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P00257

- ADX_BOVIN

UniProt

P00257 - ADX_BOVIN

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Protein

Adrenodoxin, mitochondrial

Gene

FDX1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Cofactori

[2Fe-2S] clusterNote: Binds 1 [2Fe-2S] cluster.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi104 – 1041Iron-sulfur (2Fe-2S)
Metal bindingi110 – 1101Iron-sulfur (2Fe-2S)
Metal bindingi113 – 1131Iron-sulfur (2Fe-2S)
Metal bindingi150 – 1501Iron-sulfur (2Fe-2S)

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB
  2. electron carrier activity Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. protein C-terminus binding Source: AgBase
  5. protein homodimerization activity Source: AgBase

GO - Biological processi

  1. cholesterol metabolic process Source: UniProtKB
  2. hormone biosynthetic process Source: UniProtKB
  3. oxidation-reduction process Source: UniProtKB
  4. steroid biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cholesterol metabolism, Electron transport, Lipid metabolism, Steroid metabolism, Steroidogenesis, Sterol metabolism, Transport

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_209020. Endogenous sterols.
REACT_211020. Pregnenolone biosynthesis.
REACT_215986. Mitochondrial iron-sulfur cluster biogenesis.
REACT_224048. Electron transport from NADPH to Ferredoxin.

Names & Taxonomyi

Protein namesi
Recommended name:
Adrenodoxin, mitochondrial
Alternative name(s):
Adrenal ferredoxin
Ferredoxin-1
Hepato-ferredoxin
Gene namesi
Name:FDX1
Synonyms:ADX
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 15

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5858MitochondrionAdd
BLAST
Chaini59 – 186128Adrenodoxin, mitochondrialPRO_0000000986Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641N6-acetyllysine; alternateBy similarity
Modified residuei64 – 641N6-succinyllysine; alternateBy similarity
Modified residuei156 – 1561N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Expressioni

Gene expression databases

ExpressionAtlasiP00257. baseline.

Interactioni

Subunit structurei

Interacts with CYP11A1.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
FDXRP081652EBI-593992,EBI-593948

Protein-protein interaction databases

IntActiP00257. 2 interactions.

Structurei

Secondary structure

1
186
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi64 – 707Combined sources
Beta strandi72 – 743Combined sources
Beta strandi76 – 827Combined sources
Helixi87 – 937Combined sources
Turni99 – 1046Combined sources
Beta strandi105 – 1117Combined sources
Beta strandi114 – 1163Combined sources
Helixi119 – 1224Combined sources
Helixi130 – 1367Combined sources
Beta strandi143 – 1453Combined sources
Beta strandi146 – 1483Combined sources
Helixi149 – 1513Combined sources
Helixi156 – 1583Combined sources
Beta strandi161 – 1644Combined sources
Helixi171 – 1733Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AYFX-ray1.85A/B62-166[»]
1CJEX-ray2.50A/B/C/D60-186[»]
1E6EX-ray2.30B/D59-186[»]
1L6UNMR-A59-186[»]
1L6VNMR-A59-186[»]
2BT6X-ray1.50A/B63-166[»]
2JQRNMR-B62-166[»]
ProteinModelPortaliP00257.
SMRiP00257. Positions 63-175.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00257.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 1691052Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the adrenodoxin/putidaredoxin family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0633.
GeneTreeiENSGT00530000063577.
HOGENOMiHOG000244518.
HOVERGENiHBG000092.
InParanoidiP00257.
OMAiLLMTIQC.
TreeFamiTF319845.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR001055. Adrenodoxin.
IPR018298. Adrenodoxin_Fe-S_BS.
IPR012675. Beta-grasp_dom.
[Graphical view]
PfamiPF00111. Fer2. 1 hit.
[Graphical view]
PRINTSiPR00355. ADRENODOXIN.
SUPFAMiSSF54292. SSF54292. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
PS00814. ADX. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P00257-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAARLLRVAS AALGDTAGRW RLLARPRAGA GGLRGSRGPG LGGGAVATRT
60 70 80 90 100
LSVSGRAQSS SEDKITVHFI NRDGETLTTK GKIGDSLLDV VVQNNLDIDG
110 120 130 140 150
FGACEGTLAC STCHLIFEQH IFEKLEAITD EENDMLDLAY GLTDRSRLGC
160 170 180
QICLTKAMDN MTVRVPDAVS DARESIDMGM NSSKIE
Length:186
Mass (Da):19,756
Last modified:July 1, 1989 - v2
Checksum:iF0F2EE027BFAC371
GO
Isoform 2 (identifier: P00257-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:186
Mass (Da):20,395
Checksum:i7D3E98D62C9D12D3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61L → M in AAI09850. 1 PublicationCurated
Sequence conflicti24 – 241A → V in AAA30357. (PubMed:2994043)Curated
Sequence conflicti62 – 621E → Q AA sequence (PubMed:4686920)Curated
Sequence conflicti130 – 1301D → N AA sequence (PubMed:4686920)Curated
Sequence conflicti134 – 1341D → N AA sequence (PubMed:4686920)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei24 – 6037ARPRA…RAQSS → LKSSQFIKVSCSGSWISAAQ RAFICYSKSGNITCFLR in isoform 2. 1 PublicationVSP_016558Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiJX0094. AXBO.
RefSeqiNP_851354.1. NM_181011.2. [P00257-2]
UniGeneiBt.1573.

