Reviewed, UniProtKB/Swiss-Prot P0A3C7 (FER1_ANASP)

Names and origin

Protein names

Recommended name:
    Ferredoxin-1
Alternative name(s):
    Ferredoxin I

Gene names

Name:	petF
Synonyms:	fdxV
Ordered Locus Names:	all4148

Organism

Anabaena sp. (strain PCC 7120) [Complete proteome] [HAMAP]

Taxonomic identifier

103690 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Nostoc

Protein attributes

Sequence length	99 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.
Cofactor	Binds 1 2Fe-2S cluster.
Sequence similarities	Belongs to the 2Fe2S plant-type ferredoxin family. Contains 1 2Fe-2S ferredoxin-type domain.
Mass spectrometry	Molecular mass is 10921 Da from positions 2 - 99. Determined by MALDI. Ref.3

Ontologies

Keywords
Biological process	Electron transport Transport
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding
Technical term	3D-structure Complete proteome 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	2 iron, 2 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

Initiator methionine

1

1

Removed By similarity

Chain

2 – 99

98

Ferredoxin-1

PRO_0000189300

Regions

Domain

4 – 96

93

2Fe-2S ferredoxin-type

Sites

Metal binding

42

1

Iron-sulfur (2Fe-2S)

Metal binding

47

1

Iron-sulfur (2Fe-2S)

Metal binding

50

1

Iron-sulfur (2Fe-2S)

Metal binding

80

1

Iron-sulfur (2Fe-2S)

Experimental info

Mutagenesis

43

1

R → A, E or H: No effect on electron transfer.

Mutagenesis

49

1

T → A: No effect on electron transfer.

Mutagenesis

66

1

F → A or I: 1000-fold decrease in electron transfer.

Mutagenesis

69

1

D → K: Small effect on electron transfer.

Mutagenesis

70

1

D → K: Small effect on electron transfer.

Mutagenesis

95

1

E → K: 20000-fold decrease in electron transfer.

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

99

Helix Strand Turn

Details...

Beta strand

3 – 10

8

Turn

11 – 14

4

Beta strand

15 – 22

8

Helix

27 – 33

7

Beta strand

41 – 48

8

Beta strand

51 – 57

7

Helix

69 – 73

5

Beta strand

76 – 78

3

Helix

79 – 81

3

Beta strand

83 – 86

4

Beta strand

88 – 91

4

Helix

95 – 97

3

Sequences

	Sequence		Length	Mass (Da)
	P0A3C7-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 874FD6365346BFFF	FASTA	99	10,830
	10 20 30 40 50 60 MATFKVTLIN EAEGTKHEIE VPDDEYILDA AEEQGYDLPF SCRAGACSTC AGKLVSGTVD 70 80 90 QSDQSFLDDD QIEAGYVLTC VAYPTSDVVI QTHKEEDLY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and sequence of the gene for ferredoxin I from the cyanobacterium Anabaena sp. strain PCC 7120." Alam J., Whitaker R.A., Krogmann D.W., Curtis S.E. J. Bacteriol. 168:1265-1271(1986) [PubMed: 2430949] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120." Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. , Takazawa M., Yamada M., Yasuda M., Tabata S. DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Singh H., Rajaram H., Apte S.K. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 6-16, MASS SPECTROMETRY.
[4]	"Amino acid residues in Anabaena ferredoxin crucial to interaction with ferredoxin-NADP+ reductase: site-directed mutagenesis and laser flash photolysis." Hurley J.K., Salamon Z., Meyer T.E., Fitch J.C., Cusanovich M.A., Markley J.L., Cheng H., Xia B., Chae Y.K., Medina M., Gomez-Moreno C., Tollin G. Biochemistry 32:9346-9354(1993) [PubMed: 8369305] [Abstract] Cited for: MUTAGENESIS.
[5]	"Multinuclear magnetic resonance studies of the 2Fe.2S* ferredoxin from Anabaena species strain PCC 7120. 1. Sequence-specific hydrogen-1 resonance assignments and secondary structure in solution of the oxidized form." Oh B.-H., Markley J.L. Biochemistry 29:3993-4004(1990) [PubMed: 2354171] [Abstract] Cited for: STRUCTURE BY NMR.
[6]	"Multinuclear magnetic resonance studies of the 2Fe.2S* ferredoxin from Anabaena species strain PCC 7120. 2. Sequence-specific carbon-13 and nitrogen-15 resonance assignments of the oxidized form." Oh B.-H., Mooberry E.S., Markley J.L. Biochemistry 29:4004-4011(1990) [PubMed: 2354172] [Abstract] Cited for: STRUCTURE BY NMR.
[7]	"Crystallization and structure determination to 2.5-A resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120." Rypniewski W.R., Breiter D.R., Benning M.M., Wesenberg G., Oh B.-H., Markley J.L., Rayment I., Holden H.M. Biochemistry 30:4126-4131(1991) [PubMed: 1902376] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), IRON-SULFUR CLUSTER-BINDING SITES CYS-42; CYS-47; CYS-50 AND CYS-80.
[8]	"Structure-function relationships in Anabaena ferredoxin: correlations between X-ray crystal structures, reduction potentials, and rate constants of electron transfer to ferredoxin:NADP+ reductase for site-specific ferredoxin mutants." Hurley J.K., Weber-Main A.M., Stankovich M.T., Benning M.M., Thoden J.B., Vanhooke J.L., Holden H.M., Chae Y.K., Xia B., Cheng H., Markley J.L., Martinez-Julvez M., Gomez-Moreno C., Schmeits J.L., Tollin G. Biochemistry 36:11100-11117(1997) [PubMed: 9287153] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M14737 Genomic DNA. Translation: AAA22021.1.
BA000019 Genomic DNA. Translation: BAB75847.1.

PIR

AE2324.
S25233.

RefSeq

NP_488188.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FXA	X-ray	2.50	A/B	2-99	[»]
1J7A	X-ray	1.80	A	2-99	[»]
1J7B	X-ray	1.80	A	2-99	[»]
1J7C	X-ray	1.80	A	2-99	[»]
1QOA	X-ray	1.70	A/B	2-98	[»]
1QOB	X-ray	1.80	A/B	2-99	[»]
1QOF	X-ray	1.80	A/B	2-99	[»]
1QOG	X-ray	1.80	A/B	2-99	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P0A3C7.

Genome annotation databases

GeneID

1107750.

GenomeReviews

Gene locus all4148 in contig BA000019_GR.

KEGG

ana:all4148.

NMPDR

fig|103690.1.peg.4455.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P0A3C7.

OMA

TYKVTLV.

Enzyme and pathway databases

BioCyc

NSP103690:ALL4148-MON.

Family and domain databases

InterPro

IPR006058. 2Fe2S_fd_BS.
IPR012675. b-grasp_ferredoxin-like.
IPR010241. Fdx_pln.
IPR001041. Ferredoxin.
[Graphical view]

Gene3D

G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.

Pfam

PF00111. Fer2. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02008. fdx_plant. 1 hit.

PROSITE

PS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

FER1_ANASP

Accession

Primary (citable) accession number: P0A3C7
Secondary accession number(s): P06543

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 38 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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