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Q8K9D3 (CYSJ_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:BUsg_413
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera ›

Protein attributes

Sequence length602 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.

Binds 1 FMN per subunit By similarity.

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 – 602602Sulfite reductase [NADPH] flavoprotein alpha-component HAMAP-Rule MF_01541
PRO_0000199921

Regions

Domain68 – 206139Flavodoxin-like
Domain237 – 451215FAD-binding FR-type
Nucleotide binding74 – 785FMN By similarity
Nucleotide binding121 – 1266FMN By similarity
Nucleotide binding154 – 18532FMN By similarity
Nucleotide binding389 – 3924FAD By similarity
Nucleotide binding423 – 4253FAD By similarity
Nucleotide binding522 – 5309NADP By similarity

Sites

Binding site4921NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8K9D3 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: FA3793147889B7B3

FASTA60269,930
        10         20         30         40         50         60 
MKNKNPFNIF FPLSLDKIEN LEKIKKNCSS IQYAWLSGYF WNLANQTPSR LICEKNEFFR 

        70         80         90        100        110        120 
KDNEEKIITI ISASQTGNAR QLAKRFNKYL KNENKKTNLI DAADYNFKKI KNERFLILII 

       130        140        150        160        170        180 
STQGEGEPPE EALSFYKFIM SKKAPRLENL HYSVFGLGDV SYNLFCQAGK DFDKRFSELG 

       190        200        210        220        230        240 
GKSLLHRLDS DIEYESNYIQ WSEELLLAIN KIDVSTCSVF KKNDKKNFID KLNYTKYKPA 

       250        260        270        280        290        300 
VATVLLNQKI TGRNSTKDVH HIELDITNSN IVYTPGDALG VWYQNSSQLI KQILKLLSIR 

       310        320        330        340        350        360 
ISDKVKVKDK IITIFEALKK NFELTTNTKH IIQKYTDVTQ NKFLKKIISD NKKLNNYVKK 

       370        380        390        400        410        420 
TPLLKMIYDH PKKLSSQQLI SILRPLKPRL YSISSSQSEM NDEVHITVGV VKKQISGTIH 

       430        440        450        460        470        480 
LGGSSSYLSQ FLKIDDSVKI FVEEKSNFRL PENKDVPIIM IGSGTGIAPF RAFIQQRDND 

       490        500        510        520        530        540 
KATGKNWIFF GNPNFTEDFL YQLEWQKYLK KKLLTKMSLA WSRDQKEKIY VQDKIRENGK 

       550        560        570        580        590        600 
ELWEWVNQGA QIYVCGNASK MAKDVEKELL DVFSKNGSMD IEESSEFLNN LRITRRYQRD 


VY

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References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE013218 Genomic DNA. Translation: AAM67958.1.
RefSeqNP_660747.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8K9D3.
SMRQ8K9D3. Positions 234-602.
ModBaseSearch...

Protein-protein interaction databases

STRING198804.BUsg413.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67958; AAM67958; BUsg_413.
GeneID1005748.
KEGGbas:BUsg413.
PATRIC21247670. VBIBucAph100086_0435.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0369.
KOK00380.
OMASDKDVRH.
ProtClustDBCLSK316168.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-460-MONOMER.
UniPathwayUPA00140; UER00207.

Family and domain databases

Gene3D1.20.990.10. 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.
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.
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_BUCAP
AccessionPrimary (citable) accession number: Q8K9D3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 1, 2002
Last modified: May 1, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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