Skip Header

Contribute Send feedback
Read comments (?) or add your own

P38039 (CYSJ_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sulfite reductase [NADPH] flavoprotein alpha-component
Short name=SiR-FP
EC=1.8.1.2
Gene names
Name:cysJ
Ordered Locus Names:STM2948
OrganismSalmonella typhimurium
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length599 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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 MF_01541

Catalytic activity

H2S + 3 NADP+ + 3 H2O = sulfite + 3 NADPH. HAMAP MF_01541

Cofactor

Binds 1 FAD per subunit.

Binds 1 FMN per subunit.

Pathway

Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. HAMAP MF_01541

Subunit structure

Alpha(8)-beta8. 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 599598Sulfite reductase [NADPH] flavoprotein alpha-component HAMAP MF_01541
PRO_0000199935

Regions

Domain64 – 202139Flavodoxin-like
Domain234 – 448215FAD-binding FR-type
Nucleotide binding70 – 745FMN By similarity
Nucleotide binding117 – 1226FMN By similarity
Nucleotide binding150 – 18132FMN By similarity
Nucleotide binding386 – 3894FAD By similarity
Nucleotide binding420 – 4223FAD By similarity
Nucleotide binding519 – 5279NADP By similarity

Sites

Binding site4891NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
P38039 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 13CBAC2BF806EBDB

FASTA59966,484
        10         20         30         40         50         60 
MTTPAPLTGL LPLNPEQLAR LQAATTDLTP EQLAWVSGYF WGVLNPRSGA VAVTPVPERK 

        70         80         90        100        110        120 
MPRVTLISAS QTGNARRVAE ALRDDLLAAN LNVTLVNAGD YKFKQIASEK LLVIVTSTQG 

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

       190        200        210        220        230        240 
LDRVDADVEY QAAASEWRAR VVDVLKSRAP VAAPSQSVAT GAVNDIHTSP YTKDAPLIAT 

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

       310        320        330        340        350        360 
PVTVDGKTLP LAEALEWHFE LTVNTANIVE NYATLTRSES LLPLVGDKAQ LQHYAATTPI 

       370        380        390        400        410        420 
VDMVRFSPAQ LDAQALIDLL RPLTPRLYSI ASAQAEVESE VHITVGVVRY DIEGRARAGG 

       430        440        450        460        470        480 
ASSFLADRVE EEGEVRVFIE HNDNFRLPAN PETPVIMIGP GTGIAPFRSF MQQRAAEGVE 

       490        500        510        520        530        540 
GKNWLFFGNP HFTEDFLYQV EWQRYVKEGV LSRIDLAWSR DQKEKIYVQD KLREQGAELW 

       550        560        570        580        590 
RWINDGAHIY VCGDARRMAA DVEKALLEVI AEFGGMDLES ADEYLSELRV ERRYQRDVY

« Hide

References

« Hide '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: LT2.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed: 11677609] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"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: LT2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M23007 Genomic DNA. Translation: AAA27046.1.
AE006468 Genomic DNA. Translation: AAL21828.1.
PIRA34231.
RefSeqNP_461869.1. NC_003197.1.

3D structure databases

ProteinModelPortalP38039.
SMRP38039. Positions 64-209, 226-599.
ModBaseSearch...

Proteomic databases

PRIDEP38039.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1254471.
GenomeReviewsGene locus STM2948 in contig AE006468_GR.
KEGGstm:STM2948.
NMPDRfig|99287.1.peg.2844.
PATRIC32384595. VBISalEnt20916_3109.

Phylogenomic databases

HOGENOMHBG736048.
OMAESADEYL.
ProtClustDBPRK10953.

Enzyme and pathway databases

BioCycSTYP99287:STM2948-MONOMER.

Family and domain databases

HAMAPMF_01541. CysJ.
[Tree]
InterProIPR010199. 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]
Gene3DG3DSA:1.20.990.10. NADPH_Cyt_P450_Rdtase_dom3. 1 hit.
KOK00380.
PfamPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF000207. SiR-FP_CysJ. 1 hit.
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMSSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
TIGRFAMsTIGR01931. CysJ. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSJ_SALTY
AccessionPrimary (citable) accession number: P38039
Secondary accession number(s): P14782
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents