Sulfite reductase [NADPH] flavoprotein alpha-component

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Reviewed, UniProtKB/Swiss-Prot P38038 (CYSJ_ECOLI)

Last modified June 16, 2009. Version 96. History...

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

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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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.

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General annotation (Comments)

Function	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 flavo-protein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. HAMAP MF_01541
Catalytic activity	H₂S + 3 NADP⁺ + 3 H₂O = sulfite + 3 NADPH. HAMAP MF_01541
Cofactor	Binds 1 FAD per subunit. HAMAP MF_01541 Binds 1 FMN per subunit. HAMAP 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.

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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
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 sulfate assimilation Inferred from electronic annotation. Source: HAMAP transport Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FMN binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct sulfite reductase (NADPH) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
ribB	P0A7J0	1	EBI-544440,EBI-553653
ycbX	P75863	1	EBI-544440,EBI-544422

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed HAMAP MF_01541

Chain

2 – 599

598

Sulfite reductase [NADPH] flavoprotein alpha-component HAMAP MF_01541

PRO_0000199923

Regions

Domain

64 – 202

139

Flavodoxin-like

Domain

234 – 448

215

FAD-binding FR-type

Nucleotide binding

70 – 74

FMN By similarity

Nucleotide binding

150 – 181

FMN By similarity

Nucleotide binding

236 – 288

FAD By similarity

Nucleotide binding

472 – 599

128

NADP By similarity

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...

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Sequences

Sequence

Length

Mass (Da)

Tools

P38038-1 [UniParc].

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

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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: 2550423] [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: 9278503] [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: 16738553] [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: 2670946] [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: 7589518] [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: 7657631] [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: 9153434] [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: 9618257] [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: 9558350] [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: 10455035] [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: 11888295] [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: 10984484] [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: 10860732] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 226-599.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

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

AP_003331.1.
NP_417244.1.

3D structure databases

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.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:9381N.

IntAct

P38038. 3 interactions.

Genome annotation databases

GeneID

947239.

GenomeReviews

Gene locus JW2734 in contig AP009048_GR.
Gene locus b2764 in contig U00096_GR.

KEGG

ecj:JW2734.
eco:b2764.

Organism-specific databases

EchoBASE

EB0188.

EcoGene

EG10191. cysJ.

CMR

Search...

Phylogenomic databases

HOGENOM

P38038.

OMA

P38038. EQLAWVS.

Enzyme and pathway databases

BioCyc

EcoCyc:ALPHACOMP-MON.
MetaCyc:ALPHACOMP-MON.

Family and domain databases

HAMAP

MF_01541.
[Tree]

InterPro

IPR010199. CysJ.
IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR001433. OxRdtase_FAD/NAD_bd.
[Graphical view]

Pfam

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

PRINTS

PR00369. FLAVODOXIN.
PR00371. FPNCR.

TIGRFAMs

TIGR01931. cysJ. 1 hit.

PROSITE

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

ProtoNet

Search...

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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:	June 16, 2009
This is version 96 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents