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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi94 – 941Iron (heme 1 axial ligand)Combined sources1 Publication
Binding sitei107 – 1071Heme 1 (covalent)Combined sources1 Publication
Binding sitei110 – 1101Heme 1 (covalent)Combined sources1 Publication
Metal bindingi111 – 1111Iron (heme 1 axial ligand); via tele nitrogenCombined sources1 Publication
Metal bindingi130 – 1301Iron (heme 2 axial ligand)Combined sources1 Publication
Metal bindingi144 – 1441Iron (heme 4 axial ligand); via tele nitrogenCombined sources1 Publication
Binding sitei152 – 1521Heme 2 (covalent)Combined sources1 Publication
Binding sitei155 – 1551Heme 2 (covalent)Combined sources1 Publication
Metal bindingi156 – 1561Iron (heme 2 axial ligand); via tele nitrogenCombined sources1 Publication
Metal bindingi253 – 2531Iron (heme 3 axial ligand)Combined sources1 Publication
Binding sitei264 – 2641Heme 3 (covalent)Combined sources1 Publication
Binding sitei267 – 2671Heme 3 (covalent)Combined sources1 Publication
Metal bindingi268 – 2681Iron (heme 3 axial ligand); via tele nitrogenCombined sources1 Publication
Binding sitei325 – 3251Heme 4 (covalent)Combined sources1 Publication
Binding sitei328 – 3281Heme 4 (covalent)Combined sources1 Publication
Metal bindingi329 – 3291Iron (heme 4 axial ligand); via tele nitrogenCombined sources1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi284 – 2841R → K: 110 mV decrease in redox potential of heme 3. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Chaini21 – 356336Photosynthetic reaction center cytochrome c subunitPRO_0000006551Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi21 – 211S-diacylglycerol cysteinePROSITE-ProRule annotationCombined sources2 Publications

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)LengthDescriptionGraphical viewFeature identifierActions
Sitei21 – 211Not N-palmitoylatedCombined sources2 Publications

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

Structurei

Secondary structure

1
356
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi45 – 5511Combined sources
Beta strandi69 – 713Combined sources
Helixi72 – 754Combined sources
Beta strandi76 – 783Combined sources
Beta strandi80 – 823Combined sources
Helixi87 – 10115Combined sources
Turni103 – 1053Combined sources
Helixi106 – 1094Combined sources
Helixi122 – 14019Combined sources
Helixi142 – 1454Combined sources
Turni146 – 1483Combined sources
Helixi152 – 1565Combined sources
Beta strandi159 – 1613Combined sources
Beta strandi172 – 1754Combined sources
Turni182 – 1843Combined sources
Helixi189 – 1913Combined sources
Helixi192 – 1976Combined sources
Turni198 – 2025Combined sources
Helixi209 – 2135Combined sources
Beta strandi215 – 2173Combined sources
Beta strandi226 – 2294Combined sources
Beta strandi234 – 2363Combined sources
Helixi237 – 2393Combined sources
Helixi244 – 26017Combined sources
Helixi264 – 2663Combined sources
Helixi270 – 2723Combined sources
Helixi282 – 30019Combined sources
Helixi303 – 3075Combined sources
Helixi311 – 3133Combined sources
Helixi325 – 3295Combined sources
Beta strandi332 – 3343Combined sources
Helixi335 – 3384Combined sources
Helixi342 – 3443Combined sources
Helixi346 – 3483Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 21-352.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631A → P in ACK86664 (PubMed:22054235).Curated
Sequence conflicti97 – 971I → M in ACK86664 (PubMed:22054235).Curated
Sequence conflicti104 – 1041Q → E in ACK86664 (PubMed:22054235).Curated
Sequence conflicti272 – 2721T → S in ACK86664 (PubMed:22054235).Curated
Sequence conflicti275 – 2751S → T in ACK86664 (PubMed:22054235).Curated
Sequence conflicti297 – 2971L → M in ACK86664 (PubMed:22054235).Curated
Sequence conflicti307 – 3082AS → TV in ACK86664 (PubMed:22054235).Curated
Sequence conflicti343 – 3431K → Q in ACK86664 (PubMed:22054235).Curated

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.

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
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. Positions 21-352.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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: September 7, 2016
This is version 120 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.