EzCatDB: M00164

DB codeM00164
CATH domainDomain 1-.-.-.-
Domain 22.40.30.10
Domain 31.20.990.10
Domain 43.40.50.80
Domain 5-.-.-.-
Domain 63.30.413.10Catalytic domain
Domain 73.90.480.10Catalytic domain
Domain 83.30.413.10Catalytic domain
E.C.1.8.1.2
CSA1aop

CATH domainRelated DB codes (homologues)
1.20.990.10M00006
2.40.30.10D00043,M00006,M00141,M00159
3.40.50.80D00043,M00006,M00141,M00159

Enzyme Name
Swiss-protKEGG

P38038P17846
Protein nameSulfite reductase [NADPH] flavoprotein alpha-componentSulfite reductase [NADPH] hemoprotein beta-componentsulfite reductase (NADPH)
sulfite (reduced nicotinamide adenine dinucleotide phosphate)reductase
NADPH-sulfite reductase
NADPH-dependent sulfite reductase
H2S-NADP oxidoreductase
sulfite reductase (NADPH2)
SynonymsSIR-FP
EC 1.8.1.2
SIR-HP
SIRHP
EC 1.8.1.2

KEGG pathways
MAP codePathways
MAP00920Sulfur metabolism

Swiss-prot:Accession NumberP38038P17846
Entry nameCYSJ_ECOLICYSI_ECOLI
ActivityH(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 NADPH.H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 NADPH.
SubunitAlpha(8)-beta(8). The alpha component is a flavoprotein, the beta component is a hemoprotein.Alpha(8)-beta(4). The alpha component is a flavoprotein, the beta component is a hemoprotein.
Subcellular location

CofactorBinds 1 FAD per subunit.,Binds 1 FMN per subunit.Binds 1 siroheme per subunit.,Binds 1 4Fe-4S cluster per subunit.


CofactorsSubstratesProductsintermediates
KEGG-idL00024C00748C00016C00061C00094C00005C00080C00283C00006C00001
Compound[4Fe-4S]SirohemeFADFMNSulfiteNADPHH+Hydrogen sulfideNADP+H2O
Typeheavy metal,sulfide grouparomatic ring (with nitrogen atoms),carboxyl group,heavy metalamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotideamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,phosphate group/phosphate ionsulfiteamide group,amine group,nucleotideotherssulfhydryl groupamide group,amine group,nucleotideH2O
1ddgA01UnboundUnboundBound:FADUnboundUnboundUnbound
UnboundUnbound
Unbound
1ddgB01UnboundUnboundBound:FADUnboundUnboundUnbound
UnboundUnbound
Unbound
1ddiA01UnboundUnboundBound:FADUnboundUnboundUnbound
UnboundUnbound
Unbound
1ddgA02UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
1ddgB02UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
1ddiA02UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
1ddgA03UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
1ddgB03UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
1ddiA03UnboundUnboundUnboundUnboundUnboundBound:NAP
UnboundUnbound
Unbound
1aopA01UnboundUnboundUnboundUnboundAnalogue:PO4Unbound
UnboundUnbound
Unbound
1geoA01UnboundUnboundUnboundUnboundAnalogue:PO4Unbound
UnboundUnbound
Unbound
1gepA01UnboundUnboundUnboundUnboundBound:SO3Unbound
UnboundUnbound
Unbound
2aopA01UnboundUnboundUnboundUnboundAnalogue:PO4Unbound
UnboundUnbound
Unbound
2gepA01UnboundUnboundUnboundUnboundBound:SO3Unbound
UnboundUnbound
Unbound
3aopA01UnboundUnboundUnboundUnboundAnalogue:PO4Unbound
UnboundUnbound
Unbound
3geoA01UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Intermediate-bound:NO2
4aopA01UnboundUnboundUnboundUnboundAnalogue:PO4Unbound
UnboundUnbound
Unbound
4gepA01UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Intermediate-analogue:CYN
5aopA01UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
5gepA01UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Intermediate-analogue:CMO
6gepA01UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Intermediate-analogue:_NO
7gepA01UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Intermediate-bound:_SX
8gepA01UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
1aopA02UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
1geoA02UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
1gepA02UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
2aopA02UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
2gepA02UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
3aopA02UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
3geoA02UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
4aopA02UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
4gepA02UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
5aopA02UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
5gepA02UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
6gepA02UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
7gepA02UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
8gepA02UnboundUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
1aopA03Bound:SF4Bound:SRM-PO4UnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
1geoA03Bound:FS4Bound:SRM-PO4UnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
1gepA03Bound:FS4Bound:SRM-SO3UnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
2aopA03Bound:SF4Bound:SRM-PO4UnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
2gepA03Bound:SF4Bound:SRM-SO3UnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
3aopA03Bound:SF4Bound:SRM-PO4UnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
3geoA03Bound:SF4Bound:SRM-NO2UnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
4aopA03Bound:SF4Bound:SRM-PO4UnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
4gepA03Bound:SF4Bound:SRM-CYNUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
5aopA03Bound:SF4Bound:SRMUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
5gepA03Bound:SF4Bound:SRM-CMOUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
6gepA03Bound:SF4Bound:SRM-_NOUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
7gepA03Bound:SF4Bound:SRM-_SXUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound
8gepA03Bound:SF4Bound:SRMUnboundUnboundUnboundUnbound
UnboundUnbound
Unbound

