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A7ZQK7 (CYSJ_ECO24) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 36. 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:EcE24377A_3066
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length599 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 – 599599Sulfite reductase [NADPH] flavoprotein alpha-component HAMAP MF_01541
PRO_1000087632

Regions

Domain64 – 202139Flavodoxin-like
Domain234 – 448215FAD-binding FR-type
Nucleotide binding70 – 745FMN By similarity
Nucleotide binding117 – 1226FMN By similarity
Nucleotide binding150 – 18132FMN By similarity
Nucleotide binding386 – 3894FAD By similarity
Nucleotide binding420 – 4223FAD By similarity
Nucleotide binding519 – 5279NADP By similarity

Sites

Binding site4891NADP By similarity

Sequences

Sequence LengthMass (Da)Tools
A7ZQK7 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: CA493E97DA034046

FASTA59966,252
        10         20         30         40         50         60 
MTTQVPPSAL LPLNPEQLAR LQAATTDLTP TQLAWVSGYF WGVLNQQPAA LAATPAPAAE 

        70         80         90        100        110        120 
MPGITIISAS QTGNARRVAE ALRDDLLAAK LNVKLVNAGD YKFKQIASEK LLIVVTSTQG 

       130        140        150        160        170        180 
EGEPPEEAVA LHKFLFSKKA PKLENTAFAV FSLGDSSYEF FCQSGKDFDS KLAELGGERL 

       190        200        210        220        230        240 
LDRVDADVEY QAAASEWRAR VVDALKSRAP VAAPSQSVAT GAVNEIHTSP YSKDAPLVAS 

       250        260        270        280        290        300 
LSVNQKITGR NSEKDVRHIE IDLGDSGLRY QPGDALGVWY QNDPALVKEL VELLWLKGDE 

       310        320        330        340        350        360 
PVTVEGKTLP LNEALQWHFE LTVNTANIVE NYATLTRSET LLPLVGDKAK LQHYAATTPI 

       370        380        390        400        410        420 
VDMVRFSPAQ LDAEALINLL RPLTPRLYSI ASSQAEVENE VHVTVGVVRY DVEGRARAGG 

       430        440        450        460        470        480 
ASSFLADRVE EEGEVRVFIE HNDNFRLPAN PETPVIMIGP GTGIAPFRAF MQQRAADEAP 

       490        500        510        520        530        540 
GKNWLFFGNP HFTEDFLYQV EWQRYVKDGV LTRIDLAWSR DQKEKVYVQD KLREQGAELW 

       550        560        570        580        590 
RWINDGAHIY VCGDANRMAK DVEQALLEVI AEFGGMDTEA ADEFLSELRV ERRYQRDVY

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E24377A / ETEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000800 Genomic DNA. Translation: ABV20250.1.
RefSeqYP_001464086.1. NC_009801.1.

3D structure databases

ProteinModelPortalA7ZQK7.
SMRA7ZQK7. Positions 59-599.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7ZQK7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000019669; EBESCP00000018731; EBESCG00000018723.
GeneID5587243.
GenomeReviewsGene locus EcE24377A_3066 in contig CP000800_GR.
KEGGecw:EcE24377A_3066.
NMPDRfig|331111.3.peg.780.
PATRIC18295448. VBIEscCol31211_3345.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0369.
GeneTreeEBGT00050000009975.
HOGENOMHBG736048.
OMAESADEYL.
ProtClustDBPRK10953.

Enzyme and pathway databases

BioCycECOL331111:ECE24377A_3066-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_ECO24
AccessionPrimary (citable) accession number: A7ZQK7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 23, 2007
Last modified: January 25, 2012
This is version 36 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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