pufC

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	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

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

photosynthesis
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 10736158
photosynthesis, light reaction Source: InterPro

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	Electron transport, Photosynthesis, Transport
Ligand	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
Organismⁱ	Blastochloris viridis (Rhodopseudomonas viridis)
Taxonomic identifierⁱ	1079 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Hyphomicrobiaceae › Blastochloris
Proteomesⁱ	UP000065734 Componentⁱ: Chromosome I

Subcellular locationⁱ

Cellular chromatophore membrane
2 Publications
Manual assertion based on experiment inⁱ
- Ref.8
  "The coupling of light-induced electron transfer and proton uptake as derived from crystal structures of reaction centres from Rhodopseudomonas viridis modified at the binding site of the secondary quinone, QB."
  Lancaster C.R.D., Michel H.
  Structure 5:1339-1359(1997) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS)OF 21-356 IN COMPLEXES WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA, SUBCELLULAR LOCATION.
- Ref.9
  "Refined crystal structures of reaction centres from Rhodopseudomonas viridis in complexes with the herbicide atrazine and two chiral atrazine derivatives also lead to a new model of the bound carotenoid."
  Lancaster C.R.D., Michel H.
  J. Mol. Biol. 286:883-898(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 21-356 IN COMPLEXES WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA, SUBCELLULAR LOCATION.
; Lipid-anchor
2 Publications
Manual assertion based on experiment inⁱ
- Ref.2
  "New insights into the structure of the reaction centre from Blastochloris viridis: evolution in the laboratory."
  Roszak A.W., Moulisova V., Reksodipuro A.D., Gardiner A.T., Fujii R., Hashimoto H., Isaacs N.W., Cogdell R.J.
  Biochem. J. 442:27-37(2012) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF WILD-TYPE AND MUTANT PRO-63/MET-97/GLU-104/SER-272/THR-275/MET-297/307-THR-VAL-308/GLN-343 IN COMPLEXES WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA, DIACYLGLYCEROL AT CYS-21, LACK OF PALMITOYLATION AT CYS-21.
- Ref.4
  "The cytochrome subunit of the photosynthetic reaction center from Rhodopseudomonas viridis is a lipoprotein."
  Weyer K.A., Schaefer W., Lottspeich F., Michel H.
  Biochemistry 26:2909-2914(1987)
  Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46, DIACYLGLYCEROL AT CYS-21, LACK OF PALMITOYLATION AT CYS-21.

GO - Cellular componentⁱ

plasma membrane-derived chromatophore membrane
Source: UniProtKB
Inferred from direct assayⁱ
- 10024457
- 9351808
plasma membrane light-harvesting complex Source: InterPro

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Membrane, Reaction center

Pathology & 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

Drug and drug target database More...DrugBankⁱ	DB08215 2-T-BUTYLAMINO-4-ETHYLAMINO-6-METHYLTHIO-S-TRIAZINE DB04147 Lauryl Dimethylamine-N-Oxide DB04464 N-Formylmethionine DB08689 UBIQUINONE-1 DB08690 UBIQUINONE-2

DrugBankⁱ

DB08215 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 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

