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Reviewed, UniProtKB/Swiss-Prot A7MJ63 (CYSJ_ENTS8)

Last modified November 25, 2008. Version 13. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Sulfite reductase [NADPH] flavoprotein alpha-component
      Short name=SIR-FP
    EC=1.8.1.2
Gene names
Name: cysJ
Ordered Locus Names: ESA_00533
OrganismEnterobacter sakazakii (strain ATCC BAA-894) [Complete proteome] [HAMAP]
Taxonomic identifier290339 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCronobacter

Protein attributes

Sequence length600 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavo-protein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component By similarity.

Catalytic activity

H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 NADPH.

Cofactor

Binds 1 FAD per subunit By similarity.

Binds 1 FMN per subunit By similarity.

Subunit structure

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

Sequence similarities

Contains 1 FAD-binding FR-type domain.

Contains 1 flavodoxin-like domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 600600Sulfite reductase [NADPH] flavoprotein alpha-component
PRO_1000087636

Regions

Domain63 – 201139Flavodoxin-like
Domain235 – 449215FAD-binding FR-type
Nucleotide binding69 – 735FMN By similarity
Nucleotide binding149 – 18032FMN By similarity
Nucleotide binding237 – 28953FAD By similarity
Nucleotide binding473 – 600128NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
A7MJ63-1 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: 58E4C1E4C63B438B

FASTA60066,548
        10         20         30         40         50         60 
MTTQAPPNAL LPLSPEQLAR LQTATHDFTP TQLAWLSGYF WGMVNQQPGA AVMQKPAAPA 

        70         80         90        100        110        120 
SVITLISASQ TGNARRVAEA LRDDLLAAQL NVNLVNAGDY KFKQIAQEKL LIVVASTQGE 

       130        140        150        160        170        180 
GDPPEEAVAL HKFLLSKKAP KLDGTAFAVF GLGDTSYEHF CQAGKDFDTR LAELGAERLL 

       190        200        210        220        230        240 
DRVDADVEYQ AAAQAWRQRV VDVLKARVPK EAPSQAAITA SGAVNLVDST PYTKESPLTA 

       250        260        270        280        290        300 
TLSVNQKITG RHSEKDVRHI EIDLGDAGLR YQPGDALGVW YQNDPALVQE LLELLWLKGD 

       310        320        330        340        350        360 
EPVTVGEKTL PLSEALQWHF ELTVNTAAIV ENYATLTRSE ALLPLVGDKA KLQDYAARTP 

       370        380        390        400        410        420 
IVDMVRFAPA QLEADQLLGL LRPLTPRLYS IASSQAEVEN EVHITVGVVR FDIEGRVRAG 

       430        440        450        460        470        480 
GASSYLADRL EEDSEVRVFI EHNDNFRLPA TPETPVIMIG PGTGIAPFRA FMQQREADGA 

       490        500        510        520        530        540 
TGKNWLFFGN PHFTEDFLYQ VEWQRYVKEG LLTRIDLAWS RDQDHKIYVQ DKIREQGAEL 

       550        560        570        580        590        600 
WRWLQEGAHL YVCGDANRMA KDVEQALLEV IAAYGGMDAE AADEYLSELR VERRYQRDVY 

« Hide

References

[1]McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Fulton B., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000783 Genomic DNA. Translation: ABU75824.1.
RefSeqYP_001436661.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5551773.
GenomeReviewsGene locus ESA_00533 in contig CP000783_GR.
KEGGesa:ESA_00533.

Organism-specific databases

CMRSearch...

Family and domain databases

HAMAPMF_01541.
[Tree]
InterProIPR010199. CysJ.
IPR003097. FAD-binding_1.
IPR001094. Flavdoxin_like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. FPN_cyt_redctse.
IPR001433. OxRdtase_FAD/NAD_bd.
[Graphical view]
PfamPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
TIGRFAMsTIGR01931. cysJ. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSJ_ENTS8
AccessionPrimary (citable) accession number: A7MJ63
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 2, 2007
Last modified: November 25, 2008
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents