Reviewed, UniProtKB/Swiss-Prot P00257 (ADX_BOVIN)

Names and origin

Protein names

Recommended name:
    Adrenodoxin, mitochondrial
Alternative name(s):
    Adrenal ferredoxin
    Ferredoxin-1
    Hepato-ferredoxin

Gene names

Name:	FDX1
Synonyms:	ADX

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	186 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	Adrenodoxin transfer electrons from adrenodoxin reductase to the cholesterol side chain cleavage cytochrome P450.
Cofactor	Binds 1 2Fe-2S cluster.
Subcellular location	Mitochondrion matrix.
Sequence similarities	Belongs to the adrenodoxin/putidaredoxin family. Contains 1 2Fe-2S ferredoxin-type domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	2Fe-2S 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 steroid biosynthetic process Traceable author statement. Source: UniProtKB transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: InterPro electron carrier activity Ref.12 Inferred from direct assay. Source: UniProtKB iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein C-terminus binding Ref.12 Traceable author statement. Source: AgBase protein homodimerization activity Ref.12 Inferred from direct assay. Source: AgBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FDXR	P08165	1	EBI-593992,EBI-593948
petH	P21890	1	EBI-593992,EBI-593915	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P00257-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P00257-2)

The sequence of this isoform differs from the canonical sequence as follows:
     24-60: ARPRAGAGGLRGSRGPGLGGGAVATRTLSVSGRAQSS → LKSSQFIKVSCSGSWISAAQRAFICYSKSGNITCFLR

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 58

58

Mitochondrion

Chain

59 – 186

128

Adrenodoxin, mitochondrial

PRO_0000000986

Regions

Domain

65 – 169

105

2Fe-2S ferredoxin-type

Sites

Metal binding

104

1

Iron-sulfur (2Fe-2S)

Metal binding

110

1

Iron-sulfur (2Fe-2S)

Metal binding

113

1

Iron-sulfur (2Fe-2S)

Metal binding

150

1

Iron-sulfur (2Fe-2S)

Natural variations

Alternative sequence

24 – 60

37

ARPRA…RAQSS → LKSSQFIKVSCSGSWISAAQ RAFICYSKSGNITCFLR in isoform 2.

VSP_016558

Experimental info

Sequence conflict

6

1

L → M in AAI09850. Ref.6

Sequence conflict

24

1

A → V in AAA30357. Ref.1

Sequence conflict

62

1

E → Q AA sequence Ref.8

Sequence conflict

130

1

D → N AA sequence Ref.8

Sequence conflict

134

1

D → N AA sequence Ref.8

Secondary structure

1

.

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.

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186

Helix Strand Turn

Details...

Beta strand

65 – 70

6

Beta strand

76 – 81

6

Helix

87 – 93

7

Turn

99 – 104

6

Beta strand

105 – 109

5

Beta strand

114 – 116

3

Helix

119 – 122

4

Helix

130 – 136

7

Beta strand

146 – 148

3

Helix

149 – 151

3

Helix

156 – 158

3

Beta strand

161 – 164

4

Helix

171 – 173

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 1, 1989. Version 2. Checksum: F0F2EE027BFAC371	FASTA	186	19,756
	10 20 30 40 50 60 MAARLLRVAS AALGDTAGRW RLLARPRAGA GGLRGSRGPG LGGGAVATRT LSVSGRAQSS 70 80 90 100 110 120 SEDKITVHFI NRDGETLTTK GKIGDSLLDV VVQNNLDIDG FGACEGTLAC STCHLIFEQH 130 140 150 160 170 180 IFEKLEAITD EENDMLDLAY GLTDRSRLGC QICLTKAMDN MTVRVPDAVS DARESIDMGM NSSKIE
	Isoform 2 [UniParc]. Checksum: 7D3E98D62C9D12D3		186	20,395
	10 20 30 40 50 60 MAARLLRVAS AALGDTAGRW RLLLKSSQFI KVSCSGSWIS AAQRAFICYS KSGNITCFLR 70 80 90 100 110 120 SEDKITVHFI NRDGETLTTK GKIGDSLLDV VVQNNLDIDG FGACEGTLAC STCHLIFEQH 130 140 150 160 170 180 IFEKLEAITD EENDMLDLAY GLTDRSRLGC QICLTKAMDN MTVRVPDAVS DARESIDMGM NSSKIE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and amino acid sequence of the precursor form of bovine adrenodoxin: evidence for a previously unidentified COOH-terminal peptide." Okamura T., John M.E., Zuber M.X., Simpson E.R., Waterman M.R. Proc. Natl. Acad. Sci. U.S.A. 82:5705-5709(1985) [PubMed: 2994043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Multiple species of bovine adrenodoxin mRNA. Occurrence of two different mitochondrial precursor sequences associated with the same mature sequence." Okamura T., Kagimoto M., Simpson E.R., Waterman M.R. J. Biol. Chem. 262:10335-10338(1987) [PubMed: 2440863] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]	"Structural organization of the bovine adrenodoxin gene." Sagara Y., Sawae H., Kimura A., Sagara-Nakano Y., Morohashi K., Miyoshi K., Horiuchi T. J. Biochem. 107:77-83(1990) [PubMed: 2332422] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[4]	"Molecular cloning and nucleotide sequences of bovine hepato-ferredoxin cDNA; identical primary structures of hepato- and adreno-ferredoxins." Matsuo Y., Tomita S., Tsuneoka Y., Furukawa A., Ichikawa Y. Int. J. Biochem. 24:289-295(1992) [PubMed: 1733795] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Liver.
[5]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]	NIH - Mammalian Gene Collection (MGC) project Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: Crossbred X Angus. Tissue: Liver.
[7]	"Transcription of the bovine adrenodoxin gene produces two species of mRNA of which only one is translated into adrenodoxin." Kagimoto M., Kagimoto K., Simpson E.R., Waterman M.R. J. Biol. Chem. 263:8925-8928(1988) [PubMed: 2454231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-102.
[8]	"The amino acid sequence of bovine adrenodoxin." Tanaka M., Haniu M., Yasunobu K.T., Kimura T. J. Biol. Chem. 248:1141-1157(1973) [PubMed: 4686920] [Abstract] Cited for: PROTEIN SEQUENCE OF 59-172 (ISOFORM 1).
[9]	"Isolation and purification of mature bovine adrenocortical ferredoxin with an elongated carboxyl end." Sakihama N., Hiwatashi A., Miyatake A., Shin M., Ichikawa Y. Arch. Biochem. Biophys. 264:23-29(1988) [PubMed: 3395121] [Abstract] Cited for: PROTEIN SEQUENCE OF 171-185.
[10]	"Adrenodoxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis." Mueller J.J., Lapko A., Bourenkov G., Ruckpaul K., Heinemann U. J. Biol. Chem. 276:2786-2789(2001) [PubMed: 11053423] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 59-186 IN COMPLEX WITH ADRENODOXIN REDUCTASE.
[11]	"1H NMR spectra of vertebrate [2Fe-2S] ferredoxins. Hyperfine resonances suggest different electron delocalization patterns from plant ferredoxins." Skjeldal L., Markley J.L., Coghlan V.M., Vickery L.E. Biochemistry 30:9078-9083(1991) [PubMed: 1909889] [Abstract] Cited for: STRUCTURE BY NMR OF 59-186.
[12]	"A new electron transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin." Beilke D., Weiss R., Loehr F., Pristovsek P., Hannemann F., Bernhardt R., Rueterjans H. Biochemistry 41:7969-7978(2002) [PubMed: 12069587] [Abstract] Cited for: STRUCTURE BY NMR OF 59-186.
[13]	"New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-108)." Mueller A., Mueller J.J., Muller Y.A., Uhlmann H., Bernhardt R., Heinemann U. Structure 6:269-280(1998) [PubMed: 9551550] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 63-166.
[14]	"The tertiary structure of full-length bovine adrenodoxin suggests functional dimers." Pikuleva I.A., Tesh K., Waterman M.R., Kim Y. Arch. Biochem. Biophys. 373:44-55(2000) [PubMed: 10620322] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M11746 mRNA. Translation: AAA30357.1.
M16934 mRNA. Translation: AAA30358.1.
D00467 mRNA. Translation: BAA00362.1.
D00471 Genomic DNA. Translation: BAA00363.1.
M19656, M19474 Genomic DNA. Translation: AAA78950.1.
BT030601 mRNA. Translation: ABQ13041.1.
BC109849 mRNA. Translation: AAI09850.1.
S78831 mRNA. Translation: AAB21264.1.

PIR

AXBO. JX0094.

RefSeq

NP_851354.1.

UniGene

Bt.1573

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AYF	X-ray	1.85	A/B	62-166	[»]
1CJE	X-ray	2.50	A/B/C/D	60-186	[»]
1E6E	X-ray	2.30	B/D	60-186	[»]
1L6U	NMR	-	A	59-186	[»]
1L6V	NMR	-	A	59-186	[»]
2BT6	X-ray	1.50	A/B	60-166	[»]
2JQR	NMR	-	B	62-166	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P00257.

Genome annotation databases

Ensembl

ENSBTAG00000011793. Bos taurus. [Contig view]

GeneID

281157.

KEGG

bta:281157.

Phylogenomic databases

HOVERGEN

P00257.

Family and domain databases

InterPro

IPR001055. Adrenodoxin.
IPR012675. b-grasp_ferredoxin-like.
IPR001041. Ferredoxin.
[Graphical view]

Gene3D

G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.

Pfam

PF00111. Fer2. 1 hit.
[Graphical view]

PRINTS

PR00355. ADRENODOXIN.

PROSITE

PS51085. 2FE2S_FER_2. 1 hit.
PS00814. ADX. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ADX_BOVIN

Accession

Primary (citable) accession number: P00257
Secondary accession number(s): A5D9I2 , P08498, P12713, Q32KZ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 1, 1989
Last modified:	November 25, 2008
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)