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P0A1Y3 (ASRC_SALTI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. 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:
Anaerobic sulfite reductase subunit C
EC=1.8.1.-
Gene names
Name:asrC
Ordered Locus Names:STY2796, t0306
OrganismSalmonella typhi [Complete proteome] [HAMAP]
Taxonomic identifier90370 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

This enzyme catalyzes the hydrogen sulfide production from sulfite. It is strictly anaerobic. It is regulated by electron acceptors rather than by cysteine By similarity.

Catalytic activity

Hydrogen sulfide + 3 NAD+ + 3 H2O = sulfite + 3 NADH.

Cofactor

Binds 3 4Fe-4S clusters per subunit By similarity.

Binds 1 siroheme per subunit By similarity.

Pathway

Sulfur metabolism; sulfite reduction.

Subunit structure

The anaerobic sulfite reductase seems to consist of three subunits By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

Contains 2 4Fe-4S ferredoxin-type domains.

Ontologies

Keywords
   Biological processElectron transport
Transport
   Cellular componentCytoplasm
   DomainRepeat
   Ligand4Fe-4S
Heme
Iron
Iron-sulfur
Metal-binding
NAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processelectron transport chain

Inferred from electronic annotation. Source: UniProtKB-KW

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

electron carrier activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

oxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337Anaerobic sulfite reductase subunit C
PRO_0000199964

Regions

Domain171 – 200304Fe-4S ferredoxin-type 1
Domain203 – 232304Fe-4S ferredoxin-type 2

Sites

Metal binding1151Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1211Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1531Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1571Iron (siroheme axial ligand) By similarity
Metal binding1571Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1801Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1831Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1861Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1901Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding2121Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding2151Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding2181Iron-sulfur 3 (4Fe-4S) By similarity
Metal binding2221Iron-sulfur 2 (4Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A1Y3 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 183FE2F669B34CBF

FASTA33737,291
        10         20         30         40         50         60 
MSIDIDIIKA RAKNEYRLSK VRGEAMISVR IPGGILPAHL LTVARDIAET WGNGQIHLTT 

        70         80         90        100        110        120 
RQKLAMPGIR YEDIDNVNAA LEPFLREIEI ELCDVQVEDT KAGYLAIGGR NIVACQGNRI 

       130        140        150        160        170        180 
CQKANTDTTG LSRRLEKLVY PSPYHLKTVI VGCPNDCAKA SMADLGIIGV AKMRFTADRC 

       190        200        210        220        230        240 
IGCGACVKAC SHHAVGCLAL KNGKAVKEES ACIGCGECVL ACPTLAWQRK PDQLWQVRLG 

       250        260        270        280        290        300 
GRTSKKTPRV GKLFLNWVTE DVIKQVIVNL YEFEKEMLGG KPIYLHMGHL IDKGGYLRFK 

       310        320        330 
ERVLRGVQLN PEAMVAERIY WAEDESVARM HLKPAGH

« Hide

References

[1]"Complete genome sequence of a multiple drug resistant Salmonella enterica serovar Typhi CT18."
Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., Davis P. expand/collapse author list , Davies R.M., Dowd L., White N., Farrar J., Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:848-852(2001) [PubMed: 11677608] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CT18.
[2]"Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18."
Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.
J. Bacteriol. 185:2330-2337(2003) [PubMed: 12644504] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700931 / Ty2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL627275 Genomic DNA. Translation: CAD02753.1.
AE014613 Genomic DNA. Translation: AAO68030.1.
RefSeqNP_457081.1. NC_003198.1.
NP_804181.1. NC_004631.1.

3D structure databases

ProteinModelPortalP0A1Y3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1067914.
1249106.
GenomeReviewsGene locus t0306 in contig AE014613_GR.
Gene locus STY2796 in contig AL513382_GR.
KEGGstt:t0306.
sty:STY2796.
PATRIC18543602. VBISalEnt120419_2842.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG419834.
OMAGRTGKQT.
ProtClustDBCLSK2301998.

Enzyme and pathway databases

BioCycSENT209261:T0306-MONOMER.
SENT220341:STY2796-MONOMER.

Family and domain databases

InterProIPR001450. 4Fe4S-bd_dom.
IPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR005117. NiRdtase/SiRdtase_haem-b_fer.
IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
IPR006066. NO2/SO3_Rdtase_FeS/sirohaem_BS.
IPR014261. Sulphite_reductase_C.
[Graphical view]
Gene3DG3DSA:3.90.480.10. G3DSA:3.90.480.10. 1 hit.
KOK00385.
PfamPF00037. Fer4. 2 hits.
PF01077. NIR_SIR. 1 hit.
PF03460. NIR_SIR_ferr. 1 hit.
[Graphical view]
PRINTSPR00397. SIROHAEM.
SUPFAMSSF55124. NiR_SiRalpha_1/3. 1 hit.
TIGRFAMsTIGR02912. Sulfite_red_C. 1 hit.
PROSITEPS00198. 4FE4S_FER_1. 1 hit.
PS51379. 4FE4S_FER_2. 2 hits.
PS00365. NIR_SIR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASRC_SALTI
AccessionPrimary (citable) accession number: P0A1Y3
Secondary accession number(s): P26476
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: January 25, 2012
This is version 52 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

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