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PSAB_CYCTA
ID   PSAB_CYCTA              Reviewed;         734 AA.
AC   A6H5H1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 52.
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   Cycas taitungensis (Prince sago) (Cycas taiwaniana).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Cycadidae; Cycadales; Cycadaceae; Cycas.
OX   NCBI_TaxID=54799;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17383970; DOI=10.1093/molbev/msm059;
RA   Wu C.-S., Wang Y.-N., Liu S.-M., Chaw S.-M.;
RT   "Chloroplast genome (cpDNA) of Cycas taitungensis and 56 cp protein-coding
RT   genes of Gnetum parvifolium: insights into cpDNA evolution and phylogeny of
RT   extant seed plants.";
RL   Mol. Biol. Evol. 24:1366-1379(2007).
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; AP009339; BAF64937.1; -; Genomic_DNA.
DR   RefSeq; YP_001312196.1; NC_009618.1.
DR   AlphaFoldDB; A6H5H1; -.
DR   SMR; A6H5H1; -.
DR   GeneID; 5309525; -.
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; Thylakoid; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..734
FT                   /note="Photosystem I P700 chlorophyll a apoprotein A2"
FT                   /id="PRO_0000300042"
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"
SQ   SEQUENCE   734 AA;  82445 MW;  8D37C2BEA005B733 CRC64;
     MASRFPKFSQ GLAQDPTTRR IWFGIATAHD FESHDDITEE RLYQKIFASH FGQLAIIFLW
     TSGNLFHVAW QGNFEAWVRD PLHVRPIAHA IWDLHFGQPA VEAFTRGGAP GPVNIAHSGV
     YQWWYTIGLR TNEDLYTGAL FLLFLSAISL IAGRFHLQPK WKPSVSWFKN AESRLDHHLS
     GLFGVSSLAW TGHLVHVAIP ESRGEHVRWD NFLDVLPYPR GLGPLFTGQW NLYAQNPDSS
     SHLFGTSQGA GTAILTLLGG FHPQTQSLWL TDIAHHHLAI AFVFFIAGHM YRTNFGIGHS
     IKDILEAHIP PGGLLGRGHK GLYNTINNSL HFQLGLALAS LGVITSLVAQ HMYSLPAYAF
     IAQDFTTQAA LYTHHQYIAG FIMTGAFAHG AIFFIRDYNP EQNRDNVLAR MLEHKEAIIS
     HLSWASLFLG FHTLGLYVHN DVMLAFGTPE KQILIEPIFA QWIQSAHGKA LYGFDVLLSS
     TNSPAFNAGQ SIWLPGWLNA INDNSNSLFL TIGPGDFLVH HAIALGLHTT TLILVKGALD
     ARGSKLMPDK KDFGYSFPCD GPGRGGTCDI SAWDAFYLAV FWMLNTIGWV TFYWHWKHIT
     LWQGNVAQFN ESSTYLMGWL RDYLWLNSSQ LINGYNPFGM NSLSVWAWMF LFGHLVWATG
     FMFLISWRGY WQELIETLAW AHERTPLANS VRWRDKPVAL SIVQARLVGL AHFSVGYIFT
     YAAFLIASTS GKFG
 
 
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