UniProtKB - P07173 (CYCR_BLAVI)
Protein
Photosynthetic reaction center cytochrome c subunit
Gene
pufC
Organism
Blastochloris viridis (Rhodopseudomonas viridis)
Status
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 94 | Iron (heme 1 axial ligand)Combined sources1 Publication | 1 | |
Binding sitei | 107 | Heme 1 (covalent)Combined sources1 Publication | 1 | |
Binding sitei | 110 | Heme 1 (covalent)Combined sources1 Publication | 1 | |
Metal bindingi | 111 | Iron (heme 1 axial ligand); via tele nitrogenCombined sources1 Publication | 1 | |
Metal bindingi | 130 | Iron (heme 2 axial ligand)Combined sources1 Publication | 1 | |
Metal bindingi | 144 | Iron (heme 4 axial ligand); via tele nitrogenCombined sources1 Publication | 1 | |
Binding sitei | 152 | Heme 2 (covalent)Combined sources1 Publication | 1 | |
Binding sitei | 155 | Heme 2 (covalent)Combined sources1 Publication | 1 | |
Metal bindingi | 156 | Iron (heme 2 axial ligand); via tele nitrogenCombined sources1 Publication | 1 | |
Metal bindingi | 253 | Iron (heme 3 axial ligand)Combined sources1 Publication | 1 | |
Binding sitei | 264 | Heme 3 (covalent)Combined sources1 Publication | 1 | |
Binding sitei | 267 | Heme 3 (covalent)Combined sources1 Publication | 1 | |
Metal bindingi | 268 | Iron (heme 3 axial ligand); via tele nitrogenCombined sources1 Publication | 1 | |
Binding sitei | 325 | Heme 4 (covalent)Combined sources1 Publication | 1 | |
Binding sitei | 328 | Heme 4 (covalent)Combined sources1 Publication | 1 | |
Metal bindingi | 329 | Iron (heme 4 axial ligand); via tele nitrogenCombined sources1 Publication | 1 |
GO - Molecular functioni
- electron transfer activity Source: InterPro
- heme binding Source: InterPro
- iron ion binding Source: InterPro
GO - Biological processi
- photosynthesis Source: UniProtKB
- photosynthesis, light reaction Source: InterPro
Keywordsi
Biological process | Electron transport, Photosynthesis, Transport |
Ligand | Heme, Iron, Metal-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Photosynthetic reaction center cytochrome c subunitUniRule annotationAlternative name(s): Cytochrome c558/c559 |
Gene namesi | Name:pufCImported Synonyms:cytC ORF Names:BVIRIDIS_00500Imported |
Organismi | Blastochloris viridis (Rhodopseudomonas viridis) |
Taxonomic identifieri | 1079 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Hyphomicrobiaceae › Blastochloris |
Proteomesi |
|
Subcellular locationi
- Cellular chromatophore membrane 2 Publications; Lipid-anchor 2 Publications
GO - Cellular componenti
- plasma membrane-derived chromatophore membrane Source: UniProtKB
- plasma membrane light-harvesting complex Source: InterPro
Keywords - Cellular componenti
Membrane, Reaction centerPathology & Biotechi
Disruption phenotypei
Lack of photosynthesis.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 284 | R → K: 110 mV decrease in redox potential of heme 3. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB07552, (2R)-2-{[4-chloro-6-(ethylamino)-1,3,5-triazin-2-yl]amino}-2-methylbutanenitrile DB07551, (2S)-2-{[4-chloro-6-(ethylamino)-1,3,5-triazin-2-yl]amino}-2-methylbutanenitrile DB07392, Atrazine DB04147, Dodecyldimethylamine N-oxide DB04464, N-Formylmethionine DB08215, Terbutryn DB08689, Ubiquinone Q1 DB08690, Ubiquinone Q2 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 20 | Add BLAST | 20 | |
ChainiPRO_0000006551 | 21 – 356 | Photosynthetic reaction center cytochrome c subunitAdd BLAST | 336 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Lipidationi | 21 | S-diacylglycerol cysteinePROSITE-ProRule annotationCombined sources2 Publications | 1 |
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 21 | Not N-palmitoylatedCombined sources2 Publications | 1 |
Keywords - PTMi
LipoproteinInteractioni
Subunit structurei
Component of the photosynthetic reaction center composed of protein subunits L (PufL), M (PufM), H (PuhA) and cytochrome C (PufC).
