PSAA_PROM1
ID PSAA_PROM1 Reviewed; 768 AA.
AC A2C4V3;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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}; OrderedLocusNames=NATL1_19571;
OS Prochlorococcus marinus (strain NATL1A).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167555;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL1A;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(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/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; CP000553; ABM76513.1; -; Genomic_DNA.
DR RefSeq; WP_011824482.1; NC_008819.1.
DR AlphaFoldDB; A2C4V3; -.
DR SMR; A2C4V3; -.
DR STRING; 167555.NATL1_19571; -.
DR EnsemblBacteria; ABM76513; ABM76513; NATL1_19571.
DR KEGG; pme:NATL1_19571; -.
DR eggNOG; COG2885; Bacteria.
DR HOGENOM; CLU_016126_1_0_3; -.
DR OMA; TWAFFHA; -.
DR Proteomes; UP000002592; 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..768
FT /note="Photosystem I P700 chlorophyll a apoprotein A1"
FT /id="PRO_0000294204"
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 310..328
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 369..392
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 408..434
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 456..478
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 559..577
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 617..638
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 682..704
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT TRANSMEM 742..762
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
FT BINDING 601
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 610
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 693
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 701
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 709
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 710
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="A"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00458"
SQ SEQUENCE 768 AA; 84390 MW; 5F51B544D4E4471E CRC64;
MTISPPEKEQ KKEPVLDKPI ETDAIPVDFS KLDKPGFWSK SLAKGPKTTT WIWNLHADAH
DFDTHVGDLQ ETSRKVFSAH FGHLAVIFIW MSAAFFHGAR FSNYSGWLSD PTHVKPGAQV
VWPIVGQEML NADLGGNYHG IQITSGIFQM WRGWGITNET ELMALAIGAL LMAAIMLHGG
IYHYHKAAPK LDWFRNLESM LNHHIAGLVG LGSIAWAGHC IHIGAPTAAL MDAIDAGKPL
IIDGIPIASI ADMPLPHELC NPAIASQIFP GLAGRTVENF FTTNWWAFSD FLTFKGGLNP
VTGSLWMTDI SHHHLAFGVL AVLGGHLYRT MFGIGHSLKE ILDNHAGDPI LFPAPNGHKG
IYEFLANSWH AQLGLNLAMI GSLSIIISHH MYAMPPYPYL SIDYPTVLGL FTHHMWIGGL
FIVGAAAHAG IAMIRDYDPA VHIDNVLDRI LKARDALISH LNWACMFLGF HSFGLYIHND
VMRALGRPAD MFSDTGIQLQ PVFAQWIQNI HNSAAGSTTL AGANVNLQPG LVSEVFNGSV
SQVGGKIGIA PIPLGTADFM IHHIHAFTIH VTLLILLKGV LFARSSRLIP DKANLGFRFP
CDGPGRGGTC QVSSWDHVFL GLFWMYNGLS VVIFHFSWKM QSDVWGLTGG NFAQSSITIN
GWLRDFLWAQ SSQVLTSYGQ PISMYGLMFL GAHFVWAFSL MFLFSGRGYW QELFESIIWA
HNKLNLAPTI QPRALSITQG RAVGAAHFLL GGIATTWAFF HARLIGLG
