PSAA_ACAM1
ID PSAA_ACAM1 Reviewed; 753 AA.
AC B0C474;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=AM1_2457;
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC Acaryochloris.
OX NCBI_TaxID=329726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017;
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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}.
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DR EMBL; CP000828; ABW27465.1; -; Genomic_DNA.
DR RefSeq; WP_012162929.1; NC_009925.1.
DR PDB; 7COY; EM; 2.50 A; aA/bA/cA=1-753.
DR PDB; 7DWQ; EM; 3.30 A; A=1-753.
DR PDBsum; 7COY; -.
DR PDBsum; 7DWQ; -.
DR AlphaFoldDB; B0C474; -.
DR SMR; B0C474; -.
DR STRING; 329726.AM1_2457; -.
DR TCDB; 5.B.4.1.2; the plant photosystem i supercomplex (psi) family.
DR EnsemblBacteria; ABW27465; ABW27465; AM1_2457.
DR KEGG; amr:AM1_2457; -.
DR eggNOG; COG2885; Bacteria.
DR HOGENOM; CLU_016126_1_0_3; -.
DR OMA; TWAFFHA; -.
DR OrthoDB; 32023at2; -.
DR Proteomes; UP000000268; 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..753
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_1000081130"
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 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"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:7DWQ"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:7DWQ"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 66..97
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 101..106
FT /evidence="ECO:0007829|PDB:7DWQ"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:7DWQ"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:7DWQ"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 144..150
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 156..182
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:7DWQ"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 207..219
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 221..229
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 240..245
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 248..253
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:7DWQ"
FT TURN 264..267
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:7DWQ"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:7DWQ"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 291..308
FT /evidence="ECO:0007829|PDB:7DWQ"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 322..326
FT /evidence="ECO:0007829|PDB:7DWQ"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:7DWQ"
FT TURN 335..340
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 341..346
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 349..373
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 384..415
FT /evidence="ECO:0007829|PDB:7DWQ"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:7DWQ"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 426..432
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 434..464
FT /evidence="ECO:0007829|PDB:7DWQ"
FT STRAND 470..473
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 482..492
FT /evidence="ECO:0007829|PDB:7DWQ"
FT STRAND 497..502
FT /evidence="ECO:0007829|PDB:7DWQ"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:7DWQ"
FT STRAND 521..524
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 531..557
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 567..570
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 589..618
FT /evidence="ECO:0007829|PDB:7DWQ"
FT STRAND 621..623
FT /evidence="ECO:0007829|PDB:7DWQ"
FT STRAND 629..633
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 637..640
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 644..650
FT /evidence="ECO:0007829|PDB:7DWQ"
FT TURN 651..656
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 657..660
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 668..688
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 692..708
FT /evidence="ECO:0007829|PDB:7DWQ"
FT STRAND 714..716
FT /evidence="ECO:0007829|PDB:7DWQ"
FT HELIX 722..752
FT /evidence="ECO:0007829|PDB:7DWQ"
SQ SEQUENCE 753 AA; 83387 MW; CA76F8A0A6F95187 CRC64;
MTTSPGGPET KGRTAEVDIN PVSASLEVAG KPGHFNKSLS KGPQTTTWIW NLHALAHDFD
TQTNDLEEIS RKIFSAHFGH LSIIFVWISG MIFHAARFSN YYAWLADPLG NKPSAHVVWP
IVGQDILNAD VGNGFRGVQI TSGLFHILRG AGMTDPGELY SAAIGALVAA VVMMYAGYYH
YHKKAPKLEW FQNAESTMTH HLIVLLGLGN LAWTGHLIHV SLPVNKLLDS GVAPQDIPIP
HEFLFDNGFM ADLYPSFAQG LMPYFTLNWG AYSDFLTFKG GLDPTTGGLW MTDIAHHHLA
LAVMYIIAGH MYRTNWGIGH SMKEIMESHK GPFTGEGHKG LYEVLTTSWH AQLAINLATW
GSFSIIVAHH MYAMPPYPYL ATDYGTQLNL FVHHMWIGGF LIVGGAAHAA IFMVRDYDPA
VNQNNVLDRM LRHRDTIISH LNWVCIFLGF HSFGLYIHND NMRSLGRPQD MFSDTAIQLQ
PIFSQWVQNL QANVAGTIRA PLAEGASSLA WGGDPLFVGG KVAMQHVSLG TADFMIHHIH
AFQIHVTVLI LIKGVLYARS SRLIPDKANL GFRFPCDGPG RGGTCQSSGW DHIFLGLFWM
YNCISIVNFH FFWKMQSDVW GAANANGGVN YLTAGNWAQS SITINGWLRD FLWAQSVQVI
NSYGSALSAY GILFLGAHFI WAFSLMFLFS GRGYWQELIE SIVWAHSKLK IAPAIQPRAM
SITQGRAVGL GHYLLGGIVT SWSFYLARIL ALG
