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P17846 (CYSI_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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

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:b2763, JW2733
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length570 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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-Rule MF_01540

Catalytic activity

H2S + 3 NADP+ + 3 H2O = sulfite + 3 NADPH. HAMAP-Rule 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-Rule 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 caution

The sequence AAA23651.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA68816.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 570569Sulfite reductase [NADPH] hemoprotein beta-component HAMAP-Rule MF_01540
PRO_0000199896

Sites

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

Experimental info

Sequence conflict231H → L in AAA23651. Ref.1

Secondary structure

.................................................................................. 570
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17846 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 03B41FEE6AB349C6

FASTA57063,998
        10         20         30         40         50         60 
MSEKHPGPLV VEGKLTDAER MKHESNYLRG TIAEDLNDGL TGGFKGDNFL LIRFHGMYQQ 

        70         80         90        100        110        120 
DDRDIRAERA EQKLEPRHAM LLRCRLPGGV ITTKQWQAID KFAGENTIYG 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 LERVGVETFK AEVERRAGIK FEPIRPYEFT GRGDRIGWVK GIDDNWHLTL 

       370        380        390        400        410        420 
FIENGRILDY PARPLKTGLL EIAKIHKGDF RITANQNLII AGVPESEKAK IEKIAKESGL 

       430        440        450        460        470        480 
MNAVTPQREN SMACVSFPTC PLAMAEAERF LPSFIDNIDN LMAKHGVSDE HIVMRVTGCP 

       490        500        510        520        530        540 
NGCGRAMLAE VGLVGKAPGR YNLHLGGNRI GTRIPRMYKE NITEPEILAS LDELIGRWAK 

       550        560        570 
EREAGEGFGD FTVRAGIIRP VLDPARDLWD 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
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 277:1453-1462(1997) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Characterisation of the gene cysH and of its product phospho-adenylylsulphate reductase from Escherichia coli."
Krone F.A., Westphal G., Schwenn J.D.
Mol. Gen. Genet. 225:314-319(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 344-570.
Strain: K12.
[5]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-13.
Strain: K12 / EMG2.
[6]"Sulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions."
Crane B.R., Siegel L.M., Getzoff E.D.
Science 270:59-67(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[7]"Structures of the siroheme- and Fe4S4-containing active center of sulfite reductase in different states of oxidation: heme activation via reduction-gated exogenous ligand exchange."
Crane B.R., Siegel L.M., Getzoff E.D.
Biochemistry 36:12101-12119(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M23008 Genomic DNA. Translation: AAA23651.1. Different initiation.
U29579 Genomic DNA. Translation: AAA69273.1.
U00096 Genomic DNA. Translation: AAC75805.1.
AP009048 Genomic DNA. Translation: BAE76840.1.
Y07525 Genomic DNA. Translation: CAA68816.1. Different initiation.
PIRRDECSH. G65057.
RefSeqNP_417243.1. NC_000913.3.
YP_490972.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOPX-ray1.60A74-570[»]
2AOPX-ray1.75A74-570[»]
2GEPX-ray1.90A74-570[»]
3AOPX-ray2.10A74-570[»]
3GEOX-ray2.10A74-570[»]
4AOPX-ray1.80A74-570[»]
4G38X-ray1.56A1-570[»]
4G39X-ray2.40A1-570[»]
4GEPX-ray2.00A74-570[»]
4HTRX-ray1.60A64-570[»]
5AOPX-ray2.20A74-570[»]
5GEPX-ray2.10A74-570[»]
6GEPX-ray1.80A74-570[»]
7GEPX-ray2.40A74-570[»]
8GEPX-ray2.20A74-570[»]
ProteinModelPortalP17846.
SMRP17846. Positions 81-570.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9380N.
IntActP17846. 10 interactions.
STRING511145.b2763.

Proteomic databases

PaxDbP17846.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75805; AAC75805; b2763.
BAE76840; BAE76840; BAE76840.
GeneID12933282.
947231.
KEGGecj:Y75_p2701.
eco:b2763.
PATRIC32120938. VBIEscCol129921_2861.

Organism-specific databases

EchoBASEEB0187.
EcoGeneEG10190. cysI.

Phylogenomic databases

eggNOGCOG0155.
HOGENOMHOG000218418.
KOK00381.
OMAELHQEAY.
OrthoDBEOG6W9XFB.
PhylomeDBP17846.

Enzyme and pathway databases

BioCycEcoCyc:BETACOMP-MONOMER.
ECOL316407:JW2733-MONOMER.
MetaCyc:BETACOMP-MONOMER.
UniPathwayUPA00140; UER00207.

Gene expression databases

GenevestigatorP17846.

Family and domain databases

Gene3D3.90.480.10. 2 hits.
HAMAPMF_01540. CysI.
InterProIPR011786. CysI.
IPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
IPR006066. NO2/SO3_Rdtase_FeS/sirohaem_BS.
[Graphical view]
PfamPF01077. NIR_SIR. 1 hit.
PF03460. NIR_SIR_ferr. 2 hits.
[Graphical view]
PRINTSPR00397. SIROHAEM.
SUPFAMSSF55124. SSF55124. 2 hits.
TIGRFAMsTIGR02041. CysI. 1 hit.
PROSITEPS00365. NIR_SIR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP17846.
PROP17846.

Entry information

Entry nameCYSI_ECOLI
AccessionPrimary (citable) accession number: P17846
Secondary accession number(s): Q2MA66
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 140 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

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