Active-site residues
resource
Swiss-prot;P17846 & PDB;1aop & literature [14], [15]
pdbCatalytic residuesCofactor-binding residues
1ddgA01

1ddgB01

1ddiA01

1ddgA02

1ddgB02

1ddiA02

1ddgA03

1ddgB03

1ddiA03

1aopA01ARG 153;LYS 215;LYS 217

1geoA01ARG 153;LYS 215;LYS 217

1gepA01ARG 153;LYS 215;LYS 217

2aopA01ARG 153;LYS 215;LYS 217

2gepA01ARG 153;LYS 215;LYS 217

3aopA01ARG 153;LYS 215;LYS 217

3geoA01ARG 153;LYS 215;LYS 217

4aopA01ARG 153;LYS 215;LYS 217

4gepA01ARG 153;LYS 215;LYS 217

5aopA01ARG 153;LYS 215;LYS 217

5gepA01ARG 153;LYS 215;LYS 217

6gepA01ARG 153;LYS 215;LYS 217

7gepA01ARG 153;LYS 215;LYS 217

8gepA01ARG 153;LYS 215;LYS 217

1aopA02ARG 83

1geoA02ARG 83

1gepA02ARG 83

2aopA02ARG 83

2gepA02ARG 83

3aopA02ARG 83

3geoA02ARG 83

4aopA02ARG 83

4gepA02ARG 83

5aopA02ARG 83

5gepA02ARG 83

6gepA02ARG 83

7gepA02ARG 83

8gepA02ARG 83

1aopA03
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding)
1geoA03
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding)
1gepA03
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding)
2aopA03
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding)
2gepA03
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding)
3aopA03
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding)
3geoA03
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding)
4aopA03
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding)
4gepA03
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding)
5aopA03
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding)
5gepA03
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding)
6gepA03
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding)
7gepA03
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding)
8gepA03
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[5]Scheme 1, p.15805-15806
[8]p.18607-18608
[9]p.64-66
[12]Scheme 1, p.20554-20555
[13]

[14]p.12114-12118
[15]Fig.13, 12133-12126
[17]Scheme 2, Scheme 3, p.6120-6122
[18]Scheme 1
[21]

[22]


references
[1]
PubMed ID6281269
JournalJ Biol Chem
Year1982
Volume257
Pages6343-50
AuthorsSiegel LM, Rueger DC, Barber MJ, Krueger RJ, Orme-Johnson NR, Orme-Johnson WH
TitleEscherichia coli sulfite reductase hemoprotein subunit. Prosthetic groups, catalytic parameters, and ligand complexes.
[2]
PubMed ID3525540
JournalJ Biol Chem
Year1986
Volume261
Pages10277-81
AuthorsMcRee DE, Richardson DC, Richardson JS, Siegel LM
TitleThe heme and Fe4S4 cluster in the crystallographic structure of Escherichia coli sulfite reductase.
[3]
PubMed ID3056517
JournalBiochemistry
Year1988
Volume27
Pages5984-90
AuthorsYoung LJ, Siegel LM
TitleSuperoxidized states of Escherichia coli sulfite reductase heme protein subunit.
[4]
PubMed ID2670946
JournalJ Biol Chem
Year1989
Volume264
Pages15726-37
AuthorsOstrowski J, Wu JY, Rueger DC, Miller BE, Siegel LM, Kredich NM
TitleCharacterization of the cysJIH regions of Salmonella typhimurium and Escherichia coli B. DNA sequences of cysI and cysH and a model for the siroheme-Fe4S4 active center of sulfite reductase hemoprotein based on amino acid homology with spinach nitrite reductase.
[5]
PubMed ID2550423
JournalJ Biol Chem
Year1989
Volume264
Pages15796-808
AuthorsOstrowski J, Barber MJ, Rueger DC, Miller BE, Siegel LM, Kredich NM
TitleCharacterization of the flavoprotein moieties of NADPH-sulfite reductase from Salmonella typhimurium and Escherichia coli. Physicochemical and catalytic properties, amino acid sequence deduced from DNA sequence of cysJ, and comparison with NADPH-cytochrome P-450 reductase.
[6]
PubMed ID8457551
JournalBiochemistry
Year1993
Volume32
Pages2853-67
AuthorsKaufman J, Spicer LD, Siegel LM
TitleProton NMR of Escherichia coli sulfite reductase: the unligated hemeprotein subunit.
[7]
PubMed ID8395881
JournalBiochemistry
Year1993
Volume32
Pages8782-91
AuthorsKaufman J, Siegel LM, Spicer LD
TitleProton NMR of Escherichia coli sulfite reductase: studies of the heme protein subunit with added ligands.
[8]
PubMed ID8360156
JournalJ Biol Chem
Year1993
Volume268
Pages18604-9
AuthorsCoves J, Niviere V, Eschenbrenner M, Fontecave M
TitleNADPH-sulfite reductase from Escherichia coli. A flavin reductase participating in the generation of the free radical of ribonucleotide reductase.
[9]
PubMed ID7928966
JournalJ Bacteriol
Year1994
Volume176
Pages6050-8
AuthorsHansen J, Cherest H, Kielland-Brandt MC
TitleTwo divergent MET10 genes, one from Saccharomyces cerevisiae and one from Saccharomyces carlsbergensis, encode the alpha subunit of sulfite reductase and specify potential binding sites for FAD and NADPH.
[10]
CommentsX-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS)
Medline ID96008578
PubMed ID7569952
JournalScience
Year1995
Volume270
Pages59-67
AuthorsCrane BR, Siegel LM, Getzoff ED
TitleSulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions.
Related PDB1aop,1geo,1gep
Related Swiss-protP17846
[11]
CommentsCHARACTERIZATION OF FAD AND FMN DOMAINS.
Medline ID96049560
PubMed ID7589518
JournalFEBS Lett
Year1995
Volume374
Pages82-4
AuthorsEschenbrenner M, Coves J, Fontecave M
TitleNADPH-sulfite reductase flavoprotein from Escherichia coli: contribution to the flavin content and subunit interaction.
Related Swiss-protP38038
[12]
CommentsCHARACTERIZATION AS A NADPH:FLAVIN OXIDOREDUCTASE.
Medline ID95386502
PubMed ID7657631
JournalJ Biol Chem
Year1995
Volume270
Pages20550-5
AuthorsEschenbrenner M, Coves J, Fontecave M
TitleThe flavin reductase activity of the flavoprotein component of sulfite reductase from Escherichia coli. A new model for the protein structure.
Related Swiss-protP38038
[13]
CommentsCHARACTERIZATION OF FMN DOMAIN 1-219.
Medline ID97297802
PubMed ID9153434
JournalBiochemistry
Year1997
Volume36
Pages5921-8
AuthorsCoves J, Zeghouf M, Macherel D, Guigliarelli B, Asso M, Fontecave M
TitleFlavin mononucleotide-binding domain of the flavoprotein component of the sulfite reductase from Escherichia coli.
Related Swiss-protP38038
[14]
CommentsX-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS)
