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PSAA_CUCSA
ID   PSAA_CUCSA              Reviewed;         750 AA.
AC   Q2QD89; A5J1T4; Q4VZN3;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 72.
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}; OrderedLocusNames=CsCp034;
OS   Cucumis sativus (Cucumber).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Baekmibaekdadagi;
RX   PubMed=16362300; DOI=10.1007/s00299-005-0097-y;
RA   Kim J.-S., Jung J.D., Lee J.-A., Park H.-W., Oh K.-H., Jeong W.J.,
RA   Choi D.-W., Liu J.R., Cho K.Y.;
RT   "Complete sequence and organization of the cucumber (Cucumis sativus L. cv.
RT   Baekmibaekdadagi) chloroplast genome.";
RL   Plant Cell Rep. 25:334-340(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Borszczagowski;
RX   PubMed=17607527; DOI=10.2478/s11658-007-0029-7;
RA   Plader W.W., Yukawa Y., Sugiura M., Malepszy S.;
RT   "The complete structure of the cucumber (Cucumis sativus L.) chloroplast
RT   genome: its composition and comparative analysis.";
RL   Cell. Mol. Biol. Lett. 12:584-594(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chipper, and cv. Gy14;
RX   PubMed=17546086; DOI=10.1139/g07-003;
RA   Chung S.-M., Gordon V.S., Staub J.E.;
RT   "Sequencing cucumber (Cucumis sativus L.) chloroplast genomes identifies
RT   differences between chilling-tolerant and -susceptible cucumber lines.";
RL   Genome 50:215-225(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   -!- 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; AJ970307; CAJ00758.1; -; Genomic_DNA.
DR   EMBL; DQ119058; AAZ94651.1; -; Genomic_DNA.
DR   EMBL; DQ865975; ABI97417.1; -; Genomic_DNA.
DR   EMBL; DQ865976; ABI98746.1; -; Genomic_DNA.
DR   RefSeq; YP_247599.1; NC_007144.1.
DR   AlphaFoldDB; Q2QD89; -.
DR   SMR; Q2QD89; -.
DR   STRING; 3659.XP_004153784.1; -.
DR   GeneID; 3429270; -.
DR   KEGG; csv:3429270; -.
DR   eggNOG; ENOG502QRYE; Eukaryota.
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   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..750
FT                   /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT                   /id="PRO_0000275940"
FT   TRANSMEM        70..93
FT                   /note="Helical; Name=I"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        156..179
FT                   /note="Helical; Name=II"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        195..219
FT                   /note="Helical; Name=III"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        291..309
FT                   /note="Helical; Name=IV"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        346..369
FT                   /note="Helical; Name=V"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        385..411
FT                   /note="Helical; Name=VI"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        433..455
FT                   /note="Helical; Name=VII"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        531..549
FT                   /note="Helical; Name=VIII"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        589..610
FT                   /note="Helical; Name=IX"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        664..686
FT                   /note="Helical; Name=X"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   TRANSMEM        724..744
FT                   /note="Helical; Name=XI"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   BINDING         573
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         582
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         675
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         683
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         691
FT                   /ligand="chlorophyll a"
FT                   /ligand_id="ChEBI:CHEBI:58416"
FT                   /ligand_label="A3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   BINDING         692
FT                   /ligand="phylloquinone"
FT                   /ligand_id="ChEBI:CHEBI:18067"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT   CONFLICT        479..485
FT                   /note="VFAQWIQ -> RLCSMDT (in Ref. 2; CAJ00758)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        610
FT                   /note="W -> R (in Ref. 2; CAJ00758)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        626
FT                   /note="V -> L (in Ref. 2; CAJ00758)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   750 AA;  83246 MW;  A2CBC67E3DB642CC CRC64;
     MIIRSPEPEV KILVDRDPIK TSFEDWARPG HFSRTIAKGP DTTTWIWNLH ADAHDFDSHT
     SDLEEISRKV FSAHFGQLSI IFLWLSGMYF HGARFSNYEA WLGDPTHIGP SAQVVWPIVG
     QEILNGDVGG GFRGIQITSG FFQMWRASGI TNELQLYCTA IGALVFAALM LFAGWFHYHK
     AAPKLAWFQD VESMLNHHLA GLLGLGSLSW AGHQVHVSLP INQFLNAGVD PKEIPLPHEF
     ILNRDLLAQL YPSFAEGATP FFTLNWSKYA EFLTFRGGLD PVTGGLWLTD IAHHHLAIAI
     LFLIAGHMYR TNWGIGHGIK DILEAHKGPF TGQGHKGLYE ILTTSWHAQL SINLAMLGSL
     TIIVAHHMYA MPPYPYLATD YGTQLSLFTH HMWIGGFLIV GAAAHAAIFM VRDYDPTTRY
     NDLLDRVLRH RDAIISHLNW VCIFLGFHSF GLYIHNDTMS ALGRPQDMFS DTAIQLQPVF
     AQWIQNTHAL APRITAPGAT TGTSLTWGGG DLVAVGGKVA LLPIPLGTAD FLVHHIHAFT
     IHVTVLILLK GVLFSRSSRL IPDKANLGFR FPCDGPGRGG TCQVSAWDHV FLGLFWMYNS
     ISVVIFHFSW KMQSDVWGSV SDQGVVTHIT GGNFAQSSIT INGWLRDFLW AQASQVIQSY
     GSSLSAYGLF FLGAHFVWAF SLMFLFSGRG YWQELIESIV WAHNKLKVAP ATQPRALSIV
     QGRAVGVTHY LLGGIATTWA FFLARIIAVG
 
 
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