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UniProtKB/Swiss-Prot entry Q1R7T4

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CYSJ_ECOUT
Primary accession number Q1R7T4
Secondary accession numbers None
Integrated into Swiss-Prot on June 26, 2007
Sequence was last modified on May 16, 2006 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 17)
Name and origin of the protein
Protein name Sulfite reductase [NADPH] flavoprotein alpha-component
Synonyms SIR-FP
EC 1.8.1.2
Gene name
Name: cysJ
OrderedLocusNames: UTI89_C3128
From
Escherichia coli (strain UTI89 / UPEC) [TaxID: 364106] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0600938103; PubMed=16585510 [NCBI, ExPASy, EBI, Israel, Japan]
Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I.;
"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach.";
Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CP000243; ABE08580.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_542111.1; -.
3D structure databases
SMR Q1R7T4; 64-209, 226-599.
ModBase Q1R7T4.
Enzyme and pathway databases
BioCyc ECOL364106:UTI89_C3128-MON; -.
Ontologies
GO
GO:0004783; Molecular function: sulfite reductase (NADPH) activity (inferred from electronic annotation from HAMAP).
GO:0000103; Biological process: sulfate assimilation (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01541; -; 1.
PBIL [Tree]
InterPro IPR010199; CysJ.
IPR003097; FAD-binding_1.
IPR001094; Flavdoxin_like.
IPR008254; Flavodoxin/NO_synth.
IPR001709; FPN_cyt_redctse.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.
Pfam PF00667; FAD_binding_1; 1.
PF00258; Flavodoxin_1; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00369; FLAVODOXIN.
PR00371; FPNCR.
TIGRFAMs TIGR01931; cysJ; 1.
PROSITE PS51384; FAD_FR; 1.
PS50902; FLAVODOXIN_LIKE; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q1R7T4.
Genome annotation databases
GeneID 3990453; -.
GenomeReviews CP000243_GR; UTI89_C3128.
KEGG eci:UTI89_C3128; -.
Phylogenomic databases
HOGENOM Q1R7T4; -.
Genome annotation databases
CMR Q1R7T4; UTI89_C3128.
Other
ProtoNet Q1R7T4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Cysteine biosynthesis; Electron transport; FAD; Flavoprotein; FMN; NADP; Oxidoreductase; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   599  599     Sulfite reductase [NADPH] flavoprotein alpha-component. PRO_0000292966
DOMAIN   64   202  139     Flavodoxin-like. 
DOMAIN   234   448  215     FAD-binding FR-type. 
NP_BIND   70    74  5     FMN (By similarity). 
NP_BIND   150   181  32     FMN (By similarity). 
NP_BIND   236   288  53     FAD (By similarity). 
NP_BIND   472   599  128     NADP (By similarity). 
Sequence information
Length: 599 AA [This is the length of the unprocessed precursor] Molecular weight: 66312 Da [This is the MW of the unprocessed precursor] CRC64: 9E957AD0872A050E [This is a checksum on the sequence] 
        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 GTVNEIHTSP YSKDAPLAAS 

       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 HNDNFRLPTN PETPVIMIGP GTGIAPFRAF MQQRAADEAP 

       490        500        510        520        530        540 
GKNWLFFGNP HFTEDFLYQV EWQRYVKEGV LTRIDLAWSR DQKEKIYVQD KLREQGAELW 

       550        560        570        580        590 
RWINDGAHIY VCGDANRMAK DVEQALLEVI AEFGGMDTEA ADEFLSELRV ERRYQRDVY
Q1R7T4 in FASTA format

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