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P17845 (CYSI_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Sulfite reductase [NADPH] hemoprotein beta-component

Short name=SiR-HP
Short name=SiRHP
EC=1.8.1.2
Gene names
Name:cysI
Ordered Locus Names:STM2947
OrganismSalmonella typhimurium
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length570 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. HAMAP MF_01540

Catalytic activity

H2S + 3 NADP+ + 3 H2O = sulfite + 3 NADPH. HAMAP MF_01540

Cofactor

Binds 1 siroheme per subunit.

Binds 1 4Fe-4S cluster per subunit.

Pathway

Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. HAMAP MF_01540

Subunit structure

Alpha(8)-beta8. The alpha component is a flavoprotein, the beta component is a hemoprotein.

Sequence similarities

Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 570569Sulfite reductase [NADPH] hemoprotein beta-component HAMAP MF_01540
PRO_0000199908

Sites

Metal binding4341Iron-sulfur (4Fe-4S) By similarity
Metal binding4401Iron-sulfur (4Fe-4S) By similarity
Metal binding4791Iron-sulfur (4Fe-4S) By similarity
Metal binding4831Iron (siroheme axial ligand) By similarity
Metal binding4831Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
P17845 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 62A9B26F077443C7

FASTA57064,023
        10         20         30         40         50         60 
MSEKHPGPLV VEGKLSDAER MKLESNYLRG TIAEDLNDGL TGGFKGDNFL LIRFHGMYQQ 

        70         80         90        100        110        120 
DDRDIRAERA AQKLEPRHAM LLRCRLPGGV ITTTQWQAID KFAADNTIYG SIRLTNRQTF 

       130        140        150        160        170        180 
QFHGILKKNV KPVHQMLHSV GLDALATAND MNRNVLCTSN PYESQLHAEA YEWAKKISEH 

       190        200        210        220        230        240 
LLPRTRAYAE IWLDQEKVAT TDEEPILGQT YLPRKFKTTV VIPPQNDIDL HANDMNFVAI 

       250        260        270        280        290        300 
AENGKLVGFN LLVGGGLSIE HGNKKTYART ASEFGYLPLE HTLAVAEAVV TTQRDWGNRT 

       310        320        330        340        350        360 
DRKNAKTKYT LERVGLETFK AEVERRAGIK FEPIRPYEFT GRGDRIGWVK GIDDKWHLTL 

       370        380        390        400        410        420 
FIENGRILDY PGRPLKTGLL EIAKIHQGEF RITANQNLII ASVPESQKAK IETLARDHGL 

       430        440        450        460        470        480 
MNAVKPQREN SMACVSFPTC PLAMAEAERF LPSFTDKVEA ILEKHGIPDE HIVMRVTGCP 

       490        500        510        520        530        540 
NGCGRAMLAE IGLVGKAPGR YNLHLGGNRI GSRIPRMYKE NIAEPDILAS LDELIGRWAK 

       550        560        570 
EREAGEGFGD FTVRAGIIRP VLDPARDFWE 

« Hide

References

« Hide 'large scale' references
[1]"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].
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M23007 Genomic DNA. Translation: AAA27047.1.
AE006468 Genomic DNA. Translation: AAL21827.1.
PIRA34354.
RefSeqNP_461868.1. NC_003197.1.

3D structure databases

ProteinModelPortalP17845.
SMRP17845. Positions 81-570.
ModBaseSearch...

Proteomic databases

PRIDEP17845.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1254470.
GenomeReviewsGene locus STM2947 in contig AE006468_GR.
KEGGstm:STM2947.
NMPDRfig|99287.1.peg.2843.
PATRIC32384593. VBISalEnt20916_3108.

Phylogenomic databases

HOGENOMHBG626671.
OMATRQAFQM.
ProtClustDBPRK13504.

Enzyme and pathway databases

BioCycSTYP99287:STM2947-MONOMER.

Family and domain databases

HAMAPMF_01540. CysI.
[Tree]
InterProIPR011786. CysI.
IPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
IPR006066. NO2/SO3_Rdtase_FeS/sirohaem_BS.
[Graphical view]
Gene3DG3DSA:3.90.480.10. G3DSA:3.90.480.10. 2 hits.
KOK00381.
PfamPF01077. NIR_SIR. 2 hits.
PF03460. NIR_SIR_ferr. 2 hits.
[Graphical view]
PRINTSPR00397. SIROHAEM.
SUPFAMSSF55124. NiR_SiRalpha_1/3. 2 hits.
TIGRFAMsTIGR02041. CysI. 1 hit.
PROSITEPS00365. NIR_SIR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSI_SALTY
AccessionPrimary (citable) accession number: P17845
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 96 of the entry and version 3 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