P00214 (FER1_AZOVI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ferredoxin-1

Alternative name(s):
Ferredoxin I
Short name=FdI

Gene names

Name:

fdxA

Organism

Azotobacter vinelandii

Taxonomic identifier

354 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Azotobacter group › Azotobacter

Protein attributes

Sequence length	107 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. This ferredoxin could play a role in regulating gene expression by interacting directly with DNA.
Cofactor	Binds 1 4Fe-4S cluster. Binds 1 3Fe-4S cluster.
Sequence similarities	Contains 2 4Fe-4S ferredoxin-type domains.
Biophysicochemical properties	Redox potential: E0 is -450 mV for the 3Fe-4S, and -645 mV for the 4Fe-4S clusters.

Ontologies

Keywords
Biological process	Electron transport Transport
Domain	Repeat
Ligand	3Fe-4S 4Fe-4S DNA-binding 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
Molecular_function	3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity 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

Initiator methionine

1

1

Removed Ref.3

Chain

2 – 107

106

Ferredoxin-1

PRO_0000159095

Regions

Domain

2 – 30

29

4Fe-4S ferredoxin-type 1

Domain

31 – 60

30

4Fe-4S ferredoxin-type 2

Sites

Metal binding

9

1

Iron-sulfur 1 (3Fe-4S) Ref.5

Metal binding

17

1

Iron-sulfur 1 (3Fe-4S) Ref.5

Metal binding

21

1

Iron-sulfur 2 (4Fe-4S) Ref.5

Metal binding

40

1

Iron-sulfur 2 (4Fe-4S) Ref.5

Metal binding

43

1

Iron-sulfur 2 (4Fe-4S) Ref.5

Metal binding

46

1

Iron-sulfur 2 (4Fe-4S) Ref.5

Metal binding

50

1

Iron-sulfur 1 (3Fe-4S) Ref.5

Experimental info

Sequence conflict

49

1

E → R in AAA16869. Ref.2

Sequence conflict

53

1

Q → E AA sequence Ref.3

Secondary structure

1

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107

Helix Strand Turn

Details...

Beta strand

3 – 5

3

Helix

7 – 9

3

Turn

10 – 12

3

Helix

16 – 20

5

Beta strand

22 – 24

3

Beta strand

26 – 28

3

Beta strand

33 – 35

3

Turn

37 – 39

3

Helix

47 – 49

3

Beta strand

55 – 57

3

Helix

58 – 60

3

Helix

63 – 66

4

Helix

67 – 75

9

Turn

76 – 78

3

Helix

92 – 95

4

Helix

101 – 104

4

Sequences

	Sequence		Length	Mass (Da)
	P00214 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 3B4B0D1A55765B2B	FASTA	107	12,182
	10 20 30 40 50 60 MAFVVTDNCI KCKYTDCVEV CPVDCFYEGP NFLVIHPDEC IDCALCEPEC PAQAIFSEDE 70 80 90 100 VPEDMQEFIQ LNAELAEVWP NITEKKDPLP DAEDWDGVKG KLQHLER

