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P26475 (ASRB_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. 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

Names and origin

Protein namesRecommended name:
Anaerobic sulfite reductase subunit B
Gene names
Name:asrB
Ordered Locus Names:STM2549
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length272 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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.

Cofactor

Binds 1 2Fe-2S cluster per subunit By similarity.

Binds 1 FAD per subunit By similarity.

Pathway

Sulfur metabolism; sulfite reduction.

Subunit structure

The anaerobic sulfite reductase seems to consist of three subunits.

Subcellular location

Cytoplasm.

Induction

By sulfite. Repressed by oxygen.

Sequence similarities

Belongs to the PyrK family.

Contains 1 FAD-binding FR-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 272272Anaerobic sulfite reductase subunit B
PRO_0000148385

Regions

Domain14 – 10592FAD-binding FR-type
Nucleotide binding113 – 12917FAD By similarity
Nucleotide binding168 – 21346NAD By similarity

Sites

Metal binding2401Iron-sulfur (2Fe-2S) Potential
Metal binding2451Iron-sulfur (2Fe-2S) Potential
Metal binding2481Iron-sulfur (2Fe-2S) Potential
Metal binding2561Iron-sulfur (2Fe-2S) Potential
Binding site1661NAD By similarity

Experimental info

Sequence conflict161P → A in AAA99276. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P26475 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 5C73ACCC200AE302

FASTA27230,609
        10         20         30         40         50         60 
MSHCSCHDKP QHSLLPAAYR ILSITRHTPL EWNFRVAVDF PAHWGQFVEV SLPRVGEAPI 

        70         80         90        100        110        120 
SVSDYGDGWI DLLIRNVGKV TSALFTLKEG DNVWLRGCYG NGYPVDTLRH KPLLVVAGGT 

       130        140        150        160        170        180 
GVAPVKGLMR YFVENPQEIG QLDMILGYKN RDCVLYKEEM ATWRGKHNLV LTLDEGEADD 

       190        200        210        220        230        240 
RYQIGRVTDR LADMTLSDID TMQAIVVGPP IMITFTVKML LQKGLKPEQI WVDYERRMAC 

       250        260        270 
SVGKCGHCRM GEVYVCTDGP IFNYAVAQRF AD 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis and expression of the Salmonella typhimurium asr operon encoding production of hydrogen sulfide from sulfite."
Huang C.J., Barrett E.L.
J. Bacteriol. 173:1544-1553(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: EB303.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M57706 Genomic DNA. Translation: AAA99276.1.
AE006468 Genomic DNA. Translation: AAL21443.1.
PIRB38453.
RefSeqNP_461484.1. NC_003197.1.

3D structure databases

ProteinModelPortalP26475.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM2549.

Proteomic databases

PaxDbP26475.
PRIDEP26475.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL21443; AAL21443; STM2549.
GeneID1254071.
KEGGstm:STM2549.
PATRIC32383733. VBISalEnt20916_2689.

Phylogenomic databases

eggNOGCOG0543.
HOGENOMHOG000225119.
KOK16951.
OMAMECGIGH.
OrthoDBEOG6JX7JM.
PhylomeDBP26475.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12545.
SENT99287:GCTI-2563-MONOMER.
UniPathwayUPA00370.

Family and domain databases

Gene3D2.10.240.10. 1 hit.
InterProIPR012165. Cyt_c3_hydrogenase_gsu.
IPR019480. Dihydroorotate_DH_Fe-S-bd.
IPR017927. Fd_Rdtase_FAD-bd.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
IPR014260. Sulphite_reductase_B.
[Graphical view]
PfamPF10418. DHODB_Fe-S_bind. 1 hit.
PF00970. FAD_binding_6. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF006816. Cyc3_hyd_g. 1 hit.
SUPFAMSSF63380. SSF63380. 1 hit.
TIGRFAMsTIGR02911. sulfite_red_B. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASRB_SALTY
AccessionPrimary (citable) accession number: P26475
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2002
Last modified: July 9, 2014
This is version 108 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways