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Protein

Reaction center protein L chain

Gene

pufL

Organism
Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
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

  1. bacteriochlorophyll binding Source: UniProtKB-KW
  2. electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity Source: InterPro
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. photosynthetic electron transport in photosystem II Source: InterPro
  2. protein-chromophore linkage Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Electron transport, Photosynthesis, Transport

Keywords - Ligandi

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

Protein family/group databases

TCDBi3.E.2.1.1. the photosynthetic reaction center (prc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Reaction center protein L chain
Alternative name(s):
Photosynthetic reaction center L subunit
Gene namesi
Name:pufL
OrganismiRhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Taxonomic identifieri1063 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 3231Cytoplasmic1 PublicationAdd
BLAST
Transmembranei33 – 5624HelicalAdd
BLAST
Topological domaini57 – 8327Periplasmic1 PublicationAdd
BLAST
Transmembranei84 – 11229HelicalAdd
BLAST
Topological domaini113 – 1164Cytoplasmic1 Publication
Transmembranei117 – 13923HelicalAdd
BLAST
Topological domaini140 – 17132Periplasmic1 PublicationAdd
BLAST
Transmembranei172 – 19928HelicalAdd
BLAST
Topological domaini200 – 22526Cytoplasmic1 PublicationAdd
BLAST
Transmembranei226 – 25126HelicalAdd
BLAST
Topological domaini252 – 28231Periplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane-derived chromatophore membrane Source: UniProtKB-SubCell
  3. plasma membrane light-harvesting complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Reaction center

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 282281Reaction center protein L chainPRO_0000090407Add
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).

Protein-protein interaction databases

DIPiDIP-60489N.

Structurei

Secondary structure

1
282
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni5 – 73Combined sources
Helixi8 – 103Combined sources
Beta strandi17 – 193Combined sources
Turni20 – 234Combined sources
Beta strandi25 – 273Combined sources
Beta strandi30 – 323Combined sources
Helixi33 – 5725Combined sources
Turni62 – 643Combined sources
Helixi72 – 743Combined sources
Helixi81 – 833Combined sources
Helixi85 – 11228Combined sources
Helixi117 – 13317Combined sources
Helixi135 – 1406Combined sources
Helixi143 – 1453Combined sources
Helixi153 – 16311Combined sources
Helixi168 – 1703Combined sources
Helixi172 – 19928Combined sources
Beta strandi202 – 2054Combined sources
Helixi210 – 22112Combined sources
Helixi227 – 25024Combined sources
Turni253 – 2553Combined sources
Helixi260 – 2634Combined sources
Helixi265 – 2684Combined sources
Turni271 – 2755Combined sources
Beta strandi278 – 2803Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AIGX-ray2.60L/N2-282[»]
1AIJX-ray2.20L/R2-282[»]
1DS8X-ray2.50L/R2-282[»]
1DV3X-ray2.50L/R2-282[»]
1DV6X-ray2.50L/R2-282[»]
1E14X-ray2.70L2-282[»]
1E6DX-ray2.30L2-282[»]
1F6NX-ray2.80L2-282[»]
1FNPX-ray2.60L2-282[»]
1FNQX-ray2.60L2-282[»]
1JGWX-ray2.80L2-282[»]
1JGXX-ray3.01L2-282[»]
1JGYX-ray2.70L2-282[»]
1JGZX-ray2.70L2-282[»]
1JH0X-ray3.50L2-282[»]
1K6LX-ray3.10L2-282[»]
1K6NX-ray3.10L2-282[»]
1KBYX-ray2.50L2-282[»]
1L9BX-ray2.40L2-282[»]
1L9JX-ray3.25L/R2-282[»]
1M3XX-ray2.55L2-282[»]
1MPSX-ray2.55L2-282[»]
1OGVX-ray2.35L2-282[»]
1PCRX-ray2.65L2-282[»]
1PSSX-ray3.00L6-271[»]
1PSTX-ray3.00L6-271[»]
1QOVX-ray2.10L2-282[»]
1RG5X-ray2.50L2-282[»]
1RGNX-ray2.80L2-282[»]
1RQKX-ray2.70L2-282[»]
1RVJX-ray2.75L2-282[»]
1RY5X-ray2.10L2-282[»]
1RZHX-ray1.80L2-282[»]
1RZZX-ray2.40L/R2-282[»]
1S00X-ray2.60L/R2-282[»]
1UMXX-ray2.80L2-282[»]
1YF6X-ray2.25L2-282[»]
1YSTX-ray3.00L2-274[»]
1Z9JX-ray4.50A2-282[»]
1Z9KX-ray4.60A2-282[»]
2BNPX-ray2.70A2-282[»]
2BNSX-ray2.50A2-282[»]
2BOZX-ray2.40L2-282[»]
2GMRX-ray2.50L2-282[»]
2GNUX-ray2.20L2-282[»]
2HG3X-ray2.70L2-282[»]
2HG9X-ray2.45L2-282[»]
2HH1X-ray2.55L2-282[»]
2HHKX-ray2.50L2-282[»]
2HITX-ray2.75L2-282[»]
2HJ6X-ray3.00L2-282[»]
2J8CX-ray1.87L2-282[»]
2J8DX-ray2.07L2-282[»]
2JIYX-ray2.20L2-282[»]
2JJ0X-ray2.80L2-282[»]
2RCRX-ray3.10L2-282[»]
2UWSX-ray2.90L2-282[»]
2UWTX-ray2.50L2-282[»]
2UWUX-ray2.04L2-282[»]
2UWVX-ray2.13L2-282[»]
2UWWX-ray2.05L2-282[»]
2UX3X-ray2.50L2-282[»]
2UX4X-ray2.51L2-282[»]
2UX5X-ray2.21L2-282[»]
2UXJX-ray2.25L2-282[»]
2UXKX-ray2.31L2-282[»]
2UXLX-ray2.88L2-282[»]
2UXMX-ray2.70L2-282[»]
3DSYX-ray3.00L2-282[»]
3DTAX-ray3.20L2-282[»]
3DTRX-ray3.10L2-282[»]
3DTSX-ray3.10L2-282[»]
3DU2X-ray3.10L2-282[»]
3DU3X-ray2.80L2-282[»]
3DUQX-ray2.70L2-282[»]
3I4DX-ray2.01L2-282[»]
3V3YX-ray2.80L2-282[»]
3V3ZX-ray2.90L2-282[»]
3ZUMX-ray2.50L2-282[»]
3ZUWX-ray2.31L2-282[»]
4H99X-ray2.97L2-282[»]
4H9LX-ray2.77L2-282[»]
4HBHX-ray2.93L2-282[»]
4HBJX-ray2.74L2-282[»]
4IN7X-ray2.85L2-282[»]
4LWYX-ray2.90L1-282[»]
4N7KX-ray2.85L2-282[»]
4RCRX-ray2.80L2-282[»]
4TQQX-ray2.50L2-282[»]
4V9GX-ray7.78L1-282[»]
ProteinModelPortaliP0C0Y8.
SMRiP0C0Y8. Positions 2-282.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C0Y8.

