PSAB_PHYPA
ID PSAB_PHYPA Reviewed; 734 AA.
AC Q8MFA2;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
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};
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 {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; AB078009; BAC05489.1; -; Genomic_DNA.
DR EMBL; AP005672; BAC85053.1; -; Genomic_DNA.
DR RefSeq; NP_904203.1; NC_005087.1.
DR PDB; 6L35; EM; 3.23 A; B=2-734.
DR PDB; 7KSQ; EM; 2.80 A; B=3-734.
DR PDB; 7KUX; EM; 2.80 A; B=3-734.
DR PDBsum; 6L35; -.
DR PDBsum; 7KSQ; -.
DR PDBsum; 7KUX; -.
DR AlphaFoldDB; Q8MFA2; -.
DR SMR; Q8MFA2; -.
DR PRIDE; Q8MFA2; -.
DR GeneID; 2546723; -.
DR KEGG; ppp:2546723; -.
DR InParanoid; Q8MFA2; -.
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_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; 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..734
FT /note="Photosystem I P700 chlorophyll a apoprotein A2"
FT /id="PRO_0000088631"
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 273..291
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 330..353
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 369..395
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 417..439
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 517..535
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 575..596
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 643..665
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 707..727
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT BINDING 559
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 568
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 654
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 662
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 670
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="B3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT BINDING 671
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TURN 11..14
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 19..26
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:6L35"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 41..71
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:6L35"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:6L35"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 132..155
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 171..196
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:6L35"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:6L35"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 230..234
FT /evidence="ECO:0007829|PDB:6L35"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 270..288
FT /evidence="ECO:0007829|PDB:6L35"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 301..306
FT /evidence="ECO:0007829|PDB:6L35"
FT TURN 314..321
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 322..328
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 330..354
FT /evidence="ECO:0007829|PDB:6L35"
FT TURN 359..362
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 367..396
FT /evidence="ECO:0007829|PDB:6L35"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 407..413
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 415..445
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 458..466
FT /evidence="ECO:0007829|PDB:6L35"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 484..488
FT /evidence="ECO:0007829|PDB:6L35"
FT TURN 489..493
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 494..501
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 514..539
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 550..552
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 572..603
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 606..612
FT /evidence="ECO:0007829|PDB:6L35"
FT STRAND 613..616
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 617..622
FT /evidence="ECO:0007829|PDB:6L35"
FT TURN 623..625
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 626..628
FT /evidence="ECO:0007829|PDB:6L35"
FT TURN 629..631
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 632..634
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 644..665
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 668..683
FT /evidence="ECO:0007829|PDB:6L35"
FT STRAND 688..691
FT /evidence="ECO:0007829|PDB:6L35"
FT STRAND 694..696
FT /evidence="ECO:0007829|PDB:6L35"
FT HELIX 702..730
FT /evidence="ECO:0007829|PDB:6L35"
SQ SEQUENCE 734 AA; 82365 MW; C528B06F72CE5EDE CRC64;
MASRFPKFSR GLSQDPTTRR IWFGIATAHD FESHDDMTEE RLYQKIFASH FGQLAIIFLW
TSGNLFHVAW QGNFEAWGQD PLHVRPIAHA IWDPHFGQPA VEAFTRGGAS GPVNIAYSGV
YQWWYTIGLR TNQDLYGGSI FLLFVSALFL IAGWLHLQPK WKPSVSWFKN AESRLNHHLS
GLFGVSSLAW TGHLVHVAIP ESRGEHVRWN NLLTALPHPQ GLGPFFAGQW NVYAQNPDSN
SHLFGTSEGA GTAILTFLGG FHPQTQSLWL TDMAHHHLAI AVIFIIAGHM YRTNFGIGHS
MKEILEAHTP PGGRLGRGHK GLYDTINNSL HFQLGLALAS LGVITSLVAQ HMYSLPPYAF
LAQDFTTQAA LYTHHQYIAG FIMTGAFAHG AIFFIRDYNP EQNKDNVLAR MLEHKEAIIS
HLSWASLFLG FHTLGLYVHN DVMLAFGTPE KQILIEPVFA QWIQSAHGKA LYGFDVLLSS
ADSPAFNAGQ TLWLPGWLDA INNNSNSLFL TIGPGDFLVH HAIALGLHTT TLILVKGALD
ARGSKLMPDK KEFGYSFPCD GPGRGGTCDI SAWDAFYLAV FWMLNTIGWV TFYWHWKHIT
LWQGNVAQFN ESSTYLMGWL RDYLWLNSSQ LINGYNPFGM NSLSVWAWMF LFGHLVWATG
FMFLISWRGY WQELIETLAW AHERTPLANL VRWKDKPVAL SIVQARLVGL AHFSVGYIFT
YAAFLIASTS GKFG
