[1]	PROTEIN SEQUENCE. DOI=10.1021/bi00834a035; PubMed=5799135 [NCBI, ExPASy, EBI, Israel, Japan] Rall S.C., Bolinger R.E., Cole R.D.; "The amino acid sequence of ferredoxin from Clostridium acidi-urici."; Biochemistry 8:2486-2496(1969).
[2]	SEQUENCE REVISION TO 15; 21; 25 AND 28. STRAIN=ATCC 7906 / CIP 104303 / DSM 604 / NCCB 46094 / 9a; PubMed=8373379 [NCBI, ExPASy, EBI, Israel, Japan] Meyer J., Moulis J.-M., Scherrer N., Gagnon J., Ulrich J.; "Sequences of clostridial ferredoxins: determination of the Clostridium sticklandii sequence and correction of the Clostridium acidurici sequence."; Biochem. J. 294:622-623(1993).
[3]	X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS). DOI=10.1016/0022-2836(94)90041-8; PubMed=7966291 [NCBI, ExPASy, EBI, Israel, Japan] Duee E.D., Fanchon E., Vicat J., Sieker L.C., Meyer J., Moulis J.-M.; "Refined crystal structure of the 2[4Fe-4S] ferredoxin from Clostridium acidurici at 1.84-A resolution."; J. Mol. Biol. 243:683-695(1994).
[4]	X-RAY CRYSTALLOGRAPHY (0.94 ANGSTROMS). DOI=10.1021/bi972155y; PubMed=9405040 [NCBI, ExPASy, EBI, Israel, Japan] Dauter Z., Wilson K.S., Sieker L.C., Meyer J., Moulis J.-M.; "Atomic resolution (0.94 A) structure of Clostridium acidurici ferredoxin. Detailed geometry of [4Fe-4S] clusters in a protein."; Biochemistry 36:16065-16073(1997).

Comments

FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
COFACTOR: Binds 2 4Fe-4S clusters.
SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.

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

S36790; FECLCU.

3D structure databases

PDB

1FCA; X-ray; 1.80 A; A=1-55.	[ExPASy / RCSB / EBI]
1FDN; X-ray; 1.84 A; A=1-55.	[ExPASy / RCSB / EBI]
2FDN; X-ray; 0.94 A; A=1-55.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1FCA; -.
1FDN; -.
2FDN; -.

ModBase

P00198.

Ontologies

GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001450; 4Fe4S_Fe_S_bd.
IPR000813; 7Fe_ferredoxin.
Graphical view of domain structure.

Pfam

PF00037; Fer4; 2.
Pfam graphical view of domain structure.

PRINTS

PR00353; 4FE4SFRDOXIN.
PR00354; 7FE8SFRDOXIN.

PROSITE

PS00198; 4FE4S_FER_1; 2.
PS51379; 4FE4S_FER_2; 2.
PROSITE graphical view of domain structure (profiles).

Other

P00198; -.

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

Keywords

3D-structure; 4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur; Metal-binding; Repeat; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 55`	`55`	`Ferredoxin.`	`PRO_0000159109`
`DOMAIN`	`2 27`	`26`	`4Fe-4S ferredoxin-type 1.`
`DOMAIN`	`28 55`	`28`	`4Fe-4S ferredoxin-type 2.`
`METAL`	`8 8`		`Iron-sulfur 1 (4Fe-4S).`
`METAL`	`11 11`		`Iron-sulfur 1 (4Fe-4S).`
`METAL`	`14 14`		`Iron-sulfur 1 (4Fe-4S).`
`METAL`	`18 18`		`Iron-sulfur 2 (4Fe-4S).`
`METAL`	`37 37`		`Iron-sulfur 2 (4Fe-4S).`
`METAL`	`40 40`		`Iron-sulfur 2 (4Fe-4S).`
`METAL`	`43 43`		`Iron-sulfur 2 (4Fe-4S).`
`METAL`	`47 47`		`Iron-sulfur 1 (4Fe-4S).`
`STRAND`	`2 4`	`3`
`HELIX`	`15 17`	`3`
`STRAND`	`27 29`	`3`
`TURN`	`34 36`	`3`
`HELIX`	`42 45`	`4`
`STRAND`	`52 54`	`3`

Sequence information

Length: 55 AA [This is the length of the unprocessed precursor]

Molecular weight: 5539 Da [This is the MW of the unprocessed precursor]

CRC64: D038C1364A1E97E6 [This is a checksum on the sequence]

        10         20         30         40         50 
AYVINEACIS CGACEPECPV NAISSGDDRY VIDADTCIDC GACAGVCPVD APVQA

P00198 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