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Protein

Photosynthetic reaction center cytochrome c subunit

Gene

pufC

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

Functioni

The reaction center of purple bacteria contains a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor.1 Publication

Redox potential

E0 is -60 mV for heme 1. E0 is +320 mV for heme 2. E0 is +380 mV for heme 3. E0 is +15 mV for heme 4.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi94Iron (heme 1 axial ligand)Combined sources1 Publication1
Binding sitei107Heme 1 (covalent)Combined sources1 Publication1
Binding sitei110Heme 1 (covalent)Combined sources1 Publication1
Metal bindingi111Iron (heme 1 axial ligand); via tele nitrogenCombined sources1 Publication1
Metal bindingi130Iron (heme 2 axial ligand)Combined sources1 Publication1
Metal bindingi144Iron (heme 4 axial ligand); via tele nitrogenCombined sources1 Publication1
Binding sitei152Heme 2 (covalent)Combined sources1 Publication1
Binding sitei155Heme 2 (covalent)Combined sources1 Publication1
Metal bindingi156Iron (heme 2 axial ligand); via tele nitrogenCombined sources1 Publication1
Metal bindingi253Iron (heme 3 axial ligand)Combined sources1 Publication1
Binding sitei264Heme 3 (covalent)Combined sources1 Publication1
Binding sitei267Heme 3 (covalent)Combined sources1 Publication1
Metal bindingi268Iron (heme 3 axial ligand); via tele nitrogenCombined sources1 Publication1
Binding sitei325Heme 4 (covalent)Combined sources1 Publication1
Binding sitei328Heme 4 (covalent)Combined sources1 Publication1
Metal bindingi329Iron (heme 4 axial ligand); via tele nitrogenCombined sources1 Publication1

GO - Molecular functioni

GO - Biological processi

  • photosynthesis Source: UniProtKB
  • photosynthesis, light reaction Source: InterPro

Keywordsi

Biological processElectron transport, Photosynthesis, Transport
LigandHeme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Photosynthetic reaction center cytochrome c subunitUniRule annotation
Alternative name(s):
Cytochrome c558/c559
Gene namesi
Name:pufCImported
Synonyms:cytC
ORF Names:BVIRIDIS_00500Imported
OrganismiBlastochloris viridis (Rhodopseudomonas viridis)
Taxonomic identifieri1079 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesHyphomicrobiaceaeBlastochloris
Proteomesi
  • UP000065734 Componenti: Chromosome I

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Membrane, Reaction center

Pathology & Biotechi

Disruption phenotypei

Lack of photosynthesis.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi284R → K: 110 mV decrease in redox potential of heme 3. 1 Publication1

Chemistry databases

DrugBankiDB08215 2-T-BUTYLAMINO-4-ETHYLAMINO-6-METHYLTHIO-S-TRIAZINE
DB04147 Lauryl Dimethylamine-N-Oxide
DB04464 N-Formylmethionine
DB08689 UBIQUINONE-1
DB08690 UBIQUINONE-2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Add BLAST20
ChainiPRO_000000655121 – 356Photosynthetic reaction center cytochrome c subunitAdd BLAST336

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi21S-diacylglycerol cysteinePROSITE-ProRule annotationCombined sources2 Publications1

Post-translational modificationi

Binds 4 heme groups per subunit.6 Publications
After the signal sequence is removed, the N-terminal cysteine is modified to form a diacylglyceride thioether, but the alpha-amino group is free and is not N-palmitoylated.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei21Not N-palmitoylatedCombined sources2 Publications1

Keywords - PTMi

Lipoprotein

Interactioni

Subunit structurei

Component of the photosynthetic reaction center composed of protein subunits L (PufL), M (PufM), H (PuhA) and cytochrome C (PufC).5 Publications

Protein-protein interaction databases

IntActiP07173, 3 interactors

Structurei

Secondary structure

1356
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP07173
SMRiP07173
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07173

Family & Domainsi

Keywords - Domaini

Signal

Phylogenomic databases

KOiK13992

Family and domain databases

CDDicd09224 CytoC_RC, 1 hit
Gene3Di1.10.468.10, 3 hits
InterProiView protein in InterPro
IPR011031 Multihaem_cyt
IPR023119 Multihaem_cyt_PRC_cyt_su-like
IPR036280 Multihaem_cyt_sf
IPR003158 Photosyn_RC_cyt_c-su
PfamiView protein in Pfam
PF02276 CytoC_RC, 1 hit
PIRSFiPIRSF000017 RC_cytochrome, 1 hit
SUPFAMiSSF48695 SSF48695, 1 hit
PROSITEiView protein in PROSITE
PS51008 MULTIHEME_CYTC, 1 hit
PS51257 PROKAR_LIPOPROTEIN, 1 hit

Sequencei

Sequence statusi: Complete.

