Reviewed, UniProtKB/Swiss-Prot P00193 (FER_PEPAS)

Names and origin

Protein names	Recommended name:     Ferredoxin
Organism	Peptostreptococcus asaccharolyticus (Peptococcus asaccharolyticus)
Taxonomic identifier	1258 [NCBI]
Taxonomic lineage	Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiales Family XI. Incertae Sedis › Peptoniphilus

Protein attributes

Sequence length	54 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Cofactor	Binds 2 4Fe-4S clusters.
Sequence similarities	Contains 2 4Fe-4S ferredoxin-type domains.

Ontologies

Keywords
Biological process	Electron transport Transport
Domain	Repeat
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro iron 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 – 54

54

Ferredoxin

PRO_0000159118

Regions

Domain

2 – 25

24

4Fe-4S ferredoxin-type 1

Domain

26 – 54

29

4Fe-4S ferredoxin-type 2

Sites

Metal binding

8

1

Iron-sulfur 1 (4Fe-4S)

Metal binding

11

1

Iron-sulfur 1 (4Fe-4S)

Metal binding

14

1

Iron-sulfur 1 (4Fe-4S)

Metal binding

18

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

35

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

38

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

41

1

Iron-sulfur 2 (4Fe-4S)

Metal binding

45

1

Iron-sulfur 1 (4Fe-4S)

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

54

Helix Strand Turn

Details...

Beta strand

2 – 4

3

Helix

15 – 17

3

Beta strand

25 – 27

3

Turn

32 – 34

3

Helix

40 – 44

5

Beta strand

50 – 52

3

Sequences

	Sequence		Length	Mass (Da)
	P00193-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: C7DCEFA08223CB5D	FASTA	54	5,452
	10 20 30 40 50 AYVINDSCIA CGACKPECPV NIQQGSIYAI DADSCIDCGS CASVCPVGAP NPED

References

[1]	"Non-heme iron proteins. IX. The amino acid sequence of ferredoxin from Micrococcus aerogenes." Tsunoda J.N., Yasunobu K.T., Whiteley H.R. J. Biol. Chem. 243:6262-6272(1968) [PubMed: 5723466] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"Structure of a bacterial ferredoxin." Adman E.T., Sieker L.C., Jensen L.H. J. Biol. Chem. 248:3987-3996(1973) [PubMed: 4708097] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[3]	"Structure of Peptococcus aerogenes ferredoxin. Refinement at 2-A resolution." Adman E.T., Sieker L.C., Jensen L.H. J. Biol. Chem. 251:3801-3806(1976) [PubMed: 932007] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

PIR

FEPE. A00196.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DUR	X-ray	2.00	A	1-54	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR001450. 4Fe4S_Fe_S_bd.
[Graphical view]

Pfam

PF00037. Fer4. 2 hits.
[Graphical view]

PRINTS

PR00353. 4FE4SFRDOXIN.

PROSITE

PS00198. 4FE4S_FER_1. 2 hits.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

FER_PEPAS

Accession

Primary (citable) accession number: P00193

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	November 25, 2008
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)