Medline ID97461529
PubMed ID9315848
JournalBiochemistry
Year1997
Volume36
Pages12101-19
AuthorsCrane BR, Siegel LM, Getzoff ED
TitleStructures of the siroheme- and Fe4S4-containing active center of sulfite reductase in different states of oxidation: heme activation via reduction-gated exogenous ligand exchange.
Related PDB2aop,2gep,3aop,3geo,4aop,4gep,5aop,5gep,6gep,7gep,8gep
Related Swiss-protP17846
[15]
PubMed ID9315849
JournalBiochemistry
Year1997
Volume36
Pages12120-37
AuthorsCrane BR, Siegel LM, Getzoff ED
TitleProbing the catalytic mechanism of sulfite reductase by X-ray crystallography: structures of the Escherichia coli hemoprotein in complex with substrates, inhibitors, intermediates, and products.
[16]
CommentsCHARACTERIZATION AS A NADPH-CYTOCHROME P450 REDUCTASE.
Medline ID98289576
PubMed ID9618257
JournalBiochem Biophys Res Commun
Year1998
Volume246
Pages602-5
AuthorsZeghouf M, Defaye G, Fontecave M, Coves J
TitleThe flavoprotein component of the Escherichia coli sulfite reductase can act as a cytochrome P450c17 reductase.
Related Swiss-protP38038
[17]
CommentsCHARACTERIZATION.
Medline ID98226652
PubMed ID9558350
JournalBiochemistry
Year1998
Volume37
Pages6114-23
AuthorsZeghouf M, Fontecave M, Macherel D, Coves J
TitleThe flavoprotein component of the Escherichia coli sulfite reductase: expression, purification, and spectral and catalytic properties of a monomeric form containing both the flavin adenine dinucleotide and the flavin mononucleotide cofactors.
Related Swiss-protP38038
[18]
CommentsCHARACTERIZATION OF FAD DOMAIN.
Medline ID99386679
PubMed ID10455035
JournalBiochem J
Year1999
Volume342
Pages465-72
AuthorsCoves J, Lebrun C, Gervasi G, Dalbon P, Fontecave M
TitleOverexpression of the FAD-binding domain of the sulphite reductase flavoprotein component from Escherichia coli and its inhibition by iodonium diphenyl chloride.
Related Swiss-protP38038
[19]
PubMed ID10215853
JournalEur J Biochem
Year1999
Volume261
Pages430-7
AuthorsEvrard A, Zeghouf M, Fontecave M, Roby C, Coves J
Title31P nuclear magnetic resonance study of the flavoprotein component of the Escherichia coli sulfite reductase.
[20]
CommentsQUATERNARY STRUCTURE.
Medline ID20545508
PubMed ID10984484
JournalJ Biol Chem
Year2000
Volume275
Pages37651-6
AuthorsZeghouf M, Fontecave M, Coves J
TitleA simplifed functional version of the Escherichia coli sulfite reductase.
Related Swiss-protP38038
[21]
CommentsX-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 225-598.
Medline ID20328609
PubMed ID10860732
JournalJ Mol Biol
Year2000
Volume299
Pages199-212
AuthorsGruez A, Pignol D, Zeghouf M, Coves J, Fontecave M, Ferrer JL, Fontecilla-Camps JC
TitleFour crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module.
Related PDB1ddi,1ddg
Related Swiss-protP38038
[22]
CommentsCHARACTERIZATION AND STRUCTURE BY NMR OF 52-219.
Medline ID21885835
PubMed ID11888295
JournalBiochemistry
Year2002
Volume41
Pages3770-80
AuthorsChampier L, Sibille N, Bersch B, Brutscher B, Blackledge M, Coves J
TitleReactivity, secondary structure, and molecular topology of the Escherichia coli sulfite reductase flavodoxin-like domain.
Related Swiss-protP38038

comments
This enzyme is made of two subunits, alpha subunit (Swiss-prot;P38038) and beta subunit (Swiss-prot;P17846). The alpha subunit is composed of N-terminal FMN-binding domain, FAD-binding domain, Ferredoxin NADP+ reductase-like module, and C-terminal NADPH-binding domain. As the N-terminal domain is flexible relative to the other domains, its structure has not been determined (see [20]).
In contrast, the beta subunit is composed of N-terminal domain, two active-site domains, and C-terminal Sirohem- and Iron/sulfur-binding domain.
According to the literature [5], [12] & [18], electrons are transferred from NADPH at the alpha subunit, through FAD and FMN, to sulfite at the beta subunit.

createdupdated
2004-03-252009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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