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.

P0C0Y8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALLSFERKY RVPGGTLVGG NLFDFWVGPF YVGFFGVATF FFAALGIILI
60 70 80 90 100
AWSAVLQGTW NPQLISVYPP ALEYGLGGAP LAKGGLWQII TICATGAFVS
110 120 130 140 150
WALREVEICR KLGIGYHIPF AFAFAILAYL TLVLFRPVMM GAWGYAFPYG
160 170 180 190 200
IWTHLDWVSN TGYTYGNFHY NPAHMIAISF FFTNALALAL HGALVLSAAN
210 220 230 240 250
PEKGKEMRTP DHEDTFFRDL VGYSIGTLGI HRLGLLLSLS AVFFSALCMI
260 270 280
ITGTIWFDQW VDWWQWWVKL PWWANIPGGI NG
Length:282
Mass (Da):31,457
Last modified:January 23, 2007 - v2
Checksum:i044F4D3AF085B136
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10206 Genomic DNA. Translation: AAA26177.1.
X63404 Genomic DNA. Translation: CAA44999.1.
PIRiS24212. WNRFLS.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10206 Genomic DNA. Translation: AAA26177.1.
X63404 Genomic DNA. Translation: CAA44999.1.
PIRiS24212. WNRFLS.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AIGX-ray2.60L/N2-282[»]
1AIJX-ray2.20L/R2-282[»]
1DS8X-ray2.50L/R2-282[»]
1DV3X-ray2.50L/R2-282[»]
1DV6X-ray2.50L/R2-282[»]
1E14X-ray2.70L2-282[»]
1E6DX-ray2.30L2-282[»]
1F6NX-ray2.80L2-282[»]
1FNPX-ray2.60L2-282[»]
1FNQX-ray2.60L2-282[»]
1JGWX-ray2.80L2-282[»]
1JGXX-ray3.01L2-282[»]
1JGYX-ray2.70L2-282[»]
1JGZX-ray2.70L2-282[»]
1JH0X-ray3.50L2-282[»]
1K6LX-ray3.10L2-282[»]
1K6NX-ray3.10L2-282[»]
1KBYX-ray2.50L2-282[»]
1L9BX-ray2.40L2-282[»]
1L9JX-ray3.25L/R2-282[»]
1M3XX-ray2.55L2-282[»]
1MPSX-ray2.55L2-282[»]
1OGVX-ray2.35L2-282[»]
1PCRX-ray2.65L2-282[»]
1PSSX-ray3.00L6-271[»]
1PSTX-ray3.00L6-271[»]
1QOVX-ray2.10L2-282[»]
1RG5X-ray2.50L2-282[»]
1RGNX-ray2.80L2-282[»]
1RQKX-ray2.70L2-282[»]
1RVJX-ray2.75L2-282[»]
1RY5X-ray2.10L2-282[»]
1RZHX-ray1.80L2-282[»]
1RZZX-ray2.40L/R2-282[»]
1S00X-ray2.60L/R2-282[»]
1UMXX-ray2.80L2-282[»]
1YF6X-ray2.25L2-282[»]
1YSTX-ray3.00L2-274[»]
1Z9JX-ray4.50A2-282[»]
1Z9KX-ray4.60A2-282[»]
2BNPX-ray2.70A2-282[»]
2BNSX-ray2.50A2-282[»]
2BOZX-ray2.40L2-282[»]
2GMRX-ray2.50L2-282[»]
2GNUX-ray2.20L2-282[»]
2HG3X-ray2.70L2-282[»]
2HG9X-ray2.45L2-282[»]
2HH1X-ray2.55L2-282[»]
2HHKX-ray2.50L2-282[»]
2HITX-ray2.75L2-282[»]
2HJ6X-ray3.00L2-282[»]
2J8CX-ray1.87L2-282[»]
2J8DX-ray2.07L2-282[»]
2JIYX-ray2.20L2-282[»]
2JJ0X-ray2.80L2-282[»]
2RCRX-ray3.10L2-282[»]
2UWSX-ray2.90L2-282[»]
2UWTX-ray2.50L2-282[»]
2UWUX-ray2.04L2-282[»]
2UWVX-ray2.13L2-282[»]
2UWWX-ray2.05L2-282[»]
2UX3X-ray2.50L2-282[»]
2UX4X-ray2.51L2-282[»]
2UX5X-ray2.21L2-282[»]
2UXJX-ray2.25L2-282[»]
2UXKX-ray2.31L2-282[»]
2UXLX-ray2.88L2-282[»]
2UXMX-ray2.70L2-282[»]
3DSYX-ray3.00L2-282[»]
3DTAX-ray3.20L2-282[»]
3DTRX-ray3.10L2-282[»]
3DTSX-ray3.10L2-282[»]
3DU2X-ray3.10L2-282[»]
3DU3X-ray2.80L2-282[»]
3DUQX-ray2.70L2-282[»]
3I4DX-ray2.01L2-282[»]
3V3YX-ray2.80L2-282[»]
3V3ZX-ray2.90L2-282[»]
3ZUMX-ray2.50L2-282[»]
3ZUWX-ray2.31L2-282[»]
4H99X-ray2.97L2-282[»]
4H9LX-ray2.77L2-282[»]
4HBHX-ray2.93L2-282[»]
4HBJX-ray2.74L2-282[»]
4IN7X-ray2.85L2-282[»]
4LWYX-ray2.90L1-282[»]
4N7KX-ray2.85L2-282[»]
4RCRX-ray2.80L2-282[»]
4TQQX-ray2.50L2-282[»]
4V9GX-ray7.78L1-282[»]
ProteinModelPortaliP0C0Y8.
SMRiP0C0Y8. Positions 2-282.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60489N.

Protein family/group databases

TCDBi3.E.2.1.1. the photosynthetic reaction center (prc) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP0C0Y8.

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. "Primary structure of the L subunit of the reaction center from Rhodopseudomonas sphaeroides."
    Williams J.C., Steiner L.A., Feher G., Simon M.I.
    Proc. Natl. Acad. Sci. U.S.A. 81:7303-7307(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Towards the understanding of the function of Rb sphaeroides Y wild type reaction center: gene cloning, protein and detergent structures in the three-dimensional crystals."
    Arnoux B., Ducruix A., Astier C., Picaud M., Roth M., Reiss-Husson F.
    Biochimie 72:525-530(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Y.
  3. "Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides."
    Chang C.-H., El-Kabbani O., Tiede D., Norris J., Schiffer M.
    Biochemistry 30:5352-5360(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
  4. "Structure of the reaction center from Rhodobacter sphaeroides R-26: protein-cofactor (quinones and Fe2+) interactions."
    Allen J.P., Feher G., Yeates T.O., Komiya H., Rees D.C.
    Proc. Natl. Acad. Sci. U.S.A. 85:8487-8491(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    Strain: R-26.
  5. "Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits."
    Allen J.P., Feher G., Yeates T.O., Komiya H., Rees D.C.
    Proc. Natl. Acad. Sci. U.S.A. 84:6162-6166(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    Strain: R-26.
  6. "Structural studies of wild-type and mutant reaction centers from an antenna-deficient strain of Rhodobacter sphaeroides: monitoring the optical properties of the complex from bacterial cell to crystal."
    McAuley-Hecht K.E., Fyfe P.K., Ridge J.P., Prince S.M., Hunter C.N., Isaacs N.W., Cogdell R.J., Jones M.R.
    Biochemistry 37:4740-4750(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS).
  7. "The use of gene fusions to examine the membrane topology of the L-subunit of the photosynthetic reaction center and of the cytochrome b subunit of the bc1 complex from Rhodobacter sphaeroides."
    Yun C.H., Van Doren S.R., Crofts A.R., Gennis R.B.
    J. Biol. Chem. 266:10967-10973(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.

Entry informationi

Entry nameiRCEL_RHOSH
AccessioniPrimary (citable) accession number: P0C0Y8
Secondary accession number(s): P02954, Q9RFB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 67 of the entry and version 2 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

External Data

Dasty 3

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 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.