[1]	PROTEIN SEQUENCE. DOI=10.1038/253285a0; PubMed=803642 [NCBI, ExPASy, EBI, Israel, Japan] Ambler R.P., Bartsch R.G.; "Amino acid sequence similarity between cytochrome f from a blue-green bacterium and algal chloroplasts."; Nature 253:285-288(1975).
[2]	X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). DOI=10.1021/bi002679p; PubMed=11478889 [NCBI, ExPASy, EBI, Israel, Japan] Sawaya M.R., Krogmann D.W., Serag A., Ho K.K., Yeates T.O., Kerfeld C.A.; "Structures of cytochrome c-549 and cytochrome c6 from the cyanobacterium Arthrospira maxima."; Biochemistry 40:9215-9225(2001).
[3]	X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS). DOI=10.1107/S0907444902006534; PubMed=12077429 [NCBI, ExPASy, EBI, Israel, Japan] Kerfeld C.A., Sawaya M.R., Krogmann D.W., Yeates T.O.; "Structure of cytochrome c6 from Arthrospira maxima: an assembly of 24 subunits in a nearly symmetric shell."; Acta Crystallogr. D 58:1104-1110(2002).

Comments

FUNCTION: Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis.
BIOPHYSICOCHEMICAL PROPERTIES:

Redox potential: E⁰ is +314 mV;
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Cellular thylakoid lumen (Potential).
PTM: Binds 1 heme group per subunit.
SIMILARITY: Belongs to the cytochrome c family. PetJ subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

PIR

A00110; CCSG6.

3D structure databases

PDB

1F1F; X-ray; 2.70 A; A=1-89.	[ExPASy / RCSB / EBI]
1KIB; X-ray; 3.50 A; A/B/C/D/E/F/G/H=1-89.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1F1F; -.
1KIB; -.

ModBase

P00118.

Ontologies

GO:0031977;	Cellular component: thylakoid lumen (inferred from electronic annotation from UniProtKB-SubCell).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from HAMAP).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0015979;	Biological process: photosynthesis (inferred from electronic annotation from HAMAP).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_00594; -; 1.
PBIL [Tree]

InterPro

IPR009056; Cyt_c_monohaem.
IPR003088; Cyt_CI.
IPR008168; Cyt_CIC.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.760.10; Cytochrome_c_R; 1.

Pfam

PF00034; Cytochrom_C; 1.
Pfam graphical view of domain structure.

PRINTS

PR00605; CYTCHROMECIC.

PROSITE

PS51007; CYTC; 1.
PROSITE graphical view of domain structure (profiles).

Other

ProtoNet

P00118.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding; Photosynthesis; Thylakoid; Transport.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 89`	`89`	`Cytochrome c6.`	`PRO_0000208686`
`METAL`	`18 18`		`Iron (heme axial ligand).`
`METAL`	`62 62`		`Iron (heme axial ligand).`
`BINDING`	`14 14`		`Heme (covalent).`
`BINDING`	`17 17`		`Heme (covalent).`
`HELIX`	`3 13`	`11`
`HELIX`	`15 18`	`4`
`HELIX`	`19 21`	`3`
`STRAND`	`24 26`	`3`
`HELIX`	`33 39`	`7`
`TURN`	`41 45`	`5`
`HELIX`	`47 57`	`11`
`TURN`	`66 68`	`3`
`HELIX`	`71 87`	`17`

Sequence information

Length: 89 AA [This is the length of the unprocessed precursor]

Molecular weight: 9236 Da [This is the MW of the unprocessed precursor]

CRC64: 4796D56B3EA8AF85 [This is a checksum on the sequence]

        10         20         30         40         50         60 
GDVAAGASVF SANCAACHMG GRNVIVANKT LSKSDLAKYL KGFDDDAVAA VAYQVTNGKN 

        70         80 
AMPGFNGRLS PKQIEDVAAY VVDQAEKGW

P00118 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools