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Q8EAZ9 (CYSJ_SHEON) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 73. 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:
Sulfite reductase [NADPH] flavoprotein alpha-component

Short name=SiR-FP
EC=1.8.1.2
Gene names
Name:cysJ
Ordered Locus Names:SO_3738
OrganismShewanella oneidensis (strain MR-1) [Reference proteome] [HAMAP]
Taxonomic identifier211586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length607 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. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component By similarity. HAMAP-Rule MF_01541

Catalytic activity

H2S + 3 NADP+ + 3 H2O = sulfite + 3 NADPH. HAMAP-Rule MF_01541

Cofactor

Binds 1 FAD per subunit By similarity. HAMAP-Rule MF_01541

Binds 1 FMN per subunit By similarity. HAMAP-Rule MF_01541

Pathway

Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. HAMAP-Rule MF_01541

Subunit structure

Alpha(8)-beta8. 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 – 607607Sulfite reductase [NADPH] flavoprotein alpha-component HAMAP-Rule MF_01541
PRO_0000199936

Regions

Domain66 – 204139Flavodoxin-like
Domain239 – 456218FAD-binding FR-type
Nucleotide binding72 – 765FMN By similarity
Nucleotide binding119 – 1246FMN By similarity
Nucleotide binding152 – 18332FMN By similarity
Nucleotide binding395 – 3984FAD By similarity
Nucleotide binding429 – 4313FAD By similarity
Nucleotide binding527 – 5359NADP By similarity

Sites

Binding site4971NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8EAZ9 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: C6042663547ACD22

FASTA60766,620
        10         20         30         40         50         60 
MLLKELSSLA SPLSQSQVDK LKQLTAELNS VQLAWVSGYL AATANTSGSA IQVAASVTEA 

        70         80         90        100        110        120 
QAAQTVTILY GSQTGNGRGI AKALAEKAKT QGYSVNLASM GEYNVRQLKQ ETLLLLVVST 

       130        140        150        160        170        180 
HGEGEAPDDA IELHKFLATK RAPQLNNLHY SVLALGDSSY EFFCQTGKDF DARLSALGAK 

       190        200        210        220        230        240 
ALLPLVECDV DYEAAAGQWH ADVLTAVKPL IQTTANVVAL NEINSTSAQV ASESEFTKQN 

       250        260        270        280        290        300 
PYRAEVLVSQ KITGRDSDRD VRHVEIDLGE SGLHYEVGDA LGVWFSNSEI LVGEILAGLG 

       310        320        330        340        350        360 
LAADAKVTVG SESISLKQAL IDKKELTQLY PGLVKAWAEL SASSELLALS EDKEQLRQFI 

       370        380        390        400        410        420 
LNHQFVDLVT NYKLPAEANL DANKLLELLR PLTPRLYSIA SSQTEVDTEV HLTVALVEDE 

       430        440        450        460        470        480 
HQGQTRFGGA SHFLASAQEG AEVKVYVEPN KHFRLPENPD TPVIMIGPGT GVAPFRAFMQ 

       490        500        510        520        530        540 
ERVAQGAKGD SWLFFGNPHF EQDFLYQTEW QQYLKNGDLT RIDVAFSRDQ AHKIYVQHRI 

       550        560        570        580        590        600 
KEQGQALWQW LQNGAHLYIC GDAERMAKDV HQALLAVAVE FGGLSSEAAE EYFETLRSHK 


RYQKDVY 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014299 Genomic DNA. Translation: AAN56721.1.
RefSeqNP_719277.1. NC_004347.2.

3D structure databases

ProteinModelPortalQ8EAZ9.
SMRQ8EAZ9. Positions 234-607.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING211586.SO_3738.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN56721; AAN56721; SO_3738.
GeneID1171388.
KEGGson:SO_3738.
PATRIC23527152. VBISheOne101494_3621.

Phylogenomic databases

eggNOGCOG0369.
HOGENOMHOG000282025.
KOK00380.
OMAHEFLQSK.
OrthoDBEOG6CVV7G.
PhylomeDBQ8EAZ9.

Enzyme and pathway databases

UniPathwayUPA00140; UER00207.

Family and domain databases

Gene3D1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
HAMAPMF_01541. CysJ.
InterProIPR010199. CysJ.
IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF000207. SiR-FP_CysJ. 1 hit.
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMSSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
TIGRFAMsTIGR01931. cysJ. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSJ_SHEON
AccessionPrimary (citable) accession number: Q8EAZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 73 of the entry and version 1 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