P00257 (ADX_BOVIN) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › 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	Essential for the synthesis of various steroid hormones, participates in the reduction of mitochondrial cytochrome P450 for steroidogenesis. Transfers electrons from adrenodoxin reductase to CYP11A1, a cytochrome P450 that catalyzes cholesterol side-chain cleavage By similarity.
Cofactor	Binds 1 2Fe-2S cluster.
Subunit structure	Interacts with CYP11A1 By similarity.
Subcellular location	Mitochondrion matrix.
Sequence similarities	Belongs to the adrenodoxin/putidaredoxin family. Contains 1 2Fe-2S ferredoxin-type domain.

Ontologies

Keywords
Biological process	Cholesterol metabolism Electron transport Lipid metabolism Steroid metabolism Steroidogenesis Sterol metabolism Transport
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW oxidation-reduction process Inferred from direct assay PubMed 15110249. Source: UniProtKB steroid biosynthetic process Traceable author statement PubMed 15110249. Source: UniProtKB
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Traceable author statement PubMed 15110249. Source: UniProtKB
Molecular_function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from direct assay PubMed 15110249. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein C-terminus binding Traceable author statement Ref.12. Source: AgBase protein homodimerization activity Inferred from direct assay Ref.12. Source: AgBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FDXR	P08165	2	EBI-593992,EBI-593948

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 Ref.8

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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186

Helix Strand Turn

Details...

Beta strand

64 – 70

7

Beta strand

72 – 74

3

Beta strand

76 – 82

7

Helix

87 – 93

7

Turn

99 – 104

6

Beta strand

105 – 111

7

Beta strand

114 – 116

3

Helix

119 – 122

4

Helix

130 – 136

7

Beta strand

143 – 145

3

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	FASTA	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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00702556.
IPI00716618.

PIR

AXBO. JX0094.

RefSeq

NP_851354.1. NM_181011.2.

UniGene

Bt.1573.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P00257.

SMR

P00257. Positions 63-175.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00257. 2 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000015660; ENSBTAP00000015660; ENSBTAG00000011793.

GeneID

281157.

KEGG

bta:281157.

Organism-specific databases

CTD

2230.

Phylogenomic databases

eggNOG

COG0633.

GeneTree

ENSGT00530000063577.

HOGENOM

HOG000244518.

HOVERGEN

HBG000092.

InParanoid

P00257.

Gene expression databases

ArrayExpress

P00257.

Family and domain databases

Gene3D

3.10.20.30. 1 hit.

InterPro

IPR001041. 2Fe-2S_ferredoxin-type.
IPR001055. Adrenodoxin.
IPR018298. Adrenodoxin_Fe-S_BS.
IPR012675. Beta-grasp_dom.
[Graphical view]

Pfam

PF00111. Fer2. 1 hit.
[Graphical view]

PRINTS

PR00355. ADRENODOXIN.

SUPFAM

SSF54292. Ferredoxin. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

EvolutionaryTrace

P00257.

NextBio

20805220.

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:	May 1, 2013
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program