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Q7VQH2 (CYSJ_BLOFL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Bfl158
OrganismBlochmannia floridanus [Complete proteome] [HAMAP]
Taxonomic identifier203907 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › ant endosymbionts › Candidatus Blochmannia

Protein attributes

Sequence length610 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 MF_01541

Catalytic activity

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

Cofactor

Binds 1 FAD per subunit By similarity. HAMAP MF_01541

Binds 1 FMN per subunit By similarity. HAMAP MF_01541

Pathway

Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1. HAMAP 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 – 610610Sulfite reductase [NADPH] flavoprotein alpha-component HAMAP MF_01541
PRO_0000199922

Regions

Domain68 – 206139Flavodoxin-like
Domain243 – 459217FAD-binding FR-type
Nucleotide binding74 – 785FMN By similarity
Nucleotide binding121 – 1266FMN By similarity
Nucleotide binding154 – 18532FMN By similarity
Nucleotide binding397 – 4004FAD By similarity
Nucleotide binding431 – 4333FAD By similarity
Nucleotide binding530 – 5389NADP By similarity

Sites

Binding site5001NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VQH2 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 1D5507E560F6C562

FASTA61069,495
        10         20         30         40         50         60 
MSIMGLLSSE QLNQLKLVLD TLSKNQLIWL SGYLLGLVNS QTSTDIGVTA SGVSAGLELK 

        70         80         90        100        110        120 
PDLIDNTIIV ISASQTGNAR NIAKQLYSDL VEAGLRAVLF SAGEYKFKKI SEISLLIFIT 

       130        140        150        160        170        180 
STHGEGEPPE EALALYKYLF SEKALRMEKT SFIVLSLGDR SYEYFAKAGK DFDKRFEDLG 

       190        200        210        220        230        240 
ANRLYDRVDL DVDFQSEVDK WKEKVVSLCK SKIVSIVSKD KCINIQNNIV FKKKNPVTSY 

       250        260        270        280        290        300 
CKEFPLIAYL LNRQKITSCN SLKDVHHLEF DISGSGLCYQ PGDALGIWYE NDYNLVYELL 

       310        320        330        340        350        360 
ELLNLTGRES VQIKNQSMCL DEALVKYCDL TQNTPVVVKS IATISQDKIL LNLLQNQNQL 

       370        380        390        400        410        420 
NSFCSTTPIV EMFYQISMTK QLSSQELIQI LRPMRPRFYS IASAQSEVGE EIHITVSVVR 

       430        440        450        460        470        480 
YTINGRIRSG GASSYLVDRV QDHDEIRIFV ESNDNFRLPK DPNVSIIMIG AGTGIAPFRS 

       490        500        510        520        530        540 
FMQQRALDKA LGKNWLFFGN LKFTDDFLYQ IEWKTYFKSG ILNKIDTAWS RDQDYKVYVQ 

       550        560        570        580        590        600 
DKLLSNGLEL WDWIQKGAYI YVCGDAKYMA RDVEQALVTV VSIHGNMNMD QSNDFWNEMR 

       610 
VQHRYQRDIY

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References

[1]"The genome sequence of Blochmannia floridanus: comparative analysis of reduced genomes."
Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F., Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B., van Ham R.C.H.J., Gross R., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003) [PubMed: 12886019] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX248583 Genomic DNA. Translation: CAD83679.1.
RefSeqNP_878464.1. NC_005061.1.

3D structure databases

ProteinModelPortalQ7VQH2.
SMRQ7VQH2. Positions 236-610.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7VQH2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1499358.
GenomeReviewsGene locus Bfl158 in contig BX248583_GR.
KEGGbfl:Bfl158.
PATRIC31963909. VBICanBlo38691_0157.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0369.
HOGENOMHBG736048.
OMAESADEYL.
PhylomeDBQ7VQH2.
ProtClustDBCLSK280717.

Enzyme and pathway databases

BioCycCBLO203907:BFL158-MONOMER.

Family and domain databases

HAMAPMF_01541. CysJ.
[Tree]
InterProIPR010199. CysJ.
IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
Gene3DG3DSA:1.20.990.10. NADPH_Cyt_P450_Rdtase_dom3. 1 hit.
KOK00380.
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.
SUPFAMSSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
TIGRFAMsTIGR01931. CysJ. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSJ_BLOFL
AccessionPrimary (citable) accession number: Q7VQH2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 49 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

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