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PR00355

Identifier
ADRENODOXIN  [View Relations]  [View Alignment]  
Accession
PR00355
No. of Motifs
3
Creation Date
20-FEB-1995  (UPDATE 27-JUN-1999)
Title
Adrenodoxin signature
Database References

PROSITE; PS00814 ADX
BLOCKS; BL00814
INTERPRO; IPR001055
PDB; 1PUT
SCOP; 1PUT
Literature References
1. HANUKOGLU, I.
Steroidogenic enzymes: structure, function, and regulation of expression.
J.STEROID BIOCHEM.MOL.BIOL. 43 770-804 (1992).
 
2. PETERSON, J.A., LORENCE, M.C. AND AMARNEH, B.
Putidaredoxin reductase and putidaredoxin. Cloning, sequence determination,
and heterologous expression of the proteins. 
J.BIOL.CHEM. 265 6066-6073 (1990).
 
3. PETERSON, J.A., LU, J.Y., GEISSELSODER, J., GRAHAM-LORENCE, S., 
CARMONA, C., WITNEY, F. AND LORENCE, M.C.
Cytochrome P-450terp. Isolation and purification of the protein and cloning
and sequencing of its operon. 
J.BIOL.CHEM. 267 14193-14203 (1992).
 
4. POCHAPSKY, T.C., YE, X.M., RATNASWAMY, G. AND LYONS, T.A.
An NMR-derived model for the solution structure of oxidized putidaredoxin,
a 2-Fe, 2-S ferredoxin from Pseudomonas.
BIOCHEMISTRY 33 6424-6432 (1994).
 
5. COGHLAN, V.M. AND VICKERY, L.E.
Electrostatic interactions stabilizing ferredoxin electron transfer 
complexes. Disruption by "conservative" mutations.
J.BIOL.CHEM. 267 8932-8935 (1992).

Documentation
Adrenodoxin, putidaredoxin and terpredoxin are soluble 2Fe-2S iron-sulphur
proteins that act as single electron carriers. In mitochondrial 
monooxygenase systems, adrenodoxin transfers an electron from 
NADPH:adrenodoxin reductase to membrane-bound P450 [1]. In bacteria, 
putidaredoxin and terpredoxin serve as electron carriers between 
corresponding NADH-dependent ferredoxin reductases and soluble P450 [2,3]. 
The exact functions of other members of this family are not known.
 
The 3D structure of putidaredoxin has been solved by NMR [4]. Despite low
sequence similarity between putidaredoxin and 2Fe-2S ferredoxins,
putidaredoxin retains a similar folding topology to structurally 
characterised 2Fe-2S ferredoxins. The fold belongs to the alpha + beta
class, with 3 helices and 6 strands forming a barrel-like structure, and an
extruded loop containing 3 of the 4 cysteinyl residues of the iron-sulphur
cluster.
 
ADRENODOXIN is a 3-element fingerprint that provides a signature for the
adrenodoxins. The fingerprint was derived from an initial alignment of 13
sequences: motif 1 includes the region encoded by PROSITE pattern ADX
(PS00814), the 3 conserved cysteines of which are 2Fe-2S ligands; motif 2
contains a cluster of negatively charged residues, which is essential for
binding both the reductase and P450 [5]; and motif 3 includes the fourth
conserved Cys of the 2Fe-2S cluster. Two iterations on OWL25.1 were
required to reach convergence, at which point a true set comprising 15
sequences was identified. 
 