References

[1]	"Azotobacter vinelandii ferredoxin I: cloning, sequencing, and mutant analysis." Morgan T.V., Lundell D.J., Burgess B.K. J. Biol. Chem. 263:1370-1375(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Azotobacter vinelandii mutS: nucleotide sequence and mutant analysis." Le O., Shen B., Iismaa S.E., Burgess B.K. J. Bacteriol. 175:7707-7710(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW.
[3]	"Structure of Azotobacter vinelandii 7Fe ferredoxin. Amino acid sequence and electron density maps of residues." Howard J.B., Lorsbach T.W., Ghosh D., Melis K., Stout C.D. J. Biol. Chem. 258:508-522(1983) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-107, X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS).
[4]	"Iron-sulfur clusters and protein structure of Azotobacter ferredoxin at 2.0-A resolution." Ghosh D., O'Donnell S., Furey W.F. Jr., Robbins A.H., Stout C.D. J. Mol. Biol. 158:73-109(1982) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS).
[5]	"Structure of ferredoxin I from Azotobacter vinelandii." Stout G.H., Turley S., Sieker L.C., Jensen L.H. Proc. Natl. Acad. Sci. U.S.A. 85:1020-1022(1988) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
[6]	"Refinement of the 7 Fe ferredoxin from Azotobacter vinelandii at 1.9-A resolution." Stout G.H. J. Mol. Biol. 205:545-555(1989) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[7]	"Structure at pH 6.5 of ferredoxin I from Azotobacter vinelandii at 2.3-A resolution." Merritt E.A., Stout G.H., Turley S., Sieker L.C., Jensen L.H., Orme-Johnson W.H. Acta Crystallogr. D 49:272-281(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[8]	"Structure of Azotobacter vinelandii 7Fe ferredoxin at 1.35-A resolution and determination of the [Fe-S] bonds with 0.01-A accuracy." Stout C.D., Stura E.A., McRee D.E. J. Mol. Biol. 278:629-639(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
[9]	"Oxidized and reduced Azotobacter vinelandii ferredoxin I at 1.4-A resolution: conformational change of surface residues without significant change in the [3Fe-4S]+/0 cluster." Schipke C.G., Goodin D.B., McRee D.E., Stout C.D. Biochemistry 38:8228-8239(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
[10]	"Alteration of the reduction potential of the [4Fe-4S](2+/+) cluster of Azotobacter vinelandii ferredoxin I." Chen K., Tilley G.J., Sridhar V., Prasad G.S., Stout C.D., Armstrong F.A., Burgess B.K. J. Biol. Chem. 274:36479-36487(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[11]	"Does ferredoxin I (Azotobacter) represent a novel class of DNA-binding proteins that regulate gene expression in response to cellular iron(II)?" Thomson A.J. FEBS Lett. 285:230-236(1991) [PubMed] [Europe PMC] [Abstract] Cited for: DNA-BINDING.
[12]	"Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: [Fe-S] cluster-driven protein rearrangement." Martin A.E., Burgess B.K., Stout C.D., Cash V.L., Dean D.R., Jensen G.M., Stephens P.J. Proc. Natl. Acad. Sci. U.S.A. 87:598-602(1990) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS.
[13]	"Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I. Changes in [4Fe-4S] cluster reduction potential and reactivity." Iismaa S.E., Vazquez A.E., Jensen G.M., Stephens P.J., Butt J.N., Armstrong F.A., Burgess B.K. J. Biol. Chem. 266:21563-21571(1991) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS.
[14]	"Azotobacter vinelandii ferredoxin I. Alteration of individual surface charges and the [4FE-4S]2+/+ cluster reduction potential." Shen B., Jollie D.R., Stout C.D., Diller T.C., Armstrong F.A., Gorst C.M., la Mar G.N., Stephen P.J., Burgess B.K. J. Biol. Chem. 269:8564-8575(1994) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J03521 Genomic DNA. Translation: AAA22125.1.
M63007 Unassigned DNA. Translation: AAA16869.1.

PIR

FEAV. A29936.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A6L	X-ray	2.10	A	2-106	[»]
1AXQ	X-ray	2.10	A	2-106	[»]
1B0T	X-ray	2.10	A	2-107	[»]
1B0V	X-ray	2.80	A/B/C/D	2-107	[»]
1D3W	X-ray	1.70	A	2-107	[»]
1F5B	X-ray	1.62	A	4-106	[»]
1F5C	X-ray	1.75	A	2-106	[»]
1FD2	X-ray	1.90	A	2-107	[»]
1FDA	X-ray	2.10	A	2-106	[»]
1FDB	X-ray	2.20	A	2-106	[»]
1FDD	X-ray	1.90	A	2-106	[»]
1FER	X-ray	2.30	A	2-107	[»]
1FF2	X-ray	2.30	A	2-106	[»]
1FRH	X-ray	2.30	A	4-107	[»]
1FRI	X-ray	2.10	A	2-107	[»]
1FRJ	X-ray	2.30	A	2-107	[»]
1FRK	X-ray	2.10	A	2-107	[»]
1FRL	X-ray	2.30	A	2-107	[»]
1FRM	X-ray	2.30	A	2-107	[»]
1FRX	X-ray	2.50	A	2-106	[»]
1FTC	X-ray	2.35	A/B	2-106	[»]
1G3O	X-ray	1.65	A	2-106	[»]
1G6B	X-ray	1.90	A	2-106	[»]
1GAO	X-ray	2.20	A/B/C/D	2-106	[»]
1PC4	X-ray	1.65	A	1-107	[»]
1PC5	X-ray	1.80	A	1-107	[»]
2FD2	X-ray	1.90	A	2-106	[»]
5FD1	X-ray	1.90	A	2-106	[»]
6FD1	X-ray	1.35	A	2-107	[»]
6FDR	X-ray	1.40	A	2-107	[»]
7FD1	X-ray	1.30	A	2-107	[»]
7FDR	X-ray	1.40	A	2-107	[»]

ProteinModelPortal

P00214.

SMR

P00214. Positions 2-107.

ModBase

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Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR000813. 7Fe_ferredoxin.
IPR022569. Fd_C.
[Graphical view]

Pfam

PF11953. DUF3470. 1 hit.
PF13237. Fer4_10. 1 hit.
[Graphical view]

PRINTS

PR00354. 7FE8SFRDOXIN.

PROSITE

PS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00214.

Entry information

Entry name

FER1_AZOVI

Accession

Primary (citable) accession number: P00214

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program