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Protein

Reaction center protein L chain

Gene

pufL

Organism
Blastochloris viridis (Rhodopseudomonas viridis)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi154 – 1541Magnesium (bacteriochlorophyll b axial ligand)
Metal bindingi174 – 1741Magnesium (bacteriochlorophyll b axial ligand)
Metal bindingi191 – 1911Iron
Binding sitei217 – 2171Quinone B
Metal bindingi231 – 2311Iron

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Photosynthesis, Transport

Keywords - Ligandi

Bacteriochlorophyll, Chlorophyll, Chromophore, Iron, Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Reaction center protein L chain
Alternative name(s):
Photosynthetic reaction center L subunit
Gene namesi
Name:pufL
OrganismiBlastochloris viridis (Rhodopseudomonas viridis)
Taxonomic identifieri1079 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesHyphomicrobiaceaeBlastochloris

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 3231Cytoplasmic1 PublicationAdd
BLAST
Transmembranei33 – 5321HelicalAdd
BLAST
Topological domaini54 – 8330Periplasmic1 PublicationAdd
BLAST
Transmembranei84 – 11128HelicalAdd
BLAST
Topological domaini112 – 1154Cytoplasmic1 Publication
Transmembranei116 – 13924HelicalAdd
BLAST
Topological domaini140 – 17031Periplasmic1 PublicationAdd
BLAST
Transmembranei171 – 19828HelicalAdd
BLAST
Topological domaini199 – 22527Cytoplasmic1 PublicationAdd
BLAST
Transmembranei226 – 24924HelicalAdd
BLAST
Topological domaini250 – 27425Periplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Reaction center

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 274273Reaction center protein L chainPRO_0000090410Add
BLAST

Interactioni

Subunit structurei

Reaction center is composed of four bacteriochlorophylls, two bacteriopheophytins, two ubiquinones, one iron, and three highly hydrophobic polypeptide chains (designated L, M, and H).

Structurei

Secondary structure

1
274
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni5 – 73Combined sources
Helixi8 – 103Combined sources
Beta strandi17 – 193Combined sources
Helixi20 – 234Combined sources
Beta strandi25 – 273Combined sources
Helixi33 – 5523Combined sources
Turni56 – 583Combined sources
Turni62 – 643Combined sources
Helixi72 – 743Combined sources
Turni81 – 844Combined sources
Helixi85 – 11127Combined sources
Helixi117 – 13317Combined sources
Helixi135 – 1406Combined sources
Helixi143 – 1453Combined sources
Helixi153 – 16311Combined sources
Helixi168 – 1703Combined sources
Helixi172 – 19928Combined sources
Helixi210 – 22112Combined sources
Helixi229 – 25123Combined sources
Turni252 – 2543Combined sources
Helixi260 – 2634Combined sources
Helixi265 – 2684Combined sources
Helixi271 – 2733Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DXRX-ray2.00L2-274[»]
1PRCX-ray2.30L2-274[»]
1R2CX-ray2.86L2-274[»]
1VRNX-ray2.20L2-274[»]
2I5NX-ray1.96L2-274[»]
2JBLX-ray2.40L2-274[»]
2PRCX-ray2.45L2-274[»]
2WJMX-ray1.95L1-274[»]
2WJNX-ray1.86L1-274[»]
2X5UX-ray3.00L1-274[»]
2X5VX-ray3.00L1-274[»]
3D38X-ray3.21L2-274[»]
3G7FX-ray2.50L2-274[»]
3PRCX-ray2.40L2-274[»]
3T6DX-ray1.95L2-274[»]
3T6EX-ray1.92L2-274[»]
4AC5X-ray8.20L1-274[»]
4CASX-ray3.50B1-274[»]
5PRCX-ray2.35L2-274[»]
6PRCX-ray2.30L2-274[»]
7PRCX-ray2.65L2-274[»]
ProteinModelPortaliP06009.
SMRiP06009. Positions 2-274.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06009.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di1.20.85.10. 2 hits.
InterProiIPR005871. Photo_RC_L.
IPR000484. Photo_RC_L/M.
[Graphical view]
PfamiPF00124. Photo_RC. 1 hit.
[Graphical view]
PRINTSiPR00256. REACTNCENTRE.
SUPFAMiSSF81483. SSF81483. 1 hit.
TIGRFAMsiTIGR01157. pufL. 1 hit.
PROSITEiPS00244. REACTION_CENTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06009-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLSFERKY RVRGGTLIGG DLFDFWVGPY FVGFFGVSAI FFIFLGVSLI
60 70 80 90 100
GYAASQGPTW DPFAISINPP DLKYGLGAAP LLEGGFWQAI TVCALGAFIS
110 120 130 140 150
WMLREVEISR KLGIGWHVPL AFCVPIFMFC VLQVFRPLLL GSWGHAFPYG
160 170 180 190 200
ILSHLDWVNN FGYQYLNWHY NPGHMSSVSF LFVNAMALGL HGGLILSVAN
210 220 230 240 250
PGDGDKVKTA EHENQYFRDV VGYSIGALSI HRLGLFLASN IFLTGAFGTI
260 270
ASGPFWTRGW PEWWGWWLDI PFWS
Length:274
Mass (Da):30,578
Last modified:January 23, 2007 - v3
Checksum:i98E0F11A7345EC38
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03915 Genomic DNA. Translation: CAA27550.1.
PIRiA25102.
RefSeqiWP_055036366.1. NZ_LN907867.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03915 Genomic DNA. Translation: CAA27550.1.
PIRiA25102.
RefSeqiWP_055036366.1. NZ_LN907867.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DXRX-ray2.00L2-274[»]
1PRCX-ray2.30L2-274[»]
1R2CX-ray2.86L2-274[»]
1VRNX-ray2.20L2-274[»]
2I5NX-ray1.96L2-274[»]
2JBLX-ray2.40L2-274[»]
2PRCX-ray2.45L2-274[»]
2WJMX-ray1.95L1-274[»]
2WJNX-ray1.86L1-274[»]
2X5UX-ray3.00L1-274[»]
2X5VX-ray3.00L1-274[»]
3D38X-ray3.21L2-274[»]
3G7FX-ray2.50L2-274[»]
3PRCX-ray2.40L2-274[»]
3T6DX-ray1.95L2-274[»]
3T6EX-ray1.92L2-274[»]
4AC5X-ray8.20L1-274[»]
4CASX-ray3.50B1-274[»]
5PRCX-ray2.35L2-274[»]
6PRCX-ray2.30L2-274[»]
7PRCX-ray2.65L2-274[»]
ProteinModelPortaliP06009.
SMRiP06009. Positions 2-274.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP06009.

