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InterPro: IPR006067 Nitrite/sulphite reductase 4Fe-4S domain
Protein matches
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UniProtKB Matches: 7399 proteins |
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Accession
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IPR006067 NO2/SO3_Rdtase_4Fe4S_dom |
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Secondary
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IPR000660
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Type
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Domain |
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Signatures
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InterPro Relationships
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Found in
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IPR011786 Sulphite reductase (NADPH) hemoprotein, beta subunit
IPR011787 Sulphite reductase, ferredoxin dependent
IPR011806 Sulphite reductase, dissimilatory-type alpha subunit
IPR011808 Sulphite reductase, dissimilatory-type beta subunit
IPR012744 Nitrite reductase [NAD(P)H] large subunit, NirB
IPR014261 Sulphite reductase, subunit C
IPR017121 Nitrite reductase [NAD(P)H], large subunit
IPR017220 Sulphite reductase, assimilatory
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Contains
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IPR006066 Nitrite/sulphite reductase iron-sulphur/siroheam-binding site
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GO Term annotation
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Process
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GO:0055114 oxidation reduction
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Function
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GO:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0051536 iron-sulfur cluster binding
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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Sulphite reductases (SiRs) and related nitrite reductases (NiRs) catalyse the six-electron reduction reactions of sulphite to sulphide, and nitrite to ammonia, respectively. The Escherichia coli SiR enzyme is a complex composed of two proteins, a flavoprotein alpha-component (SiR-FP) and a hemoprotein beta-component (SiR-HP) (IPR005117), and has an alpha(8)beta(4) quaternary structure [1]. SiR-FP contains both FAD and FMN, while SiR-HP contains a Fe(4)S(4) cluster coupled to a siroheme through a cysteine bridge. Electrons are transferred from NADPH to FAD, and on to FMN in SiR-FP, from which they are transferred to the metal centre of SiR-HP, where they reduce the siroheme-bound sulphite.
SiR-HP has a two-fold symmetry, which generates a distinctive three-domain alpha/beta fold that controls assembly and reactivity [2]. In the E. coli SiR-HP enzyme (EC:1.8.1.2), the iron is bound to cysteine residues at positions 433, 439, 478 and 482, the latter also forming the siroheme ligand.
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Structural links
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Database links
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Additional Reading
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Schnell R, Sandalova T, Hellman U, Lindqvist Y, Schneider G.
Siroheme- and [Fe4-S4]-dependent NirA from Mycobacterium tuberculosis is a sulfite reductase with a covalent Cys-Tyr bond in the active site.
J. Biol. Chem. 280 2005 27319-28
[PubMed: 15917234]
http://dx.doi.org/10.1074/jbc.M502560200
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Swamy U, Wang M, Tripathy JN, Kim SK, Hirasawa M, Knaff DB, Allen JP.
Structure of spinach nitrite reductase: implications for multi-electron reactions by the iron-sulfur:siroheme cofactor.
Biochemistry 44 2005 16054-63
[PubMed: 16331965]
http://dx.doi.org/10.1021/bi050981y
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Schiffer A, Parey K, Warkentin E, Diederichs K, Huber H, Stetter KO, Kroneck PM, Ermler U.
Structure of the dissimilatory sulfite reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus.
J. Mol. Biol. 379 2008 1063-74
[PubMed: 18495156]
http://dx.doi.org/10.1016/j.jmb.2008.04.027
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Crane BR, Siegel LM, Getzoff ED.
Probing the catalytic mechanism of sulfite reductase by X-ray crystallography: structures of the Escherichia coli hemoprotein in complex with substrates, inhibitors, intermediates, and products.
Biochemistry 36 1997 12120-37
[PubMed: 9315849]
http://dx.doi.org/10.1021/bi971066i
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Oliveira TF, Vonrhein C, Matias PM, Venceslau SS, Pereira IA, Archer M.
Purification, crystallization and preliminary crystallographic analysis of a dissimilatory sulfite reductase DsrAB in complex with DsrC.
J. Struct. Biol. 2008
[PubMed: 18706503]
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Oliveira TF, Vonrhein C, Matias PM, Venceslau SS, Pereira IA, Archer M.
The crystal structure of Desulfovibrio vulgaris dissimilatory sulfite reductase bound to DsrC provides novel insights into the mechanism of sulfate respiration.
J. Biol. Chem. 283 2008 34141-9
[PubMed: 18829451]
http://dx.doi.org/10.1074/jbc.M805643200
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InterPro 23.1
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