Reviewed, UniProtKB/Swiss-Prot P38038 (CYSJ_ECOLI)

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

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	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.
Catalytic activity	H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 NADPH.
Cofactor	Binds 1 FAD per subunit. Binds 1 FMN per subunit.
Subunit structure	Alpha(8)-beta(8). The alpha component is a flavoprotein, the beta component is a hemoprotein.
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
Gene Ontology (GO)
Biological process	cysteine biosynthetic process Inferred from electronic annotation. Source: InterPro 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...

Binary interactions

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 599

598

Sulfite reductase [NADPH] flavoprotein alpha-component

PRO_0000199923

Regions

Domain

64 – 202

139

Flavodoxin-like

Domain

234 – 448

215

FAD-binding FR-type

Nucleotide binding

70 – 74

5

FMN By similarity

Nucleotide binding

150 – 181

32

FMN By similarity

Nucleotide binding

236 – 288

53

FAD By similarity

Nucleotide binding

472 – 599

128

NADP By similarity

Experimental info

Sequence conflict

156

1

S → T in AAA23650. Ref.1

Sequence conflict

268

1

M → L in AAA23650. Ref.1

Sequence conflict

508

1

D → E in AAA23650. Ref.1

Secondary structure

1

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599

Helix Strand Turn

Details...

Beta strand

65 – 69

5

Beta strand

71 – 73

3

Helix

74 – 89

16

Beta strand

94 – 97

4

Helix

98 – 100

3

Helix

103 – 108

6

Beta strand

110 – 117

8

Helix

120 – 122

3

Helix

126 – 128

3

Helix

129 – 135

7

Beta strand

147 – 153

7

Beta strand

158 – 160

3

Helix

163 – 175

13

Beta strand

178 – 181

4

Beta strand

184 – 186

3

Helix

191 – 206

16

Beta strand

237 – 246

10

Beta strand

253 – 262

10

Beta strand

275 – 278

4

Helix

284 – 293

10

Beta strand

300 – 304

5

Beta strand

307 – 310

4

Helix

311 – 318

8

Helix

326 – 336

11

Turn

339 – 341

3

Helix

342 – 344

3

Helix

349 – 357

9

Helix

360 – 366

7

Helix

373 – 379

7

Beta strand

386 – 390

5

Turn

394 – 396

3

Beta strand

399 – 407

9

Beta strand

409 – 412

4

Beta strand

415 – 418

4

Helix

420 – 427

8

Beta strand

434 – 440

7

Beta strand

455 – 458

4

Helix

461 – 464

4

Helix

465 – 477

13

Beta strand

483 – 490

8

Helix

492 – 495

4

Helix

499 – 507

9

Beta strand

513 – 518

6

Beta strand

521 – 524

4

Helix

528 – 534

7

Helix

536 – 544

9

Beta strand

548 – 554

7

Turn

555 – 557

3

Helix

558 – 572

15

Turn

573 – 575

3

Helix

578 – 590

13

Beta strand

594 – 599

6

Sequences

	Sequence		Length	Mass (Da)
	P38038-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 6B39EF5C25265113	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

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