Sulfite reductase [NADPH] flavoprotein alpha-component

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P38038 (CYSJ_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 129. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Sulfite reductase [NADPH] flavoprotein alpha-component
Short name=SiR-FP
EC=1.8.1.2

Gene names

Name:	cysJ
Ordered Locus Names:	b2764, JW2734

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	599 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. HAMAP-Rule MF_01541
Catalytic activity	H₂S + 3 NADP⁺ + 3 H₂O = sulfite + 3 NADPH. Ref.13
Cofactor	Binds 1 FAD per subunit. Ref.13 Binds 1 FMN per subunit. Ref.13
Pathway	Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. HAMAP-Rule MF_01541
Subunit structure	Alpha(8)-beta₈. The alpha component is a flavoprotein, the beta component is a hemoprotein. Ref.12
Sequence similarities	Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Cysteine biosynthesis Electron transport Transport
Ligand	FAD FMN Flavoprotein NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cysteine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW hydrogen sulfide biosynthetic process Inferred from electronic annotation. Source: HAMAP sulfate assimilation Inferred from electronic annotation. Source: HAMAP
Cellular_component	sulfite reductase complex (NADPH) Inferred from direct assay PubMed 8360156. Source: EcoCyc
Molecular_function	FMN binding Inferred from direct assay Ref.6. Source: EcoCyc NADPH-hemoprotein reductase activity Inferred from Biological aspect of Ancestor. Source: RefGenome flavin adenine dinucleotide binding Inferred from direct assay Ref.6. Source: EcoCyc iron ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen Inferred from Biological aspect of Ancestor. Source: RefGenome riboflavin reductase (NADPH) activity Inferred from direct assay Ref.6. Source: EcoCyc sulfite reductase (NADPH) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ycbX	P75863	2	EBI-544440,EBI-544422

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed HAMAP-Rule MF_01541

Chain

2 – 599

598

Sulfite reductase [NADPH] flavoprotein alpha-component HAMAP-Rule MF_01541

PRO_0000199923

Regions

Domain

64 – 202

139

Flavodoxin-like

Domain

234 – 448

215

FAD-binding FR-type

Nucleotide binding

70 – 74

FMN HAMAP-Rule MF_01541

Nucleotide binding

117 – 122

FMN HAMAP-Rule MF_01541

Nucleotide binding

150 – 181

FMN HAMAP-Rule MF_01541

Nucleotide binding

386 – 389

FAD HAMAP-Rule MF_01541

Nucleotide binding

420 – 422

FAD HAMAP-Rule MF_01541

Nucleotide binding

519 – 527

NADP HAMAP-Rule MF_01541

Sites

Binding site

489

NADP

Experimental info

Sequence conflict

156

S → T in AAA23650. Ref.1

Sequence conflict

268

M → L in AAA23650. Ref.1

Sequence conflict

508

D → E in AAA23650. Ref.1

Secondary structure

599

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P38038 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 6B39EF5C25265113
Show »

FASTA

599

66,270

        10         20         30         40         50         60 
MTTQVPPSAL LPLNPEQLAR LQAATTDLTP TQLAWVSGYF WGVLNQQPAA LAATPAPAAE 

        70         80         90        100        110        120 
MPGITIISAS QTGNARRVAE ALRDDLLAAK LNVKLVNAGD YKFKQIASEK LLIVVTSTQG 

       130        140        150        160        170        180 
EGEPPEEAVA LHKFLFSKKA PKLENTAFAV FSLGDSSYEF FCQSGKDFDS KLAELGGERL 

       190        200        210        220        230        240 
LDRVDADVEY QAAASEWRAR VVDALKSRAP VAAPSQSVAT GAVNEIHTSP YSKDAPLVAS 

       250        260        270        280        290        300 
LSVNQKITGR NSEKDVRHIE IDLGDSGMRY QPGDALGVWY QNDPALVKEL VELLWLKGDE 

       310        320        330        340        350        360 
PVTVEGKTLP LNEALQWHFE LTVNTANIVE NYATLTRSET LLPLVGDKAK LQHYAATTPI 

       370        380        390        400        410        420 
VDMVRFSPAQ LDAEALINLL RPLTPRLYSI ASSQAEVENE VHVTVGVVRY DVEGRARAGG 

       430        440        450        460        470        480 
ASSFLADRVE EEGEVRVFIE HNDNFRLPAN PETPVIMIGP GTGIAPFRAF MQQRAADEAP 

       490        500        510        520        530        540 
GKNWLFFGNP HFTEDFLYQV EWQRYVKDGV LTRIDLAWSR DQKEKVYVQD KLREQGAELW 

       550        560        570        580        590 
RWINDGAHIY VCGDANRMAK DVEQALLEVI AEFGGMDTEA ADEFLSELRV ERRYQRDVY

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." Ostrowski J., Barber M.J., Rueger D.C., Miller B.E., Siegel L.M., Kredich N.M. J. Biol. Chem. 264:15796-15808(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: B.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Characterization 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." Ostrowski J., Wu J.-Y., Rueger D.C., Miller B.E., Siegel L.M., Kredich N.M. J. Biol. Chem. 264:15726-15737(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 594-599. Strain: B.
[5]	"NADPH-sulfite reductase flavoprotein from Escherichia coli: contribution to the flavin content and subunit interaction." Eschenbrenner M., Coves J., Fontecave M. FEBS Lett. 374:82-84(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF FAD AND FMN DOMAINS.
[6]	"The flavin reductase activity of the flavoprotein component of sulfite reductase from Escherichia coli. A new model for the protein structure." Eschenbrenner M., Coves J., Fontecave M. J. Biol. Chem. 270:20550-20555(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION AS A NADPH:FLAVIN OXIDOREDUCTASE.
[7]	"Flavin mononucleotide-binding domain of the flavoprotein component of the sulfite reductase from Escherichia coli." Coves J., Zeghouf M., Macherel D., Guigliarelli B., Asso M., Fontecave M. Biochemistry 36:5921-5928(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF FMN DOMAIN 1-220.
[8]	"The flavoprotein component of the Escherichia coli sulfite reductase can act as a cytochrome P450c17 reductase." Zeghouf M., Defaye G., Fontecave M., Coves J. Biochem. Biophys. Res. Commun. 246:602-605(1998) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION AS A NADPH-CYTOCHROME P450 REDUCTASE.
[9]	"The 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." Zeghouf M., Fontecave M., Macherel D., Coves J. Biochemistry 37:6114-6123(1998) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[10]	"Overexpression of the FAD-binding domain of the sulphite reductase flavoprotein component from Escherichia coli and its inhibition by iodonium diphenyl chloride." Coves J., Lebrun C., Gervasi G., Dalbon P., Fontecave M. Biochem. J. 342:465-472(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF FAD DOMAIN.
[11]	"Reactivity, secondary structure, and molecular topology of the Escherichia coli sulfite reductase flavodoxin-like domain." Champier L., Sibille N., Bersch B., Brutscher B., Blackledge M., Coves J. Biochemistry 41:3770-3780(2002) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, STRUCTURE BY NMR OF 53-220.
[12]	"A simplifed functional version of the Escherichia coli sulfite reductase." Zeghouf M., Fontecave M., Coves J. J. Biol. Chem. 275:37651-37656(2000) [PubMed] [Europe PMC] [Abstract] Cited for: QUATERNARY STRUCTURE.
[13]	"Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module." Gruez A., Pignol D., Zeghouf M., Coves J., Fontecave M., Ferrer J.-L., Fontecilla-Camps J.-C. J. Mol. Biol. 299:199-212(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 226-599 IN COMPLEXES WITH FAD AND NADP, COFACTOR, MASS SPECTROMETRY, PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY.
[14]	"Solution structure of the sulfite reductase flavodoxin-like domain from Escherichia coli." Sibille N., Blackledge M., Brutscher B., Coves J., Bersch B. Biochemistry 44:9086-9095(2005) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 53-218 IN COMPLEX WITH FMN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M23008 Genomic DNA. Translation: AAA23650.1.
U29579 Genomic DNA. Translation: AAA69274.1.
U00096 Genomic DNA. Translation: AAC75806.1.
AP009048 Genomic DNA. Translation: BAE76841.1.

PIR

H65057.

RefSeq

NP_417244.1. NC_000913.2.
YP_490973.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DDG	X-ray	2.01	A/B	226-599	[»]
1DDI	X-ray	2.51	A	226-599	[»]
1YKG	NMR	-	A	53-218	[»]

DisProt

DP00190.

ProteinModelPortal

P38038.

SMR

P38038. Positions 64-599.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9381N.

IntAct

P38038. 3 interactions.

MINT

MINT-1239442.

STRING

511145.b2764.

Proteomic databases

PaxDb

P38038.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75806; AAC75806; b2764.
BAE76841; BAE76841; BAE76841.

GeneID

12933289.
947239.

KEGG

ecj:Y75_p2702.
eco:b2764.

PATRIC

32120940. VBIEscCol129921_2862.

Organism-specific databases

EchoBASE

EB0188.

EcoGene

EG10191. cysJ.

Phylogenomic databases

eggNOG

COG0369.

HOGENOM

HOG000282025.

K00380.

OMA

SDKDVRH.

ProtClustDB

PRK10953.

Enzyme and pathway databases

BioCyc

EcoCyc:ALPHACOMP-MONOMER.
ECOL316407:JW2734-MONOMER.
MetaCyc:ALPHACOMP-MONOMER.

UniPathway

UPA00140; UER00207.

Gene expression databases

Genevestigator

P38038.

Family and domain databases

Gene3D

1.20.990.10. 1 hit.

HAMAP

MF_01541. CysJ.

InterPro

IPR010199. CysJ.
IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]

Pfam

PF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]

PIRSF

PIRSF000207. SiR-FP_CysJ. 1 hit.

PRINTS

PR00369. FLAVODOXIN.
PR00371. FPNCR.

SUPFAM

SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.

TIGRFAMs

TIGR01931. cysJ. 1 hit.

PROSITE

PS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P38038.

Entry information

Entry name

CYSJ_ECOLI

Accession

Primary (citable) accession number: P38038
Secondary accession number(s): P14782, Q2MA65

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 129 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents