RCEM_BLAVI
ID RCEM_BLAVI Reviewed; 324 AA.
AC P06010;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Reaction center protein M chain;
DE AltName: Full=Photosynthetic reaction center M subunit;
GN Name=pufM;
OS Blastochloris viridis (Rhodopseudomonas viridis).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Blastochloridaceae; Blastochloris.
OX NCBI_TaxID=1079;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 19567 / DSM 133 / F;
RX PubMed=15966102; DOI=10.1002/j.1460-2075.1986.tb04340.x;
RA Michel H., Weyer K.A., Gruenberg H., Dunger I., Oesterhelt D.,
RA Lottspeich F.;
RT "The 'light' and 'medium' subunits of the photosynthetic reaction centre
RT from Rhodopseudomonas viridis: isolation of the genes, nucleotide and amino
RT acid sequence.";
RL EMBO J. 5:1149-1158(1986).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
RA Deisenhofer J., Epp O., Miki K., Huber R., Michel H.;
RT "Structure of the protein subunits in the photosynthetic reaction centre of
RT Rhodopseudomonas viridis at 3-A resolution.";
RL Nature 318:618-624(1985).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
RX PubMed=6392571; DOI=10.1016/s0022-2836(84)80011-x;
RA Deisenhofer J., Epp O., Miki K., Huber R., Michel H.;
RT "X-ray structure analysis of a membrane protein complex. Electron density
RT map at 3-A resolution and a model of the chromophores of the photosynthetic
RT reaction center from Rhodopseudomonas viridis.";
RL J. Mol. Biol. 180:385-398(1984).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
RC STRAIN=ATCC 19567 / DSM 133 / F;
RX PubMed=9351808; DOI=10.1016/s0969-2126(97)00285-2;
RA Lancaster C.R.D., Michel H.;
RT "The coupling of light-induced electron transfer and proton uptake as
RT derived from crystal structures of reaction centres from Rhodopseudomonas
RT viridis modified at the binding site of the secondary quinone, QB.";
RL Structure 5:1339-1359(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
RC STRAIN=ATCC 19567 / DSM 133 / F;
RX PubMed=10024457; DOI=10.1006/jmbi.1998.2532;
RA Lancaster C.R.D., Michel H.;
RT "Refined crystal structures of reaction centres from Rhodopseudomonas
RT viridis in complexes with the herbicide atrazine and two chiral atrazine
RT derivatives also lead to a new model of the bound carotenoid.";
RL J. Mol. Biol. 286:883-898(1999).
RN [6]
RP TOPOLOGY.
RX PubMed=2676514; DOI=10.1002/j.1460-2075.1989.tb08338.x;
RA Deisenhofer J., Michel H.;
RT "Nobel lecture. The photosynthetic reaction centre from the purple
RT bacterium Rhodopseudomonas viridis.";
RL EMBO J. 8:2149-2170(1989).
CC -!- FUNCTION: The reaction center is a membrane-bound complex that mediates
CC the initial photochemical event in the electron transfer process of
CC photosynthesis.
CC -!- SUBUNIT: Reaction center is composed of four bacteriochlorophylls, two
CC bacteriopheophytins, two ubiquinones, one iron, and three highly
CC hydrophobic polypeptide chains (designated L, M, and H).
CC -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
CC {ECO:0000305}.
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DR EMBL; X03915; CAA27551.1; -; Genomic_DNA.
DR PIR; B25102; B25102.
DR RefSeq; WP_055036367.1; NZ_LN907867.1.
DR PDB; 1DXR; X-ray; 2.00 A; M=2-324.
DR PDB; 1PRC; X-ray; 2.30 A; M=2-324.
DR PDB; 1R2C; X-ray; 2.86 A; M=2-324.
DR PDB; 1VRN; X-ray; 2.20 A; M=2-324.
DR PDB; 2I5N; X-ray; 1.96 A; M=2-324.
DR PDB; 2JBL; X-ray; 2.40 A; M=2-324.
DR PDB; 2PRC; X-ray; 2.45 A; M=2-324.
DR PDB; 2WJM; X-ray; 1.95 A; M=1-324.
DR PDB; 2WJN; X-ray; 1.86 A; M=1-324.
DR PDB; 2X5U; X-ray; 3.00 A; M=1-324.
DR PDB; 2X5V; X-ray; 3.00 A; M=1-324.
DR PDB; 3D38; X-ray; 3.21 A; M=2-324.
DR PDB; 3G7F; X-ray; 2.50 A; M=2-324.
DR PDB; 3PRC; X-ray; 2.40 A; M=2-324.
DR PDB; 3T6D; X-ray; 1.95 A; M=2-324.
DR PDB; 3T6E; X-ray; 1.92 A; M=2-324.
DR PDB; 4AC5; X-ray; 8.20 A; M=1-324.
DR PDB; 4CAS; X-ray; 3.50 A; C=1-324.
DR PDB; 5M7J; X-ray; 3.50 A; C=1-324.
DR PDB; 5M7K; X-ray; 3.50 A; C=1-324.
DR PDB; 5M7L; X-ray; 3.60 A; C=1-324.
DR PDB; 5NJ4; X-ray; 2.40 A; M=2-324.
DR PDB; 5O4C; X-ray; 2.80 A; M=2-324.
DR PDB; 5O64; X-ray; 3.30 A; M=2-324.
DR PDB; 5PRC; X-ray; 2.35 A; M=2-324.
DR PDB; 6ET5; EM; 3.00 A; M=2-324.
DR PDB; 6PRC; X-ray; 2.30 A; M=2-324.
DR PDB; 6ZHW; X-ray; 2.80 A; M=2-324.
DR PDB; 6ZI4; X-ray; 2.80 A; M=2-324.
DR PDB; 6ZI5; X-ray; 2.80 A; M=2-324.
DR PDB; 6ZI6; X-ray; 2.80 A; M=2-324.
DR PDB; 6ZI9; X-ray; 2.80 A; M=2-324.
DR PDB; 6ZIA; X-ray; 2.80 A; M=2-324.
DR PDB; 6ZID; X-ray; 2.80 A; M=2-324.
DR PDB; 7PRC; X-ray; 2.65 A; M=2-324.
DR PDBsum; 1DXR; -.
DR PDBsum; 1PRC; -.
DR PDBsum; 1R2C; -.
DR PDBsum; 1VRN; -.
DR PDBsum; 2I5N; -.
DR PDBsum; 2JBL; -.
DR PDBsum; 2PRC; -.
DR PDBsum; 2WJM; -.
DR PDBsum; 2WJN; -.
DR PDBsum; 2X5U; -.
DR PDBsum; 2X5V; -.
DR PDBsum; 3D38; -.
DR PDBsum; 3G7F; -.
DR PDBsum; 3PRC; -.
DR PDBsum; 3T6D; -.
DR PDBsum; 3T6E; -.
DR PDBsum; 4AC5; -.
DR PDBsum; 4CAS; -.
DR PDBsum; 5M7J; -.
DR PDBsum; 5M7K; -.
DR PDBsum; 5M7L; -.
DR PDBsum; 5NJ4; -.
DR PDBsum; 5O4C; -.
DR PDBsum; 5O64; -.
DR PDBsum; 5PRC; -.
DR PDBsum; 6ET5; -.
DR PDBsum; 6PRC; -.
DR PDBsum; 6ZHW; -.
DR PDBsum; 6ZI4; -.
DR PDBsum; 6ZI5; -.
DR PDBsum; 6ZI6; -.
DR PDBsum; 6ZI9; -.
DR PDBsum; 6ZIA; -.
DR PDBsum; 6ZID; -.
DR PDBsum; 7PRC; -.
DR AlphaFoldDB; P06010; -.
DR SMR; P06010; -.
DR IntAct; P06010; 1.
DR STRING; 1079.BVIR_605; -.
DR DrugBank; DB07552; (2R)-2-{[4-chloro-6-(ethylamino)-1,3,5-triazin-2-yl]amino}-2-methylbutanenitrile.
DR DrugBank; DB07551; (2S)-2-{[4-chloro-6-(ethylamino)-1,3,5-triazin-2-yl]amino}-2-methylbutanenitrile.
DR DrugBank; DB07392; Atrazine.
DR DrugBank; DB04147; Dodecyldimethylamine N-oxide.
DR DrugBank; DB04464; N-Formylmethionine.
DR DrugBank; DB08215; Terbutryn.
DR DrugBank; DB08689; Ubiquinone Q1.
DR DrugBank; DB08690; Ubiquinone Q2.
DR OMA; IFPHLDW; -.
DR OrthoDB; 634532at2; -.
DR EvolutionaryTrace; P06010; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030077; C:plasma membrane light-harvesting complex; IEA:InterPro.
DR GO; GO:0042717; C:plasma membrane-derived chromatophore membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042314; F:bacteriochlorophyll binding; IEA:UniProtKB-KW.
DR GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR CDD; cd09291; Photo-RC_M; 1.
DR Gene3D; 1.20.85.10; -; 2.
DR InterPro; IPR036854; Photo_II_D1/D2_sf.
DR InterPro; IPR000484; Photo_RC_L/M.
DR InterPro; IPR005781; Photo_RC_M.
DR Pfam; PF00124; Photo_RC; 1.
DR PRINTS; PR00256; REACTNCENTRE.
DR SUPFAM; SSF81483; SSF81483; 1.
DR TIGRFAMs; TIGR01115; pufM; 1.
DR PROSITE; PS00244; REACTION_CENTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacteriochlorophyll; Chlorophyll; Chromophore;
KW Electron transport; Iron; Magnesium; Membrane; Metal-binding;
KW Photosynthesis; Reaction center; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..324
FT /note="Reaction center protein M chain"
FT /id="PRO_0000090420"
FT TOPO_DOM 2..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:2676514"
FT TRANSMEM 52..76
FT /note="Helical"
FT TOPO_DOM 77..110
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:2676514"
FT TRANSMEM 111..137
FT /note="Helical"
FT TOPO_DOM 138..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:2676514"
FT TRANSMEM 143..166
FT /note="Helical"
FT TOPO_DOM 167..197
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:2676514"
FT TRANSMEM 198..223
FT /note="Helical"
FT TOPO_DOM 224..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:2676514"
FT TRANSMEM 260..284
FT /note="Helical"
FT TOPO_DOM 285..324
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:2676514"
FT BINDING 181
FT /ligand="(7R,8Z)-bacteriochlorophyll b"
FT /ligand_id="ChEBI:CHEBI:30034"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT BINDING 201
FT /ligand="(7R,8Z)-bacteriochlorophyll b"
FT /ligand_id="ChEBI:CHEBI:30034"
FT /ligand_part="Mg"
FT /ligand_part_id="ChEBI:CHEBI:25107"
FT /note="axial binding residue"
FT BINDING 218
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 233
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 251
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT BINDING 265
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:2WJN"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:2WJN"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:3T6E"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:2WJN"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3T6E"
FT HELIX 54..77
FT /evidence="ECO:0007829|PDB:2WJN"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 112..138
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 144..160
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 178..191
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 199..224
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:2WJN"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 233..238
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 242..255
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 263..285
FT /evidence="ECO:0007829|PDB:2WJN"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 293..299
FT /evidence="ECO:0007829|PDB:2WJN"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:2WJN"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:3D38"
SQ SEQUENCE 324 AA; 36036 MW; 28C33C28A0CCA945 CRC64;
MADYQTIYTQ IQARGPHITV SGEWGDNDRV GKPFYSYWLG KIGDAQIGPI YLGASGIAAF
AFGSTAILII LFNMAAEVHF DPLQFFRQFF WLGLYPPKAQ YGMGIPPLHD GGWWLMAGLF
MTLSLGSWWI RVYSRARALG LGTHIAWNFA AAIFFVLCIG CIHPTLVGSW SEGVPFGIWP
HIDWLTAFSI RYGNFYYCPW HGFSIGFAYG CGLLFAAHGA TILAVARFGG DREIEQITDR
GTAVERAALF WRWTIGFNAT IESVHRWGWF FSLMVMVSAS VGILLTGTFV DNWYLWCVKH
GAAPDYPAYL PATPDPASLP GAPK
