHDGMTEE NLYQKIFASH FGHIAIIFLW
TSGTLFHVAW QGNFEQWIKD PLNIRPIAHA IWDPHFGEGA VNAFTQAGAS NPVNIAYSGV
YHWFYTIGMT TNQELYSGAV FLLVLASLFL FAGWLHLQPK FRPSLAWFKN AESRLNHHLA
GLFGVSSLAW AGHLVHVAIP EARGQHVGWD NFLSTPPHPA GLMPFFTGNW GVYAADPDTA
GHIFGTSEGA GTAILTFLGG FHPQTESLWL TDIAHHHLAI AVIFIIAGHM YRTNWGIGHS
IKEILNAHKG PLTGAGHTNL YDTINNSLHF QLGLALASLG VITSLVAQHM YSLPSYAFIA
QDHTTQAALY THHQYIAGFL MVGAFAHGAI FFVRDYDPVA NKDNVLARML EHKEALISHL
SWVSLFLGFH TLGLYVHNDV VVAFGTPEKQ ILIEPVFAQW IQATSGKALY GFDVLLSNPD
SIASTTGAAW LPGWLDAINS GTNSLFLTIG PGDFLVHHAI ALGLHTTALI LIKGALDARG
SKLMPDKKDF GYSFPCDGPG RGGTCDISAW DAFYLAMFWM LNTLGWLTFY WHWKHLGVWS
GNVAQFNENS TYLMGWFRDY LWANSAQLIN GYNPYGVNNL SVWAWMFLFG HLVWATGFMF
LISWRGYWQE LIETIVWAHE RTPLANLVRW KDKPVALSIV QARLVGLAHF TVGYVLTYAA
FLIASTAGKF G
