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A4WDW1 (CYSJ_ENT38) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:Ent638_3227
OrganismEnterobacter sp. (strain 638) [Complete proteome] [HAMAP]
Taxonomic identifier399742 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Enterobacter

Protein attributes

Sequence length601 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 – 601601Sulfite reductase [NADPH] flavoprotein alpha-component HAMAP MF_01541
PRO_1000087635

Regions

Domain64 – 202139Flavodoxin-like
Domain236 – 450215FAD-binding FR-type
Nucleotide binding70 – 745FMN By similarity
Nucleotide binding117 – 1226FMN By similarity
Nucleotide binding150 – 18132FMN By similarity
Nucleotide binding388 – 3914FAD By similarity
Nucleotide binding422 – 4243FAD By similarity
Nucleotide binding521 – 5299NADP By similarity

Sites

Binding site4911NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
A4WDW1 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: D4C25C7138BF8496

FASTA60166,366
        10         20         30         40         50         60 
MTTQAPPSNL LPLNPEQLAR LQAATTDFSP TQLAWVSGYF WGMLNQQPGA VVNAPATAVE 

        70         80         90        100        110        120 
IPAITLISAS QTGNARRVAE ALRDDLLAAK LNVNLVNAGD YKFKQIASEK LVVVVASTQG 

       130        140        150        160        170        180 
EGEPAEEAVA LHKFLFSKKA PKLDGTAFAV FGLGDTSYEF FCQSGKDFDS KLAELGAERL 

       190        200        210        220        230        240 
LDRVDADVEY QAAAAEWRAR IVDVLKARVP KDTPAQAANS ASGAVNEVST SPYTKEEPLV 

       250        260        270        280        290        300 
ASLSVNQKIT GRDSEKDVRH IEIDLGDSGL RYQPGDALGV WYQNDPALVK ELVELLWLKG 

       310        320        330        340        350        360 
TEQVNVEGKT LPLSEALQWH FELTVNTANI VENYATLTRS ETLLPLVGDK AKLQHYAATT 

       370        380        390        400        410        420 
PIVDMVRFSP AQLDAEALIG LLRPLTPRLY SIASSQAEVE SEVHITVGAV RFDIEGRARA 

       430        440        450        460        470        480 
GGASSFLADR VEEEGEVRVF IEHNDNFRLP ANPETPVIMI GPGTGIAPFR AFMQQRAAEE 

       490        500        510        520        530        540 
APGKNWLFFG NPHFTEDFLY QVEWQRYVKE GVLSRIDLAW SRDQKQKIYV QDKLREQGAE 

       550        560        570        580        590        600 
LWAWINNGAH LYVCGDANRM AKDVEQALLE VIAEFGGMDI ETADEFLSEL RVERRYQRDV 


Y

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References

[1]"Complete sequence of chromosome of Enterobacter sp. 638."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 638.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000653 Genomic DNA. Translation: ABP61891.1.
RefSeqYP_001177942.1. NC_009436.1.

3D structure databases

ProteinModelPortalA4WDW1.
SMRA4WDW1. Positions 64-208, 228-601.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4WDW1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5112941.
GenomeReviewsGene locus Ent638_3227 in contig CP000653_GR.
KEGGent:Ent638_3227.
NMPDRfig|399742.4.peg.3073.
PATRIC20416167. VBIEntSp101211_3386.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0369.
HOGENOMHBG736048.
OMAKIQPRYY.
PhylomeDBA4WDW1.
ProtClustDBPRK10953.

Enzyme and pathway databases

BioCycESP42895:ENT638_3227-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_ENT38
AccessionPrimary (citable) accession number: A4WDW1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 29, 2007
Last modified: January 25, 2012
This is version 43 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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