位置:首页 > 蛋白库 > RCEH_BLAVI
RCEH_BLAVI
ID   RCEH_BLAVI              Reviewed;         258 AA.
AC   P06008;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Reaction center protein H chain;
DE   AltName: Full=Photosynthetic reaction center H subunit;
GN   Name=puhA;
OS   Blastochloris viridis (Rhodopseudomonas viridis).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Blastochloridaceae; Blastochloris.
OX   NCBI_TaxID=1079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FORMYLATION AT MET-1.
RC   STRAIN=ATCC 19567 / DSM 133 / F;
RX   PubMed=16453623; DOI=10.1002/j.1460-2075.1985.tb03835.x;
RA   Michel H., Weyer K.A., Gruenberg H., Lottspeich F.;
RT   "The `heavy' subunit of the photosynthetic reaction centre from
RT   Rhodopseudomonas viridis: isolation of the gene, nucleotide and amino acid
RT   sequence.";
RL   EMBO J. 4:1667-1672(1985).
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   -!- COFACTOR:
CC       Name=a bacteriochlorophyll; Xref=ChEBI:CHEBI:38201;
CC       Note=Binds 4 bacteriochlorophylls per trimer.;
CC   -!- COFACTOR:
CC       Name=a bacteriopheophytin; Xref=ChEBI:CHEBI:60411;
CC       Note=Binds 2 bacteriopheophytins per trimer.;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC       Note=Binds 1 Fe cation per trimer.;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 4 Mg(2+) ions per trimer.;
CC   -!- COFACTOR:
CC       Name=a menaquinone; Xref=ChEBI:CHEBI:16374;
CC       Note=Binds 1 menaquinone per trimer.;
CC   -!- COFACTOR:
CC       Name=a ubiquinone; Xref=ChEBI:CHEBI:16389;
CC       Note=Binds 1 ubiquinone per trimer.;
CC   -!- SUBUNIT: Heterotrimer composed of subunits L, M, and H.
CC   -!- SUBCELLULAR LOCATION: Cellular chromatophore membrane; Single-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the reaction center PuhA family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X02659; CAA26495.1; -; Genomic_DNA.
DR   PIR; A22841; A22841.
DR   RefSeq; WP_055036342.1; NZ_LN907867.1.
DR   PDB; 1DXR; X-ray; 2.00 A; H=1-258.
DR   PDB; 1PRC; X-ray; 2.30 A; H=1-258.
DR   PDB; 1R2C; X-ray; 2.86 A; H=1-258.
DR   PDB; 1VRN; X-ray; 2.20 A; H=1-258.
DR   PDB; 2I5N; X-ray; 1.96 A; H=1-258.
DR   PDB; 2JBL; X-ray; 2.40 A; H=1-258.
DR   PDB; 2PRC; X-ray; 2.45 A; H=1-258.
DR   PDB; 2WJM; X-ray; 1.95 A; H=1-258.
DR   PDB; 2WJN; X-ray; 1.86 A; H=1-258.
DR   PDB; 2X5U; X-ray; 3.00 A; H=1-258.
DR   PDB; 2X5V; X-ray; 3.00 A; H=1-258.
DR   PDB; 3D38; X-ray; 3.21 A; H=1-258.
DR   PDB; 3G7F; X-ray; 2.50 A; H=1-258.
DR   PDB; 3PRC; X-ray; 2.40 A; H=1-258.
DR   PDB; 3T6D; X-ray; 1.95 A; H=1-258.
DR   PDB; 3T6E; X-ray; 1.92 A; H=1-258.
DR   PDB; 4AC5; X-ray; 8.20 A; H=1-258.
DR   PDB; 4CAS; X-ray; 3.50 A; D=1-258.
DR   PDB; 5M7J; X-ray; 3.50 A; D=2-258.
DR   PDB; 5M7K; X-ray; 3.50 A; D=1-258.
DR   PDB; 5M7L; X-ray; 3.60 A; D=1-258.
DR   PDB; 5NJ4; X-ray; 2.40 A; H=1-258.
DR   PDB; 5O4C; X-ray; 2.80 A; H=1-258.
DR   PDB; 5O64; X-ray; 3.30 A; H=2-258.
DR   PDB; 5PRC; X-ray; 2.35 A; H=1-258.
DR   PDB; 6ET5; EM; 3.00 A; H=1-258.
DR   PDB; 6PRC; X-ray; 2.30 A; H=1-258.
DR   PDB; 6ZHW; X-ray; 2.80 A; H=1-258.
DR   PDB; 6ZI4; X-ray; 2.80 A; H=1-258.
DR   PDB; 6ZI5; X-ray; 2.80 A; H=1-258.
DR   PDB; 6ZI6; X-ray; 2.80 A; H=1-258.
DR   PDB; 6ZI9; X-ray; 2.80 A; H=1-258.
DR   PDB; 6ZIA; X-ray; 2.80 A; H=1-258.
DR   PDB; 6ZID; X-ray; 2.80 A; H=1-258.
DR   PDB; 7PRC; X-ray; 2.65 A; H=1-258.
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; P06008; -.
DR   SMR; P06008; -.
DR   IntAct; P06008; 1.
