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PSAB_MAIZE
ID   PSAB_MAIZE              Reviewed;         735 AA.
AC   P04967;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Photosystem I P700 chlorophyll a apoprotein A2 {ECO:0000255|HAMAP-Rule:MF_00482};
DE            EC=1.97.1.12 {ECO:0000255|HAMAP-Rule:MF_00482};
DE   AltName: Full=PSI-B {ECO:0000255|HAMAP-Rule:MF_00482};
DE   AltName: Full=PsaB {ECO:0000255|HAMAP-Rule:MF_00482};
GN   Name=psaB {ECO:0000255|HAMAP-Rule:MF_00482}; Synonyms=ps1a2;
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).
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       {ECO:0000255|HAMAP-Rule:MF_00482}.
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_00482};
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_00482};
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_00482}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_00482}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_00482}.
CC   -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00482}.
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DR   EMBL; M11203; AAA84486.1; -; Genomic_DNA.
DR   EMBL; X86563; CAA60285.1; -; Genomic_DNA.
DR   PIR; S58551; S58551.
DR   RefSeq; NP_043024.1; NC_001666.2.
DR   AlphaFoldDB; P04967; -.
DR   SMR; P04967; -.
DR   PRIDE; P04967; -.
DR   GeneID; 845196; -.
DR   KEGG; zma:845196; -.
DR   MaizeGDB; 57312; -.
DR   OrthoDB; 209831at2759; -.
DR   Proteomes; UP000007305; Chloroplast.
DR   ExpressionAtlas; P04967; 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_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   3: Inferred from homology;
KW   4Fe-4S; Chlorophyll; Chloroplast; Chromophore; Electron transport; Iron;
KW   Iron-sulfur; Magnesium; Membrane; Metal-binding; Oxidoreductase;
KW   Photosynthesis; Photosystem I; Plastid; Reference proteome; Thylakoid;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..735
FT                   /note="Photosystem I P700 chlorophyll a apoprotein A2"
FT                   /id="PRO_0000088620"
FT   TRANSMEM        46..69
FT                   /note="Helical; Name=I"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   TRANSMEM        135..158
FT                   /note="Helical; Name=II"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   TRANSMEM        175..199
FT                   /note="Helical; Name=III"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   TRANSMEM        274..292
FT                   /note="Helical; Name=IV"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   TRANSMEM        331..354
FT                   /note="Helical; Name=V"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   TRANSMEM        370..396
FT                   /note="Helical; Name=VI"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   TRANSMEM        418..440
FT                   /note="Helical; Name=VII"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   TRANSMEM        518..536
FT                   /note="Helical; Name=VIII"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   TRANSMEM        576..597
FT                   /note="Helical; Name=IX"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   TRANSMEM        644..666
FT                   /note="Helical; Name=X"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   TRANSMEM        708..728
FT                   /note="Helical; Name=XI"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   BINDING         560
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_00482"
FT   BINDING         569
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_00482"
FT   BINDING         655
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:0000255|HAMAP-Rule:MF_00482"
FT   BINDING         663
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:0000255|HAMAP-Rule:MF_00482"
FT   BINDING         671
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="B3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT   BINDING         672
FT                   /ligand="phylloquinone"
FT                   /ligand_id="ChEBI:CHEBI:18067"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
SQ   SEQUENCE   735 AA;  82657 MW;  22D3CB5B1891D5CE CRC64;
     MELRFPRFSQ GLAQDPTTRR IWFGIATAHD FESHDDITEE RLYQNIFASH FGQLAIIFLW
     TSGNLFHVAW QGNFESWIQD PLHVRPIAHA IWDPHFGQPA VEAFTRGGAA GPVNIAYSGV
     YQWWYTIGLR TNEDLYTGAL FLLFLSTLSL IGGWLHLQPK WKPSLSWFKN AESRLNHHLS
     GLFGVSSLAW TGHLVHVAIP GSSRGEYVRW NNFLDVLPYP QGLGPLLTGQ WNLYAQNPDS
     SNHLFGTTQG AGTAILTLLG GFHPQTQSLW LTDIAHHHLA IAFIFLIAGH MYRTNFGIGH
     SIKDLLEAHT PPGGRLGRGH KGLYDTINNS IHFQLGLALA SLGVITSLVA QHMYSLPAYA
     FIAQDFTTQA ALYTHHQYIA GFIMTGAFAH GAIFFIRDYN PEQNEDNVLA RMLDHKEAII
     SHLSWASLFL GFHTLGPYVH NDVMLAFGTP EKQILIEPIF AQWIQSAHGK TTYGFDILLS
     STNGPTFNAG RNIWLPGWLN AVNENSNSLF LTIGPGDFLV HHAIALGLHT TTLILVKGAL
     DARGSKLMPD KKDFGYSFPC DGPGRGGTCD ISAWDAFYLA VFWMLNTIGW VTFYWHWKHI
     TLWQGNVSQF NESSTYLMGW LRDYLWLNSS QLINGYNPFG MNSLSVWAWM FLFGHLVWAT
     GFMFLISWRG YWQELIETLA WAHERTPLAN LIRWRDKPVA LSVVQARLVG LAHFSVGYIF
     TYAAFLIAST SGKFG
 
 
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