P00137 (CYC3_DESAC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytochrome c3

Alternative name(s):
Cytochrome c551.5
Cytochrome c7

Gene names

Name:

cyd

Organism

Desulfuromonas acetoxidans (Chloropseudomonas ethylica)

Taxonomic identifier

891 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Deltaproteobacteria › Desulfuromonadales › Desulfuromonadaceae › Desulfuromonas

Protein attributes

Sequence length	68 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Participates in sulfate respiration coupled with phosphorylation by transferring electrons from the enzyme dehydrogenase to ferredoxin. Ref.4
Post-translational modification	Binds 3 heme groups per subunit.
Biophysicochemical properties	Redox potential: E0 are -140 mV, -210 mV and -240 mV.

Ontologies

Keywords
Biological process	Electron transport Sulfate respiration Transport
Ligand	Heme Iron Metal-binding
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	anaerobic respiration Inferred from electronic annotation. Source: UniProtKB-KW electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 68

68

Cytochrome c3

PRO_0000108364

Sites

Metal binding

17

1

Iron (heme 1 axial ligand)

Metal binding

20

1

Iron (heme 2 axial ligand)

Metal binding

30

1

Iron (heme 1 axial ligand)

Metal binding

45

1

Iron (heme 3 axial ligand)

Metal binding

53

1

Iron (heme 2 axial ligand)

Metal binding

66

1

Iron (heme 3 axial ligand)

Binding site

26

1

Heme 1 (covalent)

Binding site

29

1

Heme 1 (covalent)

Binding site

49

1

Heme 2 (covalent)

Binding site

52

1

Heme 2 (covalent)

Binding site

62

1

Heme 3 (covalent)

Binding site

65

1

Heme 3 (covalent)

Secondary structure

1

.

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68

Helix Strand Turn

Details...

Beta strand

3 – 6

4

Beta strand

9 – 11

3

Beta strand

13 – 16

4

Helix

17 – 24

8

Helix

26 – 28

3

Beta strand

30 – 33

4

Helix

41 – 44

4

Turn

45 – 49

5

Helix

50 – 53

4

Beta strand

56 – 58

3

Helix

62 – 65

4

Sequences

	Sequence		Length	Mass (Da)
	P00137 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 6A54074BF1A5DAB8	FASTA	68	7,262
	10 20 30 40 50 60 ADVVTYENKK GNVTFDHKAH AEKLGCDACH EGTPAKIAID KKSAHKDACK TCHKSNNGPT KCGGCHIK

References

[1]	"The amino acid sequence of cytochrome c551.5 (cytochrome c-7) from the green photosynthetic bacterium Chloropseudomonas ethylica." Ambler R.P. FEBS Lett. 18:351-353(1971) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"The Desulfuromonas acetoxidans triheme cytochrome c7 produced in Desulfovibrio desulfuricans retains its metal reductase activity." Aubert C., Lojou E., Bianco P., Rousset M., Durand M.C., Bruschi M., Dolla A. Appl. Environ. Microbiol. 64:1308-1312(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Assignment of the ligand geometry and redox potentials of the trihaem ferricytochrome c3 from Desulfuromonas acetoxidans." Turner D.L., Costa H.S., Coutinho I.B., Legall J., Xavier A.V. Eur. J. Biochem. 243:474-481(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[4]	"The metal reductase activity of some multiheme cytochromes c: NMR structural characterization of the reduction of chromium(VI) to chromium(III) by cytochrome c7." Assfalg M., Bertini I., Bruschi M., Michel C., Turano P. Proc. Natl. Acad. Sci. U.S.A. 99:9750-9754(2002) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR, FUNCTION AS A METAL REDUCTASE.
[5]	"Structure of cytochrome c7 from Desulfuromonas acetoxidans at 1.9 A resolution." Czjzek M., Arnoux P., Haser R., Shepard W. Acta Crystallogr. D 57:670-678(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[6]	"NMR characterization and solution structure determination of the oxidized cytochrome c7 from Desulfuromonas acetoxidans." Banci L., Bertini I., Bruschi M., Sompornpisut P., Turano P. Proc. Natl. Acad. Sci. U.S.A. 93:14396-14400(1996) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[7]	"800 MHz 1H NMR solution structure refinement of oxidized cytochrome c7 from Desulfuromonas acetoxidans." Assfalg M., Banci L., Bertini I., Bruschi M., Turano P. Eur. J. Biochem. 256:261-270(1998) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[8]	"A proton-NMR investigation of the fully reduced cytochrome c7 from Desulfuromonas acetoxidans: comparison between the reduced and the oxidized forms." Assfalg M., Banci L., Bertini I., Bruschi M., Giudici-Orticoni M.-T., Turano P. Eur. J. Biochem. 266:634-643(1999) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[9]	"A quick solution structure determination of the fully oxidized double mutant K9-10A cytochrome c7 from Desulfuromonas acetoxidans and mechanistic implications." Assfalg M., Bertini I., Turano P., Bruschi M., Durand M.C., Giudici-Orticoni M.-T., Dolla A. J. Biomol. NMR 22:107-122(2002) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF005234 Genomic DNA. Translation: AAC46253.1.

PIR

CCDS7. A00130.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EHJ	NMR	-	A	1-68	[»]
1F22	NMR	-	A	1-68	[»]
1HH5	X-ray	1.90	A	1-68	[»]
1KWJ	NMR	-	A	1-68	[»]
1L3O	NMR	-	A	1-68	[»]
1LM2	NMR	-	A	1-68	[»]
1NEW	NMR	-	A	1-68	[»]

ProteinModelPortal

P00137.

SMR

P00137. Positions 1-68.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR002322. Cyt_c_III.
[Graphical view]

PRINTS

PR00609. CYTOCHROMEC3.

PROSITE

PS51008. MULTIHEME_CYTC. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00137.

Entry information

Entry name

CYC3_DESAC

Accession

Primary (citable) accession number: P00137

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program