An update on SPTR37_9f identified a true set of 22 sequences, and 2
partial matches.
Summary Information
  22 codes involving  3 elements
2 codes involving 2 elements
Composite Feature Index
3222222
2202
123
True Positives
ADX1_BOVIN    ADX2_BOVIN    ADXH_DROME    ADX_HUMAN     
ADX_MOUSE ADX_PIG ADX_RAT ADX_SHEEP
FER6_RHOCA FER_BUCAP FER_CAUCR FER_ECOLI
FER_HAEIN FER_PSEAE O49551 O69222
P74283 PUTX_PSEPU Q12184 TERP_PSESP
THCC_RHOSO YDBA_SCHPO
True Positive Partials
Codes involving 2 elements
O07876 P74447
Sequence Titles
ADX1_BOVIN  ADRENODOXIN PRECURSOR 1 (ADRENAL FERREDOXIN) - BOS TAURUS (BOVINE). 
ADX2_BOVIN ADRENODOXIN PRECURSOR 2 (ADRENAL FERREDOXIN) - BOS TAURUS (BOVINE).
ADXH_DROME HYPOTHETICAL ADRENODOXIN-LIKE 10.5 KD PROTEIN IN HSP67BC 3'REGION - DROSOPHILA MELANOGASTER (FRUIT FLY).
ADX_HUMAN ADRENODOXIN PRECURSOR (ADRENAL FERREDOXIN) - HOMO SAPIENS (HUMAN).
ADX_MOUSE ADRENODOXIN PRECURSOR (ADRENAL FERREDOXIN) - MUS MUSCULUS (MOUSE).
ADX_PIG ADRENODOXIN PRECURSOR (ADRENAL FERREDOXIN) - SUS SCROFA (PIG).
ADX_RAT ADRENODOXIN PRECURSOR (ADRENAL FERREDOXIN) - RATTUS NORVEGICUS (RAT).
ADX_SHEEP ADRENODOXIN (ADRENAL FERREDOXIN) - OVIS ARIES (SHEEP).
FER6_RHOCA FERREDOXIN VI (FDVI) - RHODOBACTER CAPSULATUS (RHODOPSEUDOMONAS CAPSULATA).
FER_BUCAP FERREDOXIN, 2FE-2S - BUCHNERA APHIDICOLA.
FER_CAUCR FERREDOXIN, 2FE-2S (FDII) - CAULOBACTER CRESCENTUS.
FER_ECOLI FERREDOXIN, 2FE-2S - ESCHERICHIA COLI.
FER_HAEIN FERREDOXIN, 2FE-2S - HAEMOPHILUS INFLUENZAE.
FER_PSEAE FERREDOXIN, 2FE-2S - PSEUDOMONAS AERUGINOSA.
O49551 ADRENODOXIN - LIKE PROTEIN - ARABIDOPSIS THALIANA (MOUSE-EAR CRESS).
O69222 FERREDOXIN - AZOTOBACTER VINELANDII.
P74283 HYDROGENASE COMPONENT - SYNECHOCYSTIS SP. (STRAIN PCC 6803).
PUTX_PSEPU PUTIDAREDOXIN (PDX) - PSEUDOMONAS PUTIDA.
Q12184 ORF YPL252C - SACCHAROMYCES CEREVISIAE (BAKER'S YEAST).
TERP_PSESP TERPREDOXIN - PSEUDOMONAS SP.
THCC_RHOSO RHODOCOXIN - RHODOCOCCUS SP. (STRAIN NI86/21).
YDBA_SCHPO HYPOTHETICAL 70.2 KD PROTEIN C22E12.10C IN CHROMOSOME I - SCHIZOSACCHAROMYCES POMBE (FISSION YEAST).

O07876 FERREDOXIN - SPHINGOMONAS SP.
P74447 HYPOTHETICAL 20.6 KD PROTEIN - SYNECHOCYSTIS SP. (STRAIN PCC 6803).
Scan History
OWL25_1    2  100  NSINGLE    
SPTR37_9f 4 50 NSINGLE
Initial Motifs
Motif 1  width=11
Element Seqn Id St Int Rpt
CGGSASCATCH PUTX_PSEPU 39 39 -
CGGSCVCATCR TERP_PSESP 39 39 -
CEGTLACSTCH ADX_CHICK 65 65 -
CEGTLACSTCH ADX_SHEEP 40 40 -
CEGTLACSTCH ADX_PIG 46 46 -
CEGTLACSTCH ADX2_BOVIN 104 104 -
CEGTLACSTCH ADX1_BOVIN 104 104 -
CEGTLACSTCH ADX_HUMAN 106 106 -
CEGTLACSTCH ADX_RAT 110 110 -
CEKSCACTTCH FER_ECOLI 41 41 -
CEASLACTTCH ADXH_DROME 5 5 -
CGGACACSTCH FER6_RHOCA 39 39 -
CGGACACATCH FER_CAUCR 40 40 -

Motif 2 width=15
Element Seqn Id St Int Rpt
EKLDAITDEENDMLD ADX_HUMAN 125 8 -
EKLDAITDEEMDMLD ADX_CHICK 84 8 -
EKLEAITDEENDMLD ADX_SHEEP 59 8 -
EKLEAITDEENDMLD ADX_PIG 65 8 -
EKLEAITDEENDMLD ADX2_BOVIN 123 8 -
EKLEAITDEENDMLD ADX1_BOVIN 123 8 -
EKLDAITDEENDMLD ADX_RAT 129 8 -
DSLPESSEQEDDMLD FER_ECOLI 59 7 -
QKLKEAEEQEDDLLD ADXH_DROME 24 8 -
DKLPKALPTETDMID FER6_RHOCA 58 8 -
DKTGDKSAMEESMLD FER_CAUCR 59 8 -
DKVPAANEREIGMLE PUTX_PSEPU 58 8 -
EIVGEANPDENDLLQ TERP_PSESP 58 8 -

