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PSAA_PROM9
ID   PSAA_PROM9              Reviewed;         767 AA.
AC   Q318L9;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=PsaA {ECO:0000255|HAMAP-Rule:MF_00458};
GN   Name=psaA {ECO:0000255|HAMAP-Rule:MF_00458};
GN   OrderedLocusNames=PMT9312_1616;
OS   Prochlorococcus marinus (strain MIT 9312).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9312;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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/cytochrome c6-ferredoxin oxidoreductase,
CC       converting photonic excitation into a charge separation, which
CC       transfers an electron from the donor P700 chlorophyll pair to the
CC       spectroscopically characterized acceptors A0, A1, FX, FA and FB in
CC       turn. Oxidized P700 is reduced on the lumenal side of the thylakoid
CC       membrane by plastocyanin or cytochrome c6. {ECO:0000255|HAMAP-
CC       Rule:MF_00458}.
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=PSI electron transfer chain: 5 divinyl chlorophyll a, 1 divinyl
CC       chlorophyll a', 2 phylloquinones and 3 4Fe-4S clusters. PSI core
CC       antenna: 90 divinyl chlorophyll a, 22 carotenoids, 3 phospholipids and
CC       1 galactolipid. P700 is a divinyl chlorophyll a/divinyl chlorophyll a'
CC       dimer, A0 is one or more divinyl chlorophyll a, A1 is one or both
CC       phylloquinones and FX is a shared 4Fe-4S iron-sulfur center.
CC       {ECO:0000255|HAMAP-Rule:MF_00458};
CC   -!- SUBUNIT: The PsaA/B heterodimer binds the P700 divinyl chlorophyll
CC       special pair and subsequent electron acceptors. PSI consists of a core
CC       antenna complex that captures photons, and an electron transfer chain
CC       that converts photonic excitation into a charge separation. The
CC       cyanobacterial PSI reaction center is composed of one copy each of
CC       PsaA,B,C,D,E,F,I,J,K,L,M and X, and forms trimeric complexes.
CC       {ECO:0000255|HAMAP-Rule:MF_00458}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00458}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00458}.
CC   -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00458}.
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DR   EMBL; CP000111; ABB50676.1; -; Genomic_DNA.
DR   RefSeq; WP_011377158.1; NC_007577.1.
DR   AlphaFoldDB; Q318L9; -.
DR   SMR; Q318L9; -.
DR   STRING; 74546.PMT9312_1616; -.
DR   EnsemblBacteria; ABB50676; ABB50676; PMT9312_1616.
DR   KEGG; pmi:PMT9312_1616; -.
DR   eggNOG; COG2885; Bacteria.
DR   HOGENOM; CLU_016126_1_0_3; -.
DR   OMA; TWAFFHA; -.
DR   OrthoDB; 32023at2; -.
DR   Proteomes; UP000002715; Chromosome.
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:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
KW   4Fe-4S; Chlorophyll; Chromophore; Electron transport; Iron; Iron-sulfur;
KW   Magnesium; Membrane; Metal-binding; Oxidoreductase; Photosynthesis;
KW   Photosystem I; Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..767
FT                   /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT                   /id="PRO_0000294202"
FT   TRANSMEM        76..99
FT                   /note="Helical; Name=I"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        162..185
FT                   /note="Helical; Name=II"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        201..225
FT                   /note="Helical; Name=III"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        309..327
FT                   /note="Helical; Name=IV"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        368..391
FT                   /note="Helical; Name=V"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        407..433
FT                   /note="Helical; Name=VI"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        455..477
FT                   /note="Helical; Name=VII"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        558..576
FT                   /note="Helical; Name=VIII"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        616..637
FT                   /note="Helical; Name=IX"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        681..703
FT                   /note="Helical; Name=X"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        741..761
FT                   /note="Helical; Name=XI"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         600
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         609
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         692
FT                   /ligand="divinylchlorophyll a'"
FT                   /ligand_id="ChEBI:CHEBI:189420"
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         700
FT                   /ligand="divinyl chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:73095"
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         708
FT                   /ligand="divinyl chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:73095"
FT                   /ligand_label="A3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   BINDING         709
FT                   /ligand="phylloquinone"
FT                   /ligand_id="ChEBI:CHEBI:18067"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
SQ   SEQUENCE   767 AA;  84315 MW;  6107D52EC714F54F CRC64;
     MTISPPESGE KNKKVLEDPV KADPRPIDFA KLDKPGFWST KLSKGPKTTT WIWNLHADAH
     DFDVHTGDAE EATRKIFSAH FGHLAIIFIW MSAAFFHGAR FSNYTGWLAD PTNVKPGAQQ
     VWAVVGQEML NGNLGADYNG IQISSGIFHM WRAWGITNES ELMALAIGAV IMAALMLHGG
     IYHYHKAAPK LEWFQNIESM LNHHIAGLVG LGSLAWAGHC IHIGAPTAAL LDAIDAGSPL
     VINGQKIATI ADMPMPHQLC DPQIIGQIFP GLASGVGNFF SLNWFAFSDF LTFKGGLNPV
     TGSLWMTDIA HHHLAFGVIA IIGGHLYRTN YGIGSSMKEI LEAHQGDPIL FPAPKGHQGL
     FEFMAESRHA QLSVNLACLG SLSILISHHM YAMPPYPYIA TDYMTVLGLF THHMWIGALF
     IVGAGAHAGI AMVRDYDPAK HIDNVLDRIL KARDALISHL NWVCMWLGFH SFGLYIHNDT
     MRALGRPQDM FSDNAIQLQP IFAQWVQSIQ ASAVGTSILA GTPEGLPQKA LSEVFNGSLV
     EVGGKVAISP IQLGTADLMI HHIHAFQIHV TVLILLKGVL YARSSRLIPD KASLGFRFPC
     DGPGRGGTCQ VSSWDHVFLA LFWMYNCISI VIFHFSWKMQ SDVWGLTGGN FSQSAITING
     WLRDFLWAQS SQVLTSYGEA ISMYGLMFLG AHFIWAFSLM FLFSGRGYWQ ELFESIVWAH
     NKLKVAPTIQ PRALSITQGR AVGVAHFLLG GIATTWAFFH ARLFGLG
 
 
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