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Q66ED3 (CYSI_YERPS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. 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:YPTB0760
OrganismYersinia pseudotuberculosis [Complete proteome] [HAMAP]
Taxonomic identifier633 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length576 AA.
Sequence statusComplete.
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 By similarity. HAMAP MF_01540

Catalytic activity

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

Cofactor

Binds 1 siroheme per subunit By similarity. HAMAP MF_01540

Binds 1 4Fe-4S cluster per subunit By similarity. HAMAP MF_01540

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 By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 576576Sulfite reductase [NADPH] hemoprotein beta-component HAMAP MF_01540
PRO_0000199918

Sites

Metal binding4351Iron-sulfur (4Fe-4S) By similarity
Metal binding4411Iron-sulfur (4Fe-4S) By similarity
Metal binding4801Iron-sulfur (4Fe-4S) By similarity
Metal binding4841Iron (siroheme axial ligand) By similarity
Metal binding4841Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q66ED3 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 976E5D7D48A69B43

FASTA57664,101
        10         20         30         40         50         60 
MNEKHPGPLV VSGKLSDGER MKSESNFLRG TIAEDLNNGL TGGFSGDNFL LIRFHGMYQQ 

        70         80         90        100        110        120 
DDRDIRAERA EQKLEPRHAM MLRCRLPGGI ITPQQWLGID KFAADNTLYG SIRITNRQTF 

       130        140        150        160        170        180 
QFHGILKGNV KPAHQLLNEL GLDALATAND VNRNVLCTSN PVESALHQEA YEWAKKISEH 

       190        200        210        220        230        240 
LLPRTRAYAE IWLDAEKVAT TDEEPILGAT YLPRKFKTTV VIPPQNDVDL HANDLNFVAV 

       250        260        270        280        290        300 
ADKGKLIGFN VLVGGGLSIA HGDKNTYPRK ASEFGYIPLK HTLAIAEAVV TTQRDWGNRT 

       310        320        330        340        350        360 
DRKNAKTKYT LERVGVETFK AEVEKRAGVS FSAIKPYQFT GRGDRIGWVK GVDKKWHLTL 

       370        380        390        400        410        420 
FIENGRLLDY PGRSLKTGVA EIAKIHQGDF RLTANQNLIV AGVPEKDKAR IEALAREHGL 

       430        440        450        460        470        480 
MDDHVTSQRE NSMACVSFPT CPLAMAEAER FLPEFVTRVE GILQQHGLAD EHIVLRVTGC 

       490        500        510        520        530        540 
PNGCGRALLA EVGLVGKAVG RYNLHLGGNR EGTRIPRMYR ENITADEILL ITDQLVGRWA 

       550        560        570 
KERHVDEGFG DFVIRAGVIA PVIDSARDFY DVQEAM 

« Hide

References

[1]"Insights into the evolution of Yersinia pestis through whole-genome comparison with Yersinia pseudotuberculosis."
Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., Simonet M., Chenal-Francisque V., Souza B. expand/collapse author list , Dacheux D., Elliott J.M., Derbise A., Hauser L.J., Garcia E.
Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004) [PubMed: 15358858] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IP32953 / Serotype I.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX936398 Genomic DNA. Translation: CAH20000.1.
RefSeqYP_069301.1. NC_006155.1.

3D structure databases

ProteinModelPortalQ66ED3.
SMRQ66ED3. Positions 81-571.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2955406.
GenomeReviewsGene locus YPTB0760 in contig BX936398_GR.
KEGGyps:YPTB0760.
NMPDRfig|273123.1.peg.885.
PATRIC18639816. VBIYerPse22266_1001.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG626671.
OMAMTLDGFR.
ProtClustDBPRK13504.

Enzyme and pathway databases

BioCycYPSE273123:YPTB0760-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_YERPS
AccessionPrimary (citable) accession number: Q66ED3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: October 11, 2004
Last modified: January 25, 2012
This is version 53 of the entry and version 1 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