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Protein

Photosynthetic reaction center cytochrome c subunit

Gene

pufC

Organism
Blastochloris viridis (Rhodopseudomonas viridis)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Manual assertion based on experiment ini

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

Complete GO annotation...

Keywords - Biological processi

Electron transport, Photosynthesis, Transport

Keywords - Ligandi

Heme, 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

  • Cellular chromatophore membrane 2 Publications; Lipid-anchor 2 Publications

GO - Cellular componenti

Complete GO annotation...

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

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

Proteomic databases

PRIDEiP07173.

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

Structurei

Secondary structure

1356
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi45 – 55Combined sources11
Beta strandi69 – 71Combined sources3
Helixi72 – 75Combined sources4
Beta strandi76 – 78Combined sources3
Beta strandi80 – 82Combined sources3
Helixi87 – 101Combined sources15
Turni103 – 105Combined sources3
Helixi106 – 109Combined sources4
Helixi122 – 140Combined sources19
Helixi142 – 145Combined sources4
Turni146 – 148Combined sources3
Helixi152 – 156Combined sources5
Beta strandi159 – 161Combined sources3
Beta strandi172 – 175Combined sources4
Turni182 – 184Combined sources3
Helixi189 – 191Combined sources3
Helixi192 – 197Combined sources6
Turni198 – 202Combined sources5
Helixi209 – 213Combined sources5
Beta strandi215 – 217Combined sources3
Beta strandi226 – 229Combined sources4
Beta strandi234 – 236Combined sources3
Helixi237 – 239Combined sources3
Helixi244 – 260Combined sources17
Helixi264 – 266Combined sources3
Helixi270 – 272Combined sources3
Helixi282 – 300Combined sources19
Helixi303 – 307Combined sources5
Helixi311 – 313Combined sources3
Helixi325 – 329Combined sources5
Beta strandi332 – 334Combined sources3
Helixi335 – 338Combined sources4
Helixi342 – 344Combined sources3
Helixi346 – 348Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DXRX-ray2.00C21-352[»]
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[»]
5PRCX-ray2.35C21-356[»]
6PRCX-ray2.30C21-356[»]
7PRCX-ray2.65C21-356[»]
ProteinModelPortaliP07173.
SMRiP07173.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07173.

Family & Domainsi

Keywords - Domaini

Signal

Family and domain databases

CDDicd09224. CytoC_RC. 1 hit.
Gene3Di1.10.468.10. 2 hits.
InterProiIPR011031. Multihaem_cyt.
IPR023119. Multihaem_cyt_PRC_cyt_su-like.
IPR003158. Photosyn_RC_cyt_c-su.
[Graphical view]
PfamiPF02276. CytoC_RC. 1 hit.
[Graphical view]
PIRSFiPIRSF000017. RC_cytochrome. 1 hit.
SUPFAMiSSF48695. SSF48695. 1 hit.
PROSITEiPS51008. MULTIHEME_CYTC. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

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

KEGGibvr:BVIR_606.

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-ray2.00C21-352[»]
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[»]
5PRCX-ray2.35C21-356[»]
6PRCX-ray2.30C21-356[»]
7PRCX-ray2.65C21-356[»]
ProteinModelPortaliP07173.
SMRiP07173.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP07173.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGibvr:BVIR_606.

Miscellaneous databases

EvolutionaryTraceiP07173.

Family and domain databases

CDDicd09224. CytoC_RC. 1 hit.
Gene3Di1.10.468.10. 2 hits.
InterProiIPR011031. Multihaem_cyt.
IPR023119. Multihaem_cyt_PRC_cyt_su-like.
IPR003158. Photosyn_RC_cyt_c-su.
[Graphical view]
PfamiPF02276. CytoC_RC. 1 hit.
[Graphical view]
PIRSFiPIRSF000017. RC_cytochrome. 1 hit.
SUPFAMiSSF48695. SSF48695. 1 hit.
PROSITEiPS51008. MULTIHEME_CYTC. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCYCR_BLAVI
AccessioniPrimary (citable) accession number: P07173
Secondary accession number(s): B8Y5U8, E2J7X6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: November 2, 2016
This is version 122 of the entry and version 1 of the sequence. [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

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.