| General information | | DisProt: | DP00190 | | Name: | Sulfite reductase [NADPH] flavoprotein alpha-component | | Synonym(s): | CYSJ_ECOLI
SiR-FP
EC=1.8.1.2
| | First appeared in release: | Release 2.2 (04/14/2005) | | UniProt: | P38038 | | UniGene: | | | SwissProt: | CYSJ_ECOLI | | TrEMBL: | | | NCBI (GI): | 109940071 | | Source organism: | Escherichia coli (strain K12) | | Sequence length: | 598 | | Percent disordered: | 34% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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TTQVPPSALL PLNPEQLARL QAATTDLTPT QLAWVSGYFW GVLNQQPAAL AATPAPAAEM - 60
PGITIISASQ TGNARRVAEA LRDDLLAAKL NVKLVNAGDY KFKQIASEKL LIVVTSTQGE - 120
GEPPEEAVAL HKFLFSKKAP KLENTAFAVF SLGDTSYEFF CQSGKDFDSK LAELGGERLL - 180
DRVDADVEYQ AAASEWRARV VDALKSRAPV AAPSQSVATG AVNEIHTSPY SKDAPLVASL - 240
SVNQKITGRN SEKDVRHIEI DLGDSGLRYQ PGDALGVWYQ NDPALVKELV ELLWLKGDEP - 300
VTVEGKTLPL NEALQWHFEL TVNTANIVEN YATLTRSETL LPLVGDKAKL QHYAATTPIV - 360
DMVRFSPAQL DAEALINLLR PLTPRLYSIA SSQAEVENEV HVTVGVVRYD VEGRARAGGA - 420
SSFLADRVEE EGEVRVFIEH NDNFRLPANP ETPVIMIGPG TGIAPFRAFM QQRAADEAPG - 480
KNWLFFGNPH FTEDFLYQVE WQRYVKEGVL TRIDLAWSRD QKEKVYVQDK LREQGAELWR - 540
WINDGAHIYV CGDANRMAKD VEQALLEVIA EFGGMDTEAA DEFLSELRVE RRYQRDVY
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| Functional narrative |
Sulfite reductase [NADPH] flavoprotein alpha-component is a multimeric hemoflavoprotein that belongs to a family of enzymes involved in the transport of electrons. SiR is composed of eight alpha-subunits (SiR-FP) and four beta-subunits (SiR-HP). It reduces sulfite to sulfide in one of the several activities required for the biosynthesis of L-cysteine from sulfate.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | FMN binding domain | | Location: | 52 - 224 | | Length: | 173 | | Region sequence: |
ATPAPAAEMPGITIISASQTGNARRVAEALRDDLLAAKLNVKLVNAGDYKFKQIASEKLL
IVVTSTQGEGEPPEEAVALHKFLFSKKAPKLENTAFAVFSLGDTSYEFFCQSGKDFDSKL
AELGGERLLDRVDADVEYQAAASEWRARVVDALKSRAPVAAPSQSVATGAVNE | | Modification type: | Fragment
| | PDB: | 1DDG:A, 1DDG:B, 1DDI:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Cofactor/heme binding
Electron transfer
| Detection methods:
- X-ray crystallography (277 K; 1-4 methyl-pentane-diol 10 %; ammonium sulfate 2 M; NADP+ (5mM) 2 µl; SiR-FP60 (15 g/mL) (protein) 2 µl; Tris-HCl (pH 7.0) 50 mM)
| References:
- Gruez A, Pignol D, Zeghouf M, Coves J, Fontecave M, Ferrer JL, Fontecilla-Camps JC. "Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module." J Mol Biol. 2000; 299(1): 199-212. PubMed: 10860732
| Comments:This is the FMN binding domain of this protein. It transfers electrons from the ferredoxin NADP+ reductase (FNR) module to the beta subunit, which contains Fe4S4 and siroheme. The FMN of one molecule binds to the FNR of an adjacent molecule. The flexibility of this region is believed to be important in optimal molecular arrangment during electron transfer.
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| Region 2 | | Type: | Ordered | | Name: | FAD-binding domain | | Location: | 225 - 279 | | Length: | 55 | | Region sequence: |
IHTSPYSKDAPLVASLSVNQKITGRNSEKDVRHIEIDLGDSGLRYQPGDALGVWY | | Modification type: | Fragment
| | PDB: | 1DDG:A, 1DDG:B, 1DDI:A | | Structural/functional type: | Function arises from the ordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Cofactor/heme binding
| Detection methods:
- X-ray crystallography (277 K; 1-4 methyl-pentane-diol 10 %; ammonium sulfate 2 M; NADP+ (5mM) 2 µl; SiR-FP60 (15 g/mL) (protein) 2 µl; Tris-HCl (pH 7.0) 50 mM)
| References:
- Gruez A, Pignol D, Zeghouf M, Coves J, Fontecave M, Ferrer JL, Fontecilla-Camps JC. "Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module." J Mol Biol. 2000; 299(1): 199-212. PubMed: 10860732
| Comments:
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| Region 3 | | Type: | Ordered | | Name: | connecting domain | | Location: | 280 - 384 | | Length: | 105 | | Region sequence: |
QNDPALVKELVELLWLKGDEPVTVEGKTLPLNEALQWHFELTVNTANIVENYATLTRSET
LLPLVGDKAKLQHYAATTPIVDMVRFSPAQLDAEALINLLRPLTP | | Modification type: | Fragment
| | PDB: | 1DDG:A, 1DDG:B, 1DDI:A | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- X-ray crystallography (277 K; 1-4 methyl-pentane-diol 10 %; ammonium sulfate 2 M; NADP+ (5mM) 2 µl; SiR-FP60 (15 g/mL) (protein) 2 µl; Tris-HCl (pH 7.0) 50 mM)
| References:
- Gruez A, Pignol D, Zeghouf M, Coves J, Fontecave M, Ferrer JL, Fontecilla-Camps JC. "Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module." J Mol Biol. 2000; 299(1): 199-212. PubMed: 10860732
| Comments:
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| Region 4 | | Type: | Ordered | | Name: | FAD-binding domain | | Location: | 385 - 444 | | Length: | 60 | | Region sequence: |
RLYSIASSQAEVENEVHVTVGVVRYDVEGRARAGGASSFLADRVEEEGEVRVFIEHNDNF
| | Modification type: | Fragment
| | PDB: | 1DDG:A, 1DDG:B, 1DDI:A | | Structural/functional type: | Function arises from the ordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Cofactor/heme binding
| Detection methods:
- X-ray crystallography (277 K; 1-4 methyl-pentane-diol 10 %; ammonium sulfate 2 M; NADP+ (5mM) 2 µl; SiR-FP60 (15 g/mL) (protein) 2 µl; Tris-HCl (pH 7.0) 50 mM)
| References:
- Gruez A, Pignol D, Zeghouf M, Coves J, Fontecave M, Ferrer JL, Fontecilla-Camps JC. "Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module." J Mol Biol. 2000; 299(1): 199-212. PubMed: 10860732
| Comments:
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| Region 5 | | Type: | Ordered | | Name: | NADP(H)-binding domain | | Location: | 445 - 598 | | Length: | 154 | | Region sequence: |
RLPANPETPVIMIGPGTGIAPFRAFMQQRAADEAPGKNWLFFGNPHFTEDFLYQVEWQRY
VKEGVLTRIDLAWSRDQKEKVYVQDKLREQGAELWRWINDGAHIYVCGDANRMAKDVEQA
LLEVIAEFGGMDTEAADEFLSELRVERRYQRDVY | | Modification type: | Fragment
| | PDB: | 1DDG:A, 1DDG:B, 1DDI:A | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (277 K; 1-4 methyl-pentane-diol 10 %; ammonium sulfate 2 M; NADP+ (5mM) 2 µl; SiR-FP60 (15 g/mL) (protein) 2 µl; Tris-HCl (pH 7.0) 50 mM)
| References:
- Gruez A, Pignol D, Zeghouf M, Coves J, Fontecave M, Ferrer JL, Fontecilla-Camps JC. "Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module." J Mol Biol. 2000; 299(1): 199-212. PubMed: 10860732
| Comments:
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| Region 6 | | Type: | Disordered | | Name: | | | Location: | 55 - 255 | | Length: | 201 | | Region sequence: |
APAAEMPGITIISASQTGNARRVAEALRDDLLAAKLNVKLVNAGDYKFKQIASEKLLIVV
TSTQGEGEPPEEAVALHKFLFSKKAPKLENTAFAVFSLGDTSYEFFCQSGKDFDSKLAEL
GGERLLDRVDADVEYQAAASEWRARVVDALKSRAPVAAPSQSVATGAVNEIHTSPYSKDA
PLVASLSVNQKITGRNSEKDV | | Modification type: | Fragment
| | PDB: | 1DDG:A, 1DDG:B, 1DDI:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Cofactor/heme binding
Electron transfer
| Detection methods:
- X-ray crystallography (277 K; 1-4 methyl-pentane-diol 10 %; ammonium sulfate 2 M; NADP+ (5mM) 2 µl; SiR-FP60 (15mg/ml) (protein) 2 µl; Tris-HCl (pH 7.0) 50 mM)
| References:
- Gruez A, Pignol D, Zeghouf M, Coves J, Fontecave M, Ferrer JL, Fontecilla-Camps JC. "Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module." J Mol Biol. 2000; 299(1): 199-212. PubMed: 10860732
| Comments:
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| References |
- Ostrowski J, Barber MJ, Rueger DC, Miller BE, Siegel LM, Kredich NM. "Characterization 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." J Biol Chem. 1989; 264(27): 15796-808. PubMed: 2550423
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| Comments |
Four polymorphs were created for this protein. #1 was used to determine the structure, and was thus used for this entry. Polymorphs 2-4 were analyzed and their structures were also determined. They had no regions of electron density from residues 55-255, and were assumed to be disordered in these regions.
The paper by Ostrowski et al. contains the full protein sequence.
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