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Overview for MACiE Entry M0123

Version history

General Information

EC Number: 1.8.99.2 (A member of the Oxidoreductases, Acting on a sulfur group of donors, With other acceptors)

Enzyme Name: adenylyl-sulfate reductase

Biological Species: Archaeoglobus fulgidus (Archaea)

Catalytic Chain UniprotKB Accession Codes:

Representative PDB Code: 1jnr - STRUCTURE OF ADENYLYLSULFATE REDUCTASE FROM THE HYPERTHERMOPHILICARCHAEOGLOBUS FULGIDUS AT 1.6 RESOLUTION (Resolution = 1.60 Å).

Catalytic CATH Codes:

"Other" CATH Codes:

  • 1.20.58.100 - Methane Monooxygenase Hydroxylase; Chain G, domain 1

Display structure information

Overall Reaction:

Image of double-electron donor

Image of proton

Image of adenylylsulphate

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Image of AMP

Image of sulphite

Image of oxidised donor

double-electron donor
X00054
proton
C00080
CHEBI:24636
adenylylsulphate
C00224
CHEBI:58243
AMP
C00020
CHEBI:456215
sulphite
C00094
CHEBI:17137
oxidised donor
C02177

View similar reactions


Stepwise Description of the Reaction

Step 1A single electron is transferred from the donor, through two iron-sulfur clusters and Trp48B to FAD, with concomitant deprotonation of water.
Step 2A second single electron is transferred from the donor, through two iron-sulfur clusters and Trp48B to FAD forming the N1 anion form of reduced FAD.
Step 3The N5 of FAD initiates a nucleophilic attack on the sulfur of the sulfate group in an addition reaction.
Step 4Water deprotonates the N5 of FAD. One of the oxygen anions of sulfate eliminates the phosphate group.
Step 5The N5 of FAD initiates the elimination of the sulfite with concomitant deprotonation of water.

View similar reactions (composite manual annotation)


Catalytic Residues Involved

Type Number Chain Location of Function
Asn 74 A Side Chain
Main Chain Amide
Glu 141 A Side Chain
Trp 234 A Side Chain
Arg 265 A Side Chain
Asp 361 A Side Chain
His 398 A Side Chain
Ser 449 A Side Chain
Main Chain Amide
Trp 48 B Side Chain

Organic Cofactors for M0123

Type Identity Chain
FAD FAD 1000 A Overview

Metal Cofactors for M0123

Type Het group Number Chain
iron SF4 1110 B Overview
iron SF4 1100 B Overview

References

  1. G. Fritz et al. (2002), Proc. Natl Acad. Sci. USA, 99, 1836-1841. Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6-A resolution.
    Medline: 11842205
  2. A. Schiffer et al. (2006), Biochemistry, 45, 2960-2967. Reaction mechanism of the iron-sulfur flavoenzyme adenosine-5'-phosphosulfate reductase based on the structural characterization of different enzymatic states.
    Medline: 16503650

Homologue information for M0123 (1jnr)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)



Entries with at least one Catalytic CATH code in common (different mechanisms):

MACiE Entry Enzyme Name
EC Number
PDB code CATH code Composite
Reaction Similarity
Catalytic Machinery
Similarity
M0294 succinate dehydrogenase (ubiquinone)
1.3.5.1
1yq4 3.50.50.60
1.20.58.100
0.250.2646Compare
M0020 succinate dehydrogenase
1.3.99.1
1qjd 3.90.700.10
3.50.50.60
0.34610.3045Compare
M0113 sarcosine oxidase
1.5.3.1
2gb0 3.50.50.60
0.31310.0621Compare
M0006 glutathione-disulfide reductase
1.8.1.7
2gh5 3.50.50.60
0.21730.1650Compare
M0131 4-hydroxybenzoate 3-monooxygenase
1.14.13.2
1doc 3.50.50.60
0.0880.0630Compare
M0142 ferredoxin-NADP+ reductase
1.18.1.2
1e6e 3.50.50.60
0.38230.1499Compare

View a comparison of the other reactions in MACiE with the CATH domain 3.50.50.60


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
Link to MetaCyc Link to KEGG Link to BRENDA Link to ExplorENZ

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nucleotide binding (molecular function)
electron carrier activity (molecular function)
oxidoreductase activity (molecular function)
metal ion binding (molecular function)
iron-sulfur cluster binding (molecular function)
4 iron, 4 sulfur cluster binding (molecular function)
oxidation-reduction process (biological process)
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