PSAB1_NOSS1
ID PSAB1_NOSS1 Reviewed; 741 AA.
AC P58565;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Photosystem I P700 chlorophyll a apoprotein A2 1;
DE EC=1.97.1.12;
DE AltName: Full=PsaB 1;
GN Name=psaB1; OrderedLocusNames=alr5155;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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 (By similarity).
CC {ECO:0000250}.
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;
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:0000250};
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000305}.
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DR EMBL; BA000019; BAB76854.1; -; Genomic_DNA.
DR PIR; AC2450; AC2450.
DR RefSeq; WP_010999281.1; NZ_RSCN01000052.1.
DR PDB; 6JEO; EM; 3.30 A; aB/bB/cB/dB=1-741.
DR PDB; 6K61; EM; 2.37 A; B/b=1-741.
DR PDB; 6TCL; EM; 3.20 A; B/B1/B2/BB=3-741.
DR PDBsum; 6JEO; -.
DR PDBsum; 6K61; -.
DR PDBsum; 6TCL; -.
DR AlphaFoldDB; P58565; -.
DR SMR; P58565; -.
DR IntAct; P58565; 1.
DR MINT; P58565; -.
DR STRING; 103690.17134293; -.
DR EnsemblBacteria; BAB76854; BAB76854; BAB76854.
DR KEGG; ana:alr5155; -.
DR eggNOG; COG2885; Bacteria.
DR OMA; FEQWVAD; -.
DR OrthoDB; 36958at2; -.
DR Proteomes; UP000002483; 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 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Chlorophyll; Chromophore; Electron transport; Iron;
KW Iron-sulfur; Magnesium; Membrane; Metal-binding; Oxidoreductase;
KW Photosynthesis; Photosystem I; Reference proteome; Thylakoid;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..741
FT /note="Photosystem I P700 chlorophyll a apoprotein A2 1"
FT /id="PRO_0000088641"
FT TRANSMEM 46..69
FT /note="Helical; Name=I"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..158
FT /note="Helical; Name=II"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..199
FT /note="Helical; Name=III"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..291
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..357
FT /note="Helical; Name=V"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..399
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..443
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..542
FT /note="Helical; Name=VIII"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..603
FT /note="Helical; Name=IX"
FT /evidence="ECO:0000255"
FT TRANSMEM 650..672
FT /note="Helical; Name=X"
FT /evidence="ECO:0000255"
FT TRANSMEM 714..734
FT /note="Helical; Name=XI"
FT /evidence="ECO:0000255"
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:0000250"
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:0000250"
FT BINDING 661
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:0000250"
FT BINDING 669
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:0000250"
FT BINDING 677
FT /ligand="chlorophyll a"
FT /ligand_id="ChEBI:CHEBI:58416"
FT /ligand_label="B3"
FT /evidence="ECO:0000250"
FT BINDING 678
FT /ligand="phylloquinone"
FT /ligand_id="ChEBI:CHEBI:18067"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 19..27
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 39..71
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:6K61"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 132..155
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:6K61"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 198..202
FT /evidence="ECO:0007829|PDB:6K61"
FT TURN 209..214
FT /evidence="ECO:0007829|PDB:6K61"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:6K61"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 270..287
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 301..306
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 326..332
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 334..358
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 369..400
FT /evidence="ECO:0007829|PDB:6K61"
FT TURN 404..409
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 411..416
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 419..449
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 462..470
FT /evidence="ECO:0007829|PDB:6K61"
FT TURN 481..483
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 488..491
FT /evidence="ECO:0007829|PDB:6K61"
FT TURN 492..495
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 501..508
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 511..516
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 521..546
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 557..559
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 579..608
FT /evidence="ECO:0007829|PDB:6K61"
FT TURN 609..611
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 613..619
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 623..634
FT /evidence="ECO:0007829|PDB:6K61"
FT TURN 635..640
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 651..672
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 675..691
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 695..697
FT /evidence="ECO:0007829|PDB:6K61"
FT STRAND 701..703
FT /evidence="ECO:0007829|PDB:6K61"
FT HELIX 709..740
FT /evidence="ECO:0007829|PDB:6K61"
SQ SEQUENCE 741 AA; 83375 MW; D4FF27AA8EDCBD17 CRC64;
MATKFPKFSQ DLAQDPTTRR IWYAMAMGND FESHDGMTEE NLYQKIFATH FGHLAIIFLW
ASSLLFHVAW QGNFEQWIKD PLHVRPIAHA IWDPHFGKPA IEAFTQAGAN GPVNIAYSGV
YHWWYTIGMR TNTELYTGSV FLLLFASLFL FAGWLHLQPK FRPSLAWFKS AESRLNHHLA
GLFGVSSLAW AGHLIHVAIP ESRGQHVGWD NFLSTAPHPA GLQPFFTGNW GVYAQNPDTA
GHIFSTSQGA GTAILTFLGG FHPQTESLWL TDMAHHHLAI AVLFIVAGHM YRTNFGIGHS
IKEMMNAKTF FGKPVEGPFN MPHQGIYDTY NNSLHFQLGW HLACLGVVTS WVAQHMYSLP
SYAFIAKDYT TQAALYTHHQ YIAIFLMVGA FAHGAIFLVR DYDPEQNKGN VLERVLQHKE
AIISHLSWVS LFLGFHTLGL YVHNDVVVAF GTPEKQILIE PVFAQFIQAA HGKVLYGLDT
LLSNPDSVAY TAYPNYANVW LPGWLDAINS GTNSLFLTIG PGDFLVHHAI ALGLHTTTLI
LVKGALDARG SKLMPDKKDF GYAFPCDGPG RGGTCDISAW DSFYLSLFWA LNTVGWVTFY
WHWKHLGIWQ GNVAQFNENS TYLMGWFRDY LWANSAQLIN GYNPYGVNNL SVWAWMFLFG
HLVWATGFMF LISWRGYWQE LIETLVWAHE RTPIANLVRW KDKPVALSIV QARVVGLAHF
TVGYVLTYAA FLIASTAGKF G
