PSAB2_TRIV2
ID PSAB2_TRIV2 Reviewed; 742 AA.
AC Q3MA04;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A2 2 {ECO:0000255|HAMAP-Rule:MF_00482};
DE EC=1.97.1.12 {ECO:0000255|HAMAP-Rule:MF_00482};
DE AltName: Full=PsaB 2 {ECO:0000255|HAMAP-Rule:MF_00482};
GN Name=psaB2 {ECO:0000255|HAMAP-Rule:MF_00482}; OrderedLocusNames=Ava_2567;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
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_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=PSI electron transfer chain: 5 chlorophyll a, 1 chlorophyll a', 2
CC phylloquinones and 3 4Fe-4S clusters. PSI core antenna: 90 chlorophyll
CC a, 22 carotenoids, 3 phospholipids and 1 galactolipid. P700 is a
CC chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1
CC is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur
CC 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
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_00482}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_00482}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00482}.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000255|HAMAP-
CC Rule:MF_00482}.
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DR EMBL; CP000117; ABA22182.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3MA04; -.
DR SMR; Q3MA04; -.
DR STRING; 240292.Ava_2567; -.
DR EnsemblBacteria; ABA22182; ABA22182; Ava_2567.
DR KEGG; ava:Ava_2567; -.
DR eggNOG; COG2885; Bacteria.
DR HOGENOM; CLU_016126_1_0_3; -.
DR OMA; FGHVAII; -.
DR Proteomes; UP000002533; 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_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; Chromophore; Electron transport; Iron; Iron-sulfur;
KW Magnesium; Membrane; Metal-binding; Oxidoreductase; Photosynthesis;
KW Photosystem I; Thylakoid; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..742
FT /note="Photosystem I P700 chlorophyll a apoprotein A2 2"
FT /id="PRO_0000300015"
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 334..357
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 373..399
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 421..443
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 524..542
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 583..604
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 651..673
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT TRANSMEM 715..735
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT BINDING 566
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 575
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 662
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 670
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 678
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="B3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
FT BINDING 679
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00482"
SQ SEQUENCE 742 AA; 83886 MW; CB8D314C7934E1C5 CRC64;
MATKYPKFSR DLAQDPTTRR IWYAIATGND FESHDGITEE NLYQKIFATH FGHVAIIFLW
ASSLLFHVAW QGNFEQWIKD PLHIRPIAHA IWDPHFGEPA IEAFSQGGAN YPVNIAYSGV
YHWWYTIGMR TNNDLYQGSI FLLLLAALFL FAGWLHLQPK FRPSLTWFKS AEPRLNHHLA
GLFGVSSLAW AGHLIHVAIP ESRGVHVGWR NFLTTLPHPA GLTPFWMGNW GVYAENADTT
GHIFGTSQGA GTAILTFLGG FHPQTESLWL TDMAHHHLAI AVIFIIAGHM YRTNFGIGHS
IKEMLNARQF FGIRTEGQFN LPHQGLYDTY NNSLHFQLSI HLAALGTALS LVAQHMYSLP
PYAFIAKDFT TQAALYTHHQ YIAGFLMVGA FAHAGIFWVR DYDPEQNQGN VLDRVLKHKE
AIISHLSWVS LFLGFHTLGL YVHNDVVVAF GTPEKQILIE PVFAQFIQAA HGKLLYGMDT
LLSNPDSIAY TAWPNHANVW LPNWLEAINS GTNSLFLTIG PGDFLVHHAI ALGLHTTTLI
CVKGALDARG TKLMPDKKDF GFTFPCDGPG RGGTCQTSSW EQSFYLALFW MLNLLGWVTF
YWHWKHLGVW QGNVAQFNEN STYLMGWFRD YLWANSAQLI NGYNPYGTNN LSVWAWMFLF
GHLVWATGFM FLISWRGYWQ ELIETLVWAH ERTPLANLVR WKDKPVALSI VQGWLVGLAH
FTVGYILTYA AFLIASTAGK FG