Family and domain databases

Gene3Di1.20.85.10. 2 hits.
InterProiIPR005871. Photo_RC_L.
IPR000484. Photo_RC_L/M.
[Graphical view]
PfamiPF00124. Photo_RC. 1 hit.
[Graphical view]
PRINTSiPR00256. REACTNCENTRE.
SUPFAMiSSF81483. SSF81483. 1 hit.
TIGRFAMsiTIGR01157. pufL. 1 hit.
PROSITEiPS00244. REACTION_CENTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The 'light' and 'medium' subunits of the photosynthetic reaction centre from Rhodopseudomonas viridis: isolation of the genes, nucleotide and amino acid sequence."
    Michel H., Weyer K.A., Gruenberg H., Dunger I., Oesterhelt D., Lottspeich F.
    EMBO J. 5:1149-1158(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 19567 / DSM 133 / F.
  2. "Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3-A resolution."
    Deisenhofer J., Epp O., Miki K., Huber R., Michel H.
    Nature 318:618-624(1985)
    Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
  3. "X-ray structure analysis of a membrane protein complex. Electron density map at 3-A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis."
    Deisenhofer J., Epp O., Miki K., Huber R., Michel H.
    J. Mol. Biol. 180:385-398(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
  4. "The coupling of light-induced electron transfer and proton uptake as derived from crystal structures of reaction centres from Rhodopseudomonas viridis modified at the binding site of the secondary quinone, QB."
    Lancaster C.R.D., Michel H.
    Structure 5:1339-1359(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
    Strain: ATCC 19567 / DSM 133 / F.
  5. "Refined crystal structures of reaction centres from Rhodopseudomonas viridis in complexes with the herbicide atrazine and two chiral atrazine derivatives also lead to a new model of the bound carotenoid."
    Lancaster C.R.D., Michel H.
    J. Mol. Biol. 286:883-898(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
    Strain: ATCC 19567 / DSM 133 / F.
  6. "Nobel lecture. The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis."
    Deisenhofer J., Michel H.
    EMBO J. 8:2149-2170(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.

Entry informationi

Entry nameiRCEL_BLAVI
AccessioniPrimary (citable) accession number: P06009
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.