Genome annotation databases

EnsembliENSBTAT00000015660; ENSBTAP00000015660; ENSBTAG00000011793. [P00257-1]
GeneIDi281157.
KEGGibta:281157.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi JX0094. AXBO.
RefSeqi NP_851354.1. NM_181011.2. [P00257-2 ]
UniGenei Bt.1573.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 59-186 [» ]
1L6U NMR - A 59-186 [» ]
1L6V NMR - A 59-186 [» ]
2BT6 X-ray 1.50 A/B 63-166 [» ]
2JQR NMR - B 62-166 [» ]
ProteinModelPortali P00257.
SMRi P00257. Positions 63-175.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P00257. 2 interactions.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000015660 ; ENSBTAP00000015660 ; ENSBTAG00000011793 . [P00257-1 ]
GeneIDi 281157.
KEGGi bta:281157.

Organism-specific databases

CTDi 2230.

Phylogenomic databases

eggNOGi COG0633.
GeneTreei ENSGT00530000063577.
HOGENOMi HOG000244518.
HOVERGENi HBG000092.
InParanoidi P00257.
OMAi LLMTIQC.
TreeFami TF319845.

Enzyme and pathway databases

Reactomei REACT_209020. Endogenous sterols.
REACT_211020. Pregnenolone biosynthesis.
REACT_215986. Mitochondrial iron-sulfur cluster biogenesis.
REACT_224048. Electron transport from NADPH to Ferredoxin.

Miscellaneous databases

EvolutionaryTracei P00257.
NextBioi 20805220.

Gene expression databases

ExpressionAtlasi P00257. baseline.

Family and domain databases

Gene3Di 3.10.20.30. 1 hit.
InterProi IPR001041. 2Fe-2S_ferredoxin-type.
IPR001055. Adrenodoxin.
IPR018298. Adrenodoxin_Fe-S_BS.
IPR012675. Beta-grasp_dom.
[Graphical view ]
Pfami PF00111. Fer2. 1 hit.
[Graphical view ]
PRINTSi PR00355. ADRENODOXIN.
SUPFAMi SSF54292. SSF54292. 1 hit.
PROSITEi PS51085. 2FE2S_FER_2. 1 hit.
PS00814. ADX. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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).

Entry informationi

Entry nameiADX_BOVIN
AccessioniPrimary (citable) accession number: P00257
Secondary accession number(s): A5D9I2
, P08498, P12713, Q32KZ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: November 26, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3