Manual assertion based on experiment inⁱ

Ref.2
"New insights into the structure of the reaction centre from Blastochloris viridis: evolution in the laboratory."
Roszak A.W., Moulisova V., Reksodipuro A.D., Gardiner A.T., Fujii R., Hashimoto H., Isaacs N.W., Cogdell R.J.
Biochem. J. 442:27-37(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF WILD-TYPE AND MUTANT PRO-63/MET-97/GLU-104/SER-272/THR-275/MET-297/307-THR-VAL-308/GLN-343 IN COMPLEXES WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA, DIACYLGLYCEROL AT CYS-21, LACK OF PALMITOYLATION AT CYS-21.
Ref.5
"Uphill electron transfer in the tetraheme cytochrome subunit of the Rhodopseudomonas viridis photosynthetic reaction center: evidence from site-directed mutagenesis."
Chen I.P., Mathis P., Koepke J., Michel H.
Biochemistry 39:3592-3602(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PTM, DISRUPTION PHENOTYPE, MUTAGENESIS OF ARG-284.
Ref.6
"X-ray structure analysis of a membrane protein complex. Electron density map at 3-A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis."
Deisenhofer J., Epp O., Miki K., Huber R., Michel H.
J. Mol. Biol. 180:385-398(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS) IN COMPLEX WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA.
Ref.7
"Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3-A resolution."
Deisenhofer J., Epp O., Miki K., Huber R., Michel H.
Nature 318:618-624(1985)
Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS) IN COMPLEX WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA.
Ref.8
"The coupling of light-induced electron transfer and proton uptake as derived from crystal structures of reaction centres from Rhodopseudomonas viridis modified at the binding site of the secondary quinone, QB."
Lancaster C.R.D., Michel H.
Structure 5:1339-1359(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS)OF 21-356 IN COMPLEXES WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA, SUBCELLULAR LOCATION.
Ref.9
"Refined crystal structures of reaction centres from Rhodopseudomonas viridis in complexes with the herbicide atrazine and two chiral atrazine derivatives also lead to a new model of the bound carotenoid."
Lancaster C.R.D., Michel H.
J. Mol. Biol. 286:883-898(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 21-356 IN COMPLEXES WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA, SUBCELLULAR LOCATION.

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

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

Manual assertion based on experiment inⁱ

Ref.2
"New insights into the structure of the reaction centre from Blastochloris viridis: evolution in the laboratory."
Roszak A.W., Moulisova V., Reksodipuro A.D., Gardiner A.T., Fujii R., Hashimoto H., Isaacs N.W., Cogdell R.J.
Biochem. J. 442:27-37(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF WILD-TYPE AND MUTANT PRO-63/MET-97/GLU-104/SER-272/THR-275/MET-297/307-THR-VAL-308/GLN-343 IN COMPLEXES WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA, DIACYLGLYCEROL AT CYS-21, LACK OF PALMITOYLATION AT CYS-21.
Ref.6
"X-ray structure analysis of a membrane protein complex. Electron density map at 3-A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis."
Deisenhofer J., Epp O., Miki K., Huber R., Michel H.
J. Mol. Biol. 180:385-398(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS) IN COMPLEX WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA.
Ref.7
"Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3-A resolution."
Deisenhofer J., Epp O., Miki K., Huber R., Michel H.
Nature 318:618-624(1985)
Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS) IN COMPLEX WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA.
Ref.8
"The coupling of light-induced electron transfer and proton uptake as derived from crystal structures of reaction centres from Rhodopseudomonas viridis modified at the binding site of the secondary quinone, QB."
Lancaster C.R.D., Michel H.
Structure 5:1339-1359(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS)OF 21-356 IN COMPLEXES WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA, SUBCELLULAR LOCATION.
Ref.9
"Refined crystal structures of reaction centres from Rhodopseudomonas viridis in complexes with the herbicide atrazine and two chiral atrazine derivatives also lead to a new model of the bound carotenoid."
Lancaster C.R.D., Michel H.
J. Mol. Biol. 286:883-898(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 21-356 IN COMPLEXES WITH HEME; PHOTOSYNTHETIC REACTION CENTER SUBUNITS PUFL; PUFM AND PUHA, SUBCELLULAR LOCATION.

Protein-protein interaction databases

IntActⁱ	P07173, 3 interactors

IntActⁱ

P07173, 3 interactors

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	45 – 55	Combined sources	11
Beta strandⁱ	69 – 71	Combined sources	3
Helixⁱ	72 – 75	Combined sources	4
Beta strandⁱ	76 – 78	Combined sources	3
Beta strandⁱ	80 – 82	Combined sources	3
Helixⁱ	87 – 101	Combined sources	15
Turnⁱ	103 – 105	Combined sources	3
Helixⁱ	106 – 109	Combined sources	4
Helixⁱ	122 – 140	Combined sources	19
Helixⁱ	142 – 145	Combined sources	4
Turnⁱ	146 – 148	Combined sources	3
Helixⁱ	152 – 156	Combined sources	5
Beta strandⁱ	159 – 161	Combined sources	3
Beta strandⁱ	172 – 175	Combined sources	4
Turnⁱ	182 – 184	Combined sources	3
Beta strandⁱ	185 – 187	Combined sources	3
Helixⁱ	189 – 191	Combined sources	3
Helixⁱ	192 – 197	Combined sources	6
Turnⁱ	198 – 202	Combined sources	5
Helixⁱ	209 – 213	Combined sources	5
Beta strandⁱ	215 – 217	Combined sources	3
Beta strandⁱ	226 – 229	Combined sources	4
Beta strandⁱ	234 – 236	Combined sources	3
Helixⁱ	237 – 239	Combined sources	3
Helixⁱ	244 – 260	Combined sources	17
Helixⁱ	264 – 266	Combined sources	3
Helixⁱ	270 – 272	Combined sources	3
Helixⁱ	282 – 300	Combined sources	19
Helixⁱ	303 – 307	Combined sources	5
Helixⁱ	311 – 313	Combined sources	3
Helixⁱ	325 – 329	Combined sources	5
Beta strandⁱ	332 – 334	Combined sources	3
Helixⁱ	335 – 338	Combined sources	4
Helixⁱ	342 – 344	Combined sources	3
Helixⁱ	346 – 348	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P07173
SMRⁱ	P07173
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P07173

EvolutionaryTraceⁱ

P07173

Family & Domainsⁱ

Keywords - Domainⁱ

Signal

Phylogenomic databases

KEGG Orthology (KO) More...KOⁱ	K13992

KOⁱ

K13992

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd09224 CytoC_RC, 1 hit
Gene3Dⁱ	1.10.468.10, 3 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
Pfam protein domain database More...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

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P07173-1 [UniParc]FASTA Add 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 key	Position(s)	DescriptionActions	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
KEGGⁱ	bvr:BVIR_606
PATRICⁱ	fig\|1079.6.peg.623

Protein	Similar proteins		Species	Score	Length	Source
P07173	Photosynthetic reaction center cytochrome c subunit		BLAVI		318	UniRef100_P07173
UPI0000111133		BLAVI		336
UPI000D18B6C6		BLAVI		333
UPI00004E17F8		BLAVI		332

Protein	Similar proteins		Species	Score	Length	Source
P07173	Photosynthetic reaction center cytochrome c subunit		BLAVI		318	UniRef90_P07173
UPI0000111133		BLAVI		336
UPI000D18B6C6		BLAVI		333
UPI00004E17F8		BLAVI		332
UPI0001895A72		BLAVI		356

Protein	Similar proteins		Species	Score	Length	Source
P07173	Photosynthetic reaction center cytochrome c subunit		BLAVI		318	UniRef50_P07173
UPI0000111133		BLAVI		336
UPI000D18B6C6		BLAVI		333
UPI00004E17F8		BLAVI		332
UPI0001895A72		BLAVI		356

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: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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	[»]
ProteinModelPortalⁱ	P07173
SMRⁱ	P07173
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

IntActⁱ	P07173, 3 interactors

IntActⁱ

P07173, 3 interactors

Chemistry databases

DrugBankⁱ	DB08215 2-T-BUTYLAMINO-4-ETHYLAMINO-6-METHYLTHIO-S-TRIAZINE DB04147 Lauryl Dimethylamine-N-Oxide DB04464 N-Formylmethionine DB08689 UBIQUINONE-1 DB08690 UBIQUINONE-2

DrugBankⁱ

DB08215 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 Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	CUU41065; CUU41065; BVIRIDIS_00500
KEGGⁱ	bvr:BVIR_606
PATRICⁱ	fig\|1079.6.peg.623

Phylogenomic databases

KOⁱ	K13992

KOⁱ

K13992

Miscellaneous databases

EvolutionaryTraceⁱ	P07173

EvolutionaryTraceⁱ

P07173

Family and domain databases

CDDⁱ	cd09224 CytoC_RC, 1 hit
Gene3Dⁱ	1.10.468.10, 3 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...

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:	October 10, 2018
	This is version 132 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P07173 (CYCR_BLAVI)

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Photosynthetic reaction center cytochrome c subunit

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Redox potential

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Sites

Keywords - PTMi

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