Motif 3 width=9
Element Seqn Id St Int Rpt
TRLSCQVFI TERP_PSESP 82 9 -
SRLGCQICL ADX_SHEEP 82 8 -
SRLGCQICL ADX_PIG 88 8 -
SRLGCQICL ADX2_BOVIN 146 8 -
SRLGCQICL ADX1_BOVIN 146 8 -
SRLGCQICL ADX_HUMAN 148 8 -
SRLGCQICL ADX_CHICK 107 8 -
SRLGCQVCL ADX_RAT 152 8 -
SRLSCQARV FER_ECOLI 82 8 -
SRLGCQILL ADXH_DROME 47 8 -
SRLTCQIKV FER6_RHOCA 82 9 -
SRLSCQIKV FER_CAUCR 82 8 -
SRLCCQIIM PUTX_PSEPU 82 9 -
Final Motifs
Motif 1  width=11
Element Seqn Id St Int Rpt
CEGTLACSTCH ADX_SHEEP 40 40 -
CEGTLACSTCH ADX_PIG 46 46 -
CEGTLACSTCH ADX2_BOVIN 104 104 -
CEGTLACSTCH ADX1_BOVIN 104 104 -
CEGTLACSTCH ADX_HUMAN 106 106 -
CEGTLACSTCH ADX_MOUSE 110 110 -
CEGTLACSTCH ADX_RAT 110 110 -
CEGSLACSTCH O49551 75 75 -
CGGSCACSTCH Q12184 98 98 -
CEGSVACSTCH YDBA_SCHPO 556 556 -
CEKSCACTTCH FER_ECOLI 41 41 -
CDGSCACTTCH FER_HAEIN 41 41 -
CEMSCACTTCH O69222 43 43 -
CEASLACTTCH ADXH_DROME 5 5 -
CEKSCACTTCH FER_PSEAE 44 44 -
CGGACACSTCH FER6_RHOCA 39 39 -
CEKSCACSTCH FER_BUCAP 42 42 -
CGGACACATCH FER_CAUCR 40 40 -
CGGQAMCATCH THCC_RHOSO 39 39 -
CGGSASCATCH PUTX_PSEPU 39 39 -
CGGSCVCATCR TERP_PSESP 39 39 -
CGGYGQCGTCI P74283 41 41 -

Motif 2 width=15
Element Seqn Id St Int Rpt
EKLEAITDEENDMLD ADX_SHEEP 59 8 -
EKLEAITDEENDMLD ADX_PIG 65 8 -
EKLEAITDEENDMLD ADX2_BOVIN 123 8 -
EKLEAITDEENDMLD ADX1_BOVIN 123 8 -
EKLDAITDEENDMLD ADX_HUMAN 125 8 -
EKLDAITDEENDMLD ADX_MOUSE 129 8 -
EKLDAITDEENDMLD ADX_RAT 129 8 -
NKLEEPTDEENDMLD O49551 95 9 -
DALPEPEDDENDMLD Q12184 117 8 -
ELLDPPEEDEEDMLD YDBA_SCHPO 575 8 -
DSLPESSEQEDDMLD FER_ECOLI 59 7 -
DSLNETSDQEEDMLD FER_HAEIN 59 7 -
DSLEPSDELEDDMLD O69222 61 7 -
QKLKEAEEQEDDLLD ADXH_DROME 24 8 -
DSMEPSDELEDDMLD FER_PSEAE 62 7 -
DKLPKALPTETDMID FER6_RHOCA 58 8 -
LSLSGWSEKEEDVLD FER_BUCAP 60 7 -
DKTGDKSAMEESMLD FER_CAUCR 59 8 -
DKFPSISEEEDEMLD THCC_RHOSO 58 8 -
DKVPAANEREIGMLE PUTX_PSEPU 58 8 -
EIVGEANPDENDLLQ TERP_PSESP 58 8 -
ENLSPKTDFENRVLR P74283 59 7 -

Motif 3 width=9
Element Seqn Id St Int Rpt
SRLGCQICL ADX_SHEEP 82 8 -
SRLGCQICL ADX_PIG 88 8 -
SRLGCQICL ADX2_BOVIN 146 8 -
SRLGCQICL ADX1_BOVIN 146 8 -
SRLGCQICL ADX_HUMAN 148 8 -
SRLGCQVCL ADX_MOUSE 152 8 -
SRLGCQVCL ADX_RAT 152 8 -
SRLGCQVIA O49551 118 8 -
SRLGCQIKM Q12184 140 8 -
SRLGCQVLL YDBA_SCHPO 598 8 -
SRLSCQARV FER_ECOLI 82 8 -
SRLSCQCVV FER_HAEIN 82 8 -
SRLSCQARV O69222 84 8 -
SRLGCQILL ADXH_DROME 47 8 -
SRLSCQAVV FER_PSEAE 85 8 -
SRLTCQIKV FER6_RHOCA 82 9 -
SRLSCQAII FER_BUCAP 83 8 -
SRLSCQIKV FER_CAUCR 82 8 -
SRLSCQLVV THCC_RHOSO 82 9 -
SRLCCQIIM PUTX_PSEPU 82 9 -
TRLSCQVFI TERP_PSESP 82 9 -
FRLACQTLV P74283 79 5 -