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

P07173-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKQLIVNSVA TVALASLVAG CFEPPPATTT QTGFRGLSMG EVLHPATVKA
60 70 80 90 100
KKERDAQYPP ALAAVKAEGP PVSQVYKNVK VLGNLTEAEF LRTMTAITEW
110 120 130 140 150
VSPQEGCTYC HDENNLASEA KYPYVVARRM LEMTRAINTN WTQHVAQTGV
160 170 180 190 200
TCYTCHRGTP LPPYVRYLEP TLPLNNRETP THVERVETRS GYVVRLAKYT
210 220 230 240 250
AYSALNYDPF TMFLANDKRQ VRVVPQTALP LVGVSRGKER RPLSDAYATF
260 270 280 290 300
ALMMSISDSL GTNCTFCHNA QTFESWGKKS TPQRAIAWWG IRMVRDLNMN
310 320 330 340 350
YLAPLNASLP ASRLGRQGEA PQADCRTCHQ GVTKPLFGAS RLKDYPELGP

IKAAAK
Length:356
Mass (Da):39,371
Last modified:April 1, 1988 - v1
Checksum:iECE3D64F1BB0877A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti63A → P in ACK86664 (PubMed:22054235).Curated1
Sequence conflicti97I → M in ACK86664 (PubMed:22054235).Curated1
Sequence conflicti104Q → E in ACK86664 (PubMed:22054235).Curated1
Sequence conflicti272T → S in ACK86664 (PubMed:22054235).Curated1
Sequence conflicti275S → T in ACK86664 (PubMed:22054235).Curated1
Sequence conflicti297L → M in ACK86664 (PubMed:22054235).Curated1
Sequence conflicti307 – 308AS → TV in ACK86664 (PubMed:22054235).Curated2
Sequence conflicti343K → Q in ACK86664 (PubMed:22054235).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05768 Genomic DNA Translation: CAA29223.1
FJ483785 Genomic DNA Translation: ACK86664.1
HQ009849 Genomic DNA Translation: ADN94690.1
LN907867 Genomic DNA Translation: CUU41065.1
M16317 Genomic DNA Translation: AAA26093.1
PIRiS00139

Genome annotation databases

EnsemblBacteriaiCUU41065; CUU41065; BVIRIDIS_00500
KEGGibvr:BVIR_606
PATRICifig|1079.6.peg.623

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05768 Genomic DNA Translation: CAA29223.1
FJ483785 Genomic DNA Translation: ACK86664.1
HQ009849 Genomic DNA Translation: ADN94690.1
LN907867 Genomic DNA Translation: CUU41065.1
M16317 Genomic DNA Translation: AAA26093.1
PIRiS00139

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DXRX-ray2.00C21-356[»]
1PRCX-ray2.30C21-356[»]
1R2CX-ray2.86C21-356[»]
1VRNX-ray2.20C21-352[»]
2I5NX-ray1.96C21-356[»]
2JBLX-ray2.40C1-356[»]
2PRCX-ray2.45C21-356[»]
2WJMX-ray1.95C21-356[»]
2WJNX-ray1.86C21-356[»]
2X5UX-ray3.00C21-356[»]
2X5VX-ray3.00C21-356[»]
3D38X-ray3.21C21-356[»]
3G7FX-ray2.50C21-356[»]
3PRCX-ray2.40C21-356[»]
3T6DX-ray1.95C1-356[»]
3T6EX-ray1.92C1-356[»]
4AC5X-ray8.20C21-356[»]
4CASX-ray3.50A1-356[»]
5M7JX-ray3.50A1-356[»]
5M7KX-ray3.50A1-356[»]
5M7LX-ray3.60A1-356[»]
5NJ4X-ray2.40C21-356[»]
5O4CX-ray2.80C21-356[»]
5O64X-ray3.30C21-356[»]
5PRCX-ray2.35C21-356[»]
6ET5electron microscopy3.00C21-353[»]
6PRCX-ray2.30C21-356[»]
7PRCX-ray2.65C21-356[»]
ProteinModelPortaliP07173
SMRiP07173
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP07173, 3 interactors

Chemistry databases

DrugBankiDB08215 2-T-BUTYLAMINO-4-ETHYLAMINO-6-METHYLTHIO-S-TRIAZINE
DB04147 Lauryl Dimethylamine-N-Oxide
DB04464 N-Formylmethionine
DB08689 UBIQUINONE-1
DB08690 UBIQUINONE-2

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCUU41065; CUU41065; BVIRIDIS_00500
KEGGibvr:BVIR_606
PATRICifig|1079.6.peg.623

Phylogenomic databases

KOiK13992

Miscellaneous databases

EvolutionaryTraceiP07173

Family and domain databases

CDDicd09224 CytoC_RC, 1 hit
Gene3Di1.10.468.10, 3 hits
InterProiView protein in InterPro
IPR011031 Multihaem_cyt
IPR023119 Multihaem_cyt_PRC_cyt_su-like
IPR036280 Multihaem_cyt_sf
IPR003158 Photosyn_RC_cyt_c-su
PfamiView protein in Pfam
PF02276 CytoC_RC, 1 hit
PIRSFiPIRSF000017 RC_cytochrome, 1 hit
SUPFAMiSSF48695 SSF48695, 1 hit
PROSITEiView protein in PROSITE
PS51008 MULTIHEME_CYTC, 1 hit
PS51257 PROKAR_LIPOPROTEIN, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCYCR_BLAVI
AccessioniPrimary (citable) accession number: P07173
Secondary accession number(s): B8Y5U8, E2J7X6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: October 10, 2018
This is version 132 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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