PSAA_PHYPA
ID PSAA_PHYPA Reviewed; 750 AA.
AC Q8MFA3;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=PSI-A {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};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Protonema;
RX PubMed=12084583; DOI=10.1016/s0167-4781(02)00346-9;
RA Miyata Y., Sugiura C., Kobayashi Y., Hagiwara M., Sugita M.;
RT "Chloroplast ribosomal S14 protein transcript is edited to create a
RT translation initiation codon in the moss Physcomitrella patens.";
RL Biochim. Biophys. Acta 1576:346-349(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004;
RX PubMed=12954768; DOI=10.1093/nar/gkg726;
RA Sugiura C., Kobayashi Y., Setsuyuki A., Sugita C., Sugita M.;
RT "Complete chloroplast DNA sequence of the moss Physcomitrella patens:
RT evidence for the loss and relocation of rpoA from the chloroplast to the
RT nucleus.";
RL Nucleic Acids Res. 31:5324-5331(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-ferredoxin oxidoreductase, converting photonic
CC excitation into a charge separation, which transfers an electron from
CC the donor P700 chlorophyll pair to the spectroscopically characterized
CC acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on
CC the lumenal side of the thylakoid membrane by plastocyanin.
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=P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more
CC chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-
CC 4S iron-sulfur 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 eukaryotic
CC PSI reaction center is composed of at least 11 subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00458}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_00458}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00458}.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000255|HAMAP-
CC Rule:MF_00458}.
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DR EMBL; AB078009; BAC05488.1; -; Genomic_DNA.
DR EMBL; AP005672; BAC85052.1; -; Genomic_DNA.
DR RefSeq; NP_904202.1; NC_005087.1.
DR PDB; 6L35; EM; 3.23 A; A=9-750.
DR PDB; 7KSQ; EM; 2.80 A; A=9-750.
DR PDB; 7KUX; EM; 2.80 A; A=9-750.
DR PDBsum; 6L35; -.
DR PDBsum; 7KSQ; -.
DR PDBsum; 7KUX; -.
DR AlphaFoldDB; Q8MFA3; -.
DR SMR; Q8MFA3; -.
DR PRIDE; Q8MFA3; -.
DR GeneID; 2546733; -.
DR KEGG; ppp:2546733; -.
DR InParanoid; Q8MFA3; -.
DR OrthoDB; 209831at2759; -.
DR Proteomes; UP000006727; Chloroplast.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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: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; Chloroplast; Chromophore;
KW Electron transport; Iron; Iron-sulfur; Magnesium; Membrane; Metal-binding;
KW Oxidoreductase; Photosynthesis; Photosystem I; Plastid; Reference proteome;
KW Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..750
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000088569"
FT TRANSMEM 70..93
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 156..179
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 195..219
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 291..309
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 346..369
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 385..411
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 433..455
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 531..549
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 589..610
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 664..686
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 724..744
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 573
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 582
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 675
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 683
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 691
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="A3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 692
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:6L35"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:6L35"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 63..94
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 98..103
FT /evidence="ECO:0007829|PDB:6L35"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:6L35"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:6L35"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:6L35"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 141..148
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 154..179
FT /evidence="ECO:0007829|PDB:6L35"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 203..226
FT /evidence="ECO:0007829|PDB:6L35"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:6L35"
FT TURN 237..241
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 244..248
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 252..256
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:6L35"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:6L35"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 288..305
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:6L35"
FT TURN 330..337
FT /evidence="ECO:0007829|PDB:6L35"
FT TURN 339..343
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 347..370
FT /evidence="ECO:0007829|PDB:6L35"
FT TURN 375..379
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 381..412
FT /evidence="ECO:0007829|PDB:6L35"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 424..428
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 431..461
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:6L35"
FT STRAND 470..474
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 479..489
FT /evidence="ECO:0007829|PDB:6L35"
FT TURN 490..495
FT /evidence="ECO:0007829|PDB:6L35"
FT STRAND 505..510
FT /evidence="ECO:0007829|PDB:6L35"
FT STRAND 513..521
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 528..553
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 564..567
FT /evidence="ECO:0007829|PDB:6L35"
FT STRAND 572..574
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 586..615
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 622..624
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 634..637
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 641..646
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 649..652
FT /evidence="ECO:0007829|PDB:6L35"
FT TURN 653..658
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 665..686
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 689..705
FT /evidence="ECO:0007829|PDB:6L35"
FT STRAND 711..713
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 719..749
FT /evidence="ECO:0007829|PDB:6L35"
SQ SEQUENCE 750 AA; 83140 MW; 78A71D538ACB2755 CRC64;
MTIRSPEPEV KIMVEKDPVK TSFEKWAKPG HFSRTLAKGP NTTTWIWNLH ADAHDFDSHT
NDLEEISRKV FSAHFGQLAV IFIWLSGMYF HGARFSNYEA WLSDPTHIKP SAQVVWPIVG
QKILNGDVGG GFQGIQITSG FFQLWRASGI TSELQLYTTA IGGLIFAALM LFAGWFHYHK
AAPKLAWFQN VESMLNHHLA GLLGLGSLAW AGHQVHVSLP INRLLDAGVD PKEIPLPHEF
ILNRDLLAQL YPSFSKGLTP FFTLNWSEYS DFLTFRGGLN PVTGGLWLTD TAHHHLAIAV
LFLVAGHMYR TNFGIGHSMK EILEAHKGPF TGEGHKGLYE ILTTSWHAQL AINLAMLGSL
TIIVAHHMYA MPPYPYLATD YATQLSLFTH HMWIGGFLVV GAAAHAAIFM VRDYDPTTQY
NNLLDRVLRH RDAIISHLNW VCIFLGFHSF GLYIHNDTMS ALGRPQDMFS DTAIQLQPVF
AQWIQNTHAL APSLTAPNAT ASTSLTWGGG DLVAVGGKVA LLPIPLGTAD FLVHHIHAFT
IHVTVLILLK GVLFARSSRL IPDKANLGFR FPCDGPGRGG TCQVSAWDHV FLGLFWMYNA
ISVVIFHFSW KMQSDVWGSI SDQGVVTHIT GGNFAQSSIT INGWLRDFLW AQASQVIQSY
GSSLSAYGLL FLGAHFVWAF SLMFLFSGRG YWQELIESIV WAHNKLKVAP AIQPRALSIV
QGRAVGVAHY LLGGIATTWA FFLARIISVG