5 PublicationsProtein-protein interaction databases
IntActi | P07173, 6 interactors |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P07173 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P07173 |
Family & Domainsi
Keywords - Domaini
SignalPhylogenomic databases
OMAi | CTYCHNT |
Family and domain databases
CDDi | cd09224, CytoC_RC, 1 hit |
Gene3Di | 1.10.468.10, 2 hits |
InterProi | View protein in InterPro IPR011031, Multihaem_cyt IPR023119, Multihaem_cyt_PRC_cyt_su-like IPR036280, Multihaem_cyt_sf IPR003158, Photosyn_RC_cyt_c-su |
Pfami | View protein in Pfam PF02276, CytoC_RC, 1 hit |
PIRSFi | PIRSF000017, RC_cytochrome, 1 hit |
SUPFAMi | SSF48695, SSF48695, 1 hit |
PROSITEi | View protein in PROSITE PS51008, MULTIHEME_CYTC, 1 hit PS51257, PROKAR_LIPOPROTEIN, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P07173-1 [UniParc]FASTAAdd to basket
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 63 | A → P in ACK86664 (PubMed:22054235).Curated | 1 | |
Sequence conflicti | 97 | I → M in ACK86664 (PubMed:22054235).Curated | 1 | |
Sequence conflicti | 104 | Q → E in ACK86664 (PubMed:22054235).Curated | 1 | |
Sequence conflicti | 272 | T → S in ACK86664 (PubMed:22054235).Curated | 1 | |
Sequence conflicti | 275 | S → T in ACK86664 (PubMed:22054235).Curated | 1 | |
Sequence conflicti | 297 | L → M in ACK86664 (PubMed:22054235).Curated | 1 | |
Sequence conflicti | 307 – 308 | AS → TV in ACK86664 (PubMed:22054235).Curated | 2 | |
Sequence conflicti | 343 | K → Q in ACK86664 (PubMed:22054235).Curated | 1 |
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 |
PIRi | S00139 |
Genome annotation databases
EnsemblBacteriai | CUU41065; CUU41065; BVIRIDIS_00500 |
PATRICi | fig|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 |
PIRi | S00139 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1DXR | X-ray | 2.00 | C | 21-356 | [»] | |
1PRC | X-ray | 2.30 | C | 21-356 | [»] | |
1R2C | X-ray | 2.86 | C | 21-356 | [»] | |
1VRN | X-ray | 2.20 | C | 21-352 | [»] | |
2I5N | X-ray | 1.96 | C | 21-356 | [»] | |
2JBL | X-ray | 2.40 | C | 1-356 | [»] | |
2PRC | X-ray | 2.45 | C | 21-356 | [»] | |
2WJM | X-ray | 1.95 | C | 21-356 | [»] | |
2WJN | X-ray | 1.86 | C | 21-356 | [»] | |
2X5U | X-ray | 3.00 | C | 21-356 | [»] | |
2X5V | X-ray | 3.00 | C | 21-356 | [»] | |
3D38 | X-ray | 3.21 | C | 21-356 | [»] | |
3G7F | X-ray | 2.50 | C | 21-356 | [»] | |
3PRC | X-ray | 2.40 | C | 21-356 | [»] | |
3T6D | X-ray | 1.95 | C | 1-356 | [»] | |
3T6E | X-ray | 1.92 | C | 1-356 | [»] | |
4AC5 | X-ray | 8.20 | C | 21-356 | [»] | |
4CAS | X-ray | 3.50 | A | 1-356 | [»] | |
5M7J | X-ray | 3.50 | A | 1-356 | [»] | |
5M7K | X-ray | 3.50 | A | 1-356 | [»] | |
5M7L | X-ray | 3.60 | A | 1-356 | [»] | |
5NJ4 | X-ray | 2.40 | C | 21-356 | [»] | |
5O4C | X-ray | 2.80 | C | 21-356 | [»] | |
5O64 | X-ray | 3.30 | C | 21-356 | [»] | |
5PRC | X-ray | 2.35 | C | 21-356 | [»] | |
6ET5 | electron microscopy | 3.00 | C | 21-353 | [»] | |
6PRC | X-ray | 2.30 | C | 21-356 | [»] | |
7PRC | X-ray | 2.65 | C | 21-356 | [»] | |
SMRi | P07173 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | P07173, 6 interactors |
Chemistry databases
DrugBanki | DB07552, (2R)-2-{[4-chloro-6-(ethylamino)-1,3,5-triazin-2-yl]amino}-2-methylbutanenitrile DB07551, (2S)-2-{[4-chloro-6-(ethylamino)-1,3,5-triazin-2-yl]amino}-2-methylbutanenitrile DB07392, Atrazine DB04147, Dodecyldimethylamine N-oxide DB04464, N-Formylmethionine DB08215, Terbutryn DB08689, Ubiquinone Q1 DB08690, Ubiquinone Q2 |
Genome annotation databases
EnsemblBacteriai | CUU41065; CUU41065; BVIRIDIS_00500 |
PATRICi | fig|1079.6.peg.623 |
Phylogenomic databases
OMAi | CTYCHNT |
Miscellaneous databases
EvolutionaryTracei | P07173 |
Family and domain databases
CDDi | cd09224, CytoC_RC, 1 hit |
Gene3Di | 1.10.468.10, 2 hits |
InterProi | View protein in InterPro IPR011031, Multihaem_cyt IPR023119, Multihaem_cyt_PRC_cyt_su-like IPR036280, Multihaem_cyt_sf IPR003158, Photosyn_RC_cyt_c-su |
Pfami | View protein in Pfam PF02276, CytoC_RC, 1 hit |
PIRSFi | PIRSF000017, RC_cytochrome, 1 hit |
SUPFAMi | SSF48695, SSF48695, 1 hit |
PROSITEi | View protein in PROSITE PS51008, MULTIHEME_CYTC, 1 hit PS51257, PROKAR_LIPOPROTEIN, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | CYCR_BLAVI | |
Accessioni | P07173Primary (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: | February 10, 2021 | |
This is version 141 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references