DR   STRING; 1079.BVIR_576; -.
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; YAFWIFF; -.
DR   OrthoDB; 1044122at2; -.
DR   EvolutionaryTrace; P06008; -.
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:0019684; P:photosynthesis, light reaction; IEA:InterPro.
DR   CDD; cd00226; PRCH; 1.
DR   Gene3D; 3.90.50.10; -; 1.
DR   Gene3D; 4.10.540.10; -; 1.
DR   InterPro; IPR014747; Bac_photo_RC_H_C.
DR   InterPro; IPR005652; Photo_RC_H.
DR   InterPro; IPR015810; Photo_RC_H_N.
DR   InterPro; IPR037097; Photo_RC_H_N_sf.
DR   InterPro; IPR027275; PRC-brl_dom.
DR   InterPro; IPR011033; PRC_barrel-like_sf.
DR   Pfam; PF05239; PRC; 1.
DR   Pfam; PF03967; PRCH; 1.
DR   SUPFAM; SSF50346; SSF50346; 1.
DR   TIGRFAMs; TIGR01150; puhA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Bacteriochlorophyll; Chlorophyll; Chromophore;
KW   Electron transport; Formylation; Membrane; Photosynthesis; Reaction center;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..258
FT                   /note="Reaction center protein H chain"
FT                   /id="PRO_0000090396"
FT   TOPO_DOM        1..11
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000269|PubMed:2676514"
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT   TOPO_DOM        31..258
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:2676514"
FT   MOD_RES         1
FT                   /note="N-formylmethionine"
FT                   /evidence="ECO:0000269|PubMed:16453623"
FT   STRAND          2..5
FT                   /evidence="ECO:0007829|PDB:2X5U"
FT   HELIX           7..9
FT                   /evidence="ECO:0007829|PDB:3T6D"
FT   HELIX           12..30
FT                   /evidence="ECO:0007829|PDB:2WJN"
FT   HELIX           32..35
FT                   /evidence="ECO:0007829|PDB:2WJN"
FT   STRAND          38..40
FT                   /evidence="ECO:0007829|PDB:2WJN"
FT   STRAND          46..48
FT                   /evidence="ECO:0007829|PDB:3T6D"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:3T6E"
FT   HELIX           56..60
FT                   /evidence="ECO:0007829|PDB:3T6E"
FT   STRAND          66..69
FT                   /evidence="ECO:0007829|PDB:2WJN"
FT   STRAND          75..79
FT                   /evidence="ECO:0007829|PDB:2WJN"
FT   STRAND          90..96
FT                   /evidence="ECO:0007829|PDB:2WJN"
FT   STRAND          101..105
FT                   /evidence="ECO:0007829|PDB:2WJN"
FT   HELIX           107..110
FT                   /evidence="ECO:0007829|PDB:2WJN"
FT   HELIX           113..115
FT                   /evidence="ECO:0007829|PDB:2WJN"
FT   STRAND          122..124
FT                   /evidence="ECO:0007829|PDB:2WJN"
FT   STRAND          130..136
FT                   /evidence="ECO:0007829|PDB:2WJN"
FT   TURN            137..139
FT                   /evidence="ECO:0007829|PDB:2WJN"
FT   STRAND          156..158
FT                   /evidence="ECO:0007829|PDB:2WJN"
FT   STRAND          160..162
FT                   /evidence="ECO:0007829|PDB:2X5V"
FT   STRAND          164..174
FT                   /evidence="ECO:0007829|PDB:2WJN"
FT   TURN            175..178
FT                   /evidence="ECO:0007829|PDB:2WJN"
FT   STRAND          179..187
FT                   /evidence="ECO:0007829|PDB:2WJN"
FT   TURN            188..191
FT                   /evidence="ECO:0007829|PDB:2WJN"
FT   STRAND          192..197
FT                   /evidence="ECO:0007829|PDB:2WJN"
FT   HELIX           198..200
FT                   /evidence="ECO:0007829|PDB:2WJN"
FT   STRAND          208..210
FT                   /evidence="ECO:0007829|PDB:1R2C"
FT   HELIX           215..220
FT                   /evidence="ECO:0007829|PDB:2WJN"
FT   STRAND          225..228
FT                   /evidence="ECO:0007829|PDB:2WJN"
FT   HELIX           232..248
FT                   /evidence="ECO:0007829|PDB:2WJN"
FT   HELIX           251..253
FT                   /evidence="ECO:0007829|PDB:2WJN"
SQ   SEQUENCE   258 AA;  28499 MW;  280D7A94093AFA87 CRC64;
     MYHGALAQHL DIAQLVWYAQ WLVIWTVVLL YLRREDRREG YPLVEPLGLV KLAPEDGQVY
     ELPYPKTFVL PHGGTVTVPR RRPETRELKL AQTDGFEGAP LQPTGNPLVD AVGPASYAER
     AEVVDATVDG KAKIVPLRVA TDFSIAEGDV DPRGLPVVAA DGVEAGTVTD LWVDRSEHYF
     RYLELSVAGS ARTALIPLGF CDVKKDKIVV TSILSEQFAN VPRLQSRDQI TLREEDKVSA
     YYAGGLLYAT PERAESLL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024