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PSAA_SORBI
ID   PSAA_SORBI              Reviewed;         750 AA.
AC   Q9T2L6; A1E9S4;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 105.
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};
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Qiuji No. 5;
RX   PubMed=1295594;
RA   Gong X., Yan J., Wu N., Yan L.;
RT   "Cloning and nucleotide sequence of chloroplast psaA gene from sorghum.";
RL   Chin. J. Biotechnol. 8:145-151(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623;
RX   PubMed=17534593; DOI=10.1007/s00122-007-0567-4;
RA   Saski C., Lee S.-B., Fjellheim S., Guda C., Jansen R.K., Luo H.,
RA   Tomkins J., Rognli O.A., Daniell H., Clarke J.L.;
RT   "Complete chloroplast genome sequences of Hordeum vulgare, Sorghum bicolor
RT   and Agrostis stolonifera, and comparative analyses with other grass
RT   genomes.";
RL   Theor. Appl. Genet. 115:571-590(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; EF115542; ABK79496.1; -; Genomic_DNA.
DR   PIR; JC1067; JC1067.
DR   RefSeq; YP_899407.1; NC_008602.1.
DR   AlphaFoldDB; Q9T2L6; -.
DR   SMR; Q9T2L6; -.
DR   GeneID; 4549120; -.
DR   KEGG; sbi:4549120; -.
DR   InParanoid; Q9T2L6; -.
DR   OrthoDB; 209831at2759; -.
DR   Proteomes; UP000000768; Chloroplast.
DR   ExpressionAtlas; Q9T2L6; baseline.
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; Reference proteome; Thylakoid;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..750
FT                   /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT                   /id="PRO_0000088577"
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"
SQ   SEQUENCE   750 AA;  83121 MW;  9EA64A3A4604E94E CRC64;
     MIIRPSEPEV KIAVDRDPVK TSFEEWARPG HFSRTIAKGP DTTTWIWNLH ADAHDFDSHT
     GDLEEISRKV FSAHFGQLSI IFLWLSGMYF HGARFSNYEA WLSDPTHIGP SAQVVWPIVG
     QEILNGDVGG GFRGIQITSG FFQIWRASGI TSELQLYCTA IGALIFASLM LFAGWFHYHK
     AAPKLAWFQD VESMLNHHLA GLLGLGSLSW AGHQIHVSLP INQFLDAGVD PKEIPLPHEF
     ILNRDLLAQL YPSFAEGATP FFTLNWSKYA EFLSFRGGLD PITGGLWLSD IAHHHLAIAI
     LFLIAGHMYR TNWGIGHGLK DILEAHKGPF TGQGHKGLYE ILTTSWHAQL SLNLAMLGST
     TIVVAHHMYS MPPYPYLATD YGTQLSLFTH HMWIGGFLIV GAAAHAAIFM VRDYDPTTRY
     NDLLDRVLRH RDAIISHLNW VCIFLGFHSF GLYIHNDTMS ALGRPQDMFS DTAIQLQPIF
     AQWIQNIHAG APGVTAPGAT TSTSLTWGGG ELVAVGGKVA LLPIPLGTAD FLVHHIHAFT
     IHVTVLILLK GVLFARSSRL IPDKANLGFR FPCDGPGRGG TCQVSAWDHV FLGLFWMYNS
     ISVVIFHFSW KMQSDVWGTI SDQGIVTHIT GGNFAQSSIT INGWLRDFLW AQASQVIQSY
     GSSLSAYGLF FLGAHFVWAF SLMFLFSGRG YWQELIESIV WAHNKLKVAP ATQPRALSII
     QGRAVGVTHY LLGGIATTWA FFLARIIAVG
 
 
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