PSAA_MAIZE
ID PSAA_MAIZE Reviewed; 751 AA.
AC P04966;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 131.
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}; Synonyms=ps1a1;
OS Zea mays (Maize).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3881431; DOI=10.1016/s0021-9258(18)89607-7;
RA Fish L.E., Kueck U., Bogorad L.;
RT "Two partially homologous adjacent light-inducible maize chloroplast genes
RT encoding polypeptides of the P700 chlorophyll a-protein complex of
RT photosystem I.";
RL J. Biol. Chem. 260:1413-1421(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=7666415; DOI=10.1006/jmbi.1995.0460;
RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.;
RT "Complete sequence of the maize chloroplast genome: gene content, hotspots
RT of divergence and fine tuning of genetic information by transcript
RT editing.";
RL J. Mol. Biol. 251:614-628(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
RC STRAIN=cv. B73N Inbred; TISSUE=Seedling leaf;
RX PubMed=1884003; DOI=10.1007/bf00040647;
RA Kangasjaervi J., McCullough A., Gengenbach B.G.;
RT "Nucleotide sequence and transcription of maize plastid genome Bam HI
RT fragment 14 containing ORF170.";
RL Plant Mol. Biol. 17:513-515(1991).
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; M11203; AAA84485.1; -; Genomic_DNA.
DR EMBL; X86563; CAA60286.2; -; Genomic_DNA.
DR EMBL; X58080; CAA41109.1; -; Genomic_DNA.
DR PIR; S14661; S14661.
DR PIR; S58552; S58552.
DR RefSeq; NP_043025.2; NC_001666.2.
DR PDB; 5ZJI; EM; 3.30 A; A=1-751.
DR PDBsum; 5ZJI; -.
DR AlphaFoldDB; P04966; -.
DR SMR; P04966; -.
DR IntAct; P04966; 1.
DR PRIDE; P04966; -.
DR GeneID; 845195; -.
DR KEGG; zma:845195; -.
DR MaizeGDB; 57301; -.
DR OrthoDB; 209831at2759; -.
DR Proteomes; UP000007305; Chloroplast.
DR ExpressionAtlas; P04966; baseline and differential.
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..751
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000088557"
FT TRANSMEM 71..94
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 157..180
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 196..220
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 292..310
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 347..370
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 386..412
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 434..456
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 TURN 24..26
FT /evidence="ECO:0007829|PDB:5ZJI"
FT TURN 29..32
FT /evidence="ECO:0007829|PDB:5ZJI"
FT TURN 34..38
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:5ZJI"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:5ZJI"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 64..95
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 99..104
FT /evidence="ECO:0007829|PDB:5ZJI"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:5ZJI"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:5ZJI"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:5ZJI"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:5ZJI"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 142..148
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 154..177
FT /evidence="ECO:0007829|PDB:5ZJI"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 192..201
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 238..242
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 245..251
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:5ZJI"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 267..272
FT /evidence="ECO:0007829|PDB:5ZJI"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 289..306
FT /evidence="ECO:0007829|PDB:5ZJI"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 320..326
FT /evidence="ECO:0007829|PDB:5ZJI"
FT TURN 330..338
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 347..370
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 382..412
FT /evidence="ECO:0007829|PDB:5ZJI"
FT TURN 417..419
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 424..430
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 432..462
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:5ZJI"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 480..490
FT /evidence="ECO:0007829|PDB:5ZJI"
FT TURN 492..496
FT /evidence="ECO:0007829|PDB:5ZJI"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:5ZJI"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:5ZJI"
FT STRAND 519..522
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 529..554
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 565..567
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 587..616
FT /evidence="ECO:0007829|PDB:5ZJI"
FT STRAND 619..621
FT /evidence="ECO:0007829|PDB:5ZJI"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 635..638
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 642..647
FT /evidence="ECO:0007829|PDB:5ZJI"
FT TURN 648..654
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 655..658
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 666..681
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 683..687
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 690..705
FT /evidence="ECO:0007829|PDB:5ZJI"
FT TURN 706..708
FT /evidence="ECO:0007829|PDB:5ZJI"
FT STRAND 712..714
FT /evidence="ECO:0007829|PDB:5ZJI"
FT HELIX 720..749
FT /evidence="ECO:0007829|PDB:5ZJI"
SQ SEQUENCE 751 AA; 83223 MW; E7EAEDFB9EE61EBC CRC64;
MIIRSSEPEV KIAVDRDPIK TSFEEWARPG HFSRTIAKGN PDTTTWIWNL HADAHDFDSH
TGDLEEISRK VFSAHFGQLS IIFLWLSGMY FHGARFSNYE AWLSDPTHIG PSAQVVWPIV
GQEILNGDVG GGFRGIQITS GFFQIWRASG ITSELQLYCT AIGALIFASL MLFAGWFHYH
KAAPKLAWFQ DVESMLNHHL AGLLGLGSLS WAGHQIHVSL PINQFLDAGV DPKEIPLPHE
FILNRDLLAQ LYPSFAEGAT PFFTLNWSKY AEFLSFRGGL DPITGGLWLS DIAHHHLAIA
ILFLIAGHMY RTNWGIGHGL KDILEAHKGP FTGQGHKGLY EILTTSWHAQ LSLNLAMLGS
TTIVVAHHMY SMPPYPYLAT DYGTQLSLFT HHMWIGGFLI VGAAAHAAIF MVRDYDPTTR
YNDLLDRVLR HRDAIISHLN WVCIFLGFHS FGLYIHNDTM SALGRPQDMF SDAAIQLQPI
FAQWIQNIHA GAPGVTAPGA TTSTSLTWGG GELVAIGGKV ALLPIPLGTA DFLVHHIHAF
TIHVTVLILL KGVLFARSSR LIPDKANLGF RFPCDGPGRG GTCQVSAWDH VFLGLFWMYN
SISVVIFHFS WKMQSDVWGT ISDQGIVTHI TGGNFAQSSI TINGWLRDFL WAQASQVIQS
YGSSLSAYGL FFLGAHFVWA FSLMFLFSGR GYWQELIESI VWAHNKLKVA PATQPRALSI
IQGRAVGVTH YLLGGIATTW AFFLARIIAV G
