ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P57503

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name CYSJ_BUCAI
Primary accession number P57503
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 2000
Sequence was last modified on December 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 49)
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: BU428
From
Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum symbiotic bacterium) [TaxID: 118099] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tokyo 1998;
DOI=10.1038/35024074; PubMed=10993077 [NCBI, ExPASy, EBI, Israel, Japan]
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS.";
Nature 407:81-86(2000).
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
BA000003; BAB13126.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_240240.1; -.
3D structure databases
HSSP P38038; 1DDG. [HSSP ENTRY / PDB]
ModBase P57503.
Enzyme and pathway databases
BioCyc BSP107806:BU428-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 P57503.
Genome annotation databases
GeneID 1109776; -.
GenomeReviews BA000003_GR; BU428.
KEGG buc:BU428; -.
Phylogenomic databases
HOGENOM P57503; -.
Genome annotation databases
CMR P57503; BU428.
Other
ProtoNet P57503.
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   601  601     Sulfite reductase [NADPH] flavoprotein alpha-component. PRO_0000199920
DOMAIN   65   203  139     Flavodoxin-like. 
DOMAIN   236   450  215     FAD-binding FR-type. 
NP_BIND   71    75  5     FMN (By similarity). 
NP_BIND   151   182  32     FMN (By similarity). 
NP_BIND   238   290  53     FAD (By similarity). 
NP_BIND   474   601  128     NADP (By similarity). 
Sequence information
Length: 601 AA [This is the length of the unprocessed precursor] Molecular weight: 69231 Da [This is the MW of the unprocessed precursor] CRC64: A7BDD35F0CCF0E8F [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKNQNKFDPV FPLSSEQLNN LKELERTCTN IQSAWLSGYF WKIANQTSNI TSFQTNESEK 

        70         80         90        100        110        120 
NDPVITIISA SQTGNAKLLS KRLYEYFNKN NKISRLIDAM DYKFKKIKDE KILILIISTQ 

       130        140        150        160        170        180 
GEGEPPEEAL SFYKFIMSKN APNLNNLYYS VFGLGDTSYN LFCQAGKDFD KRFKELGGNS 

       190        200        210        220        230        240 
LLDRFDADIE YEDNYNKWSQ DLLQSINSKE KIYKSSVSYI DQENTLILSK NHYTKKNPAE 

       250        260        270        280        290        300 
GIILTNQKIT GRNSKKDVHH IEIDISNLNI KYSPGDALGV WYKNDSNLVK NILELLSINI 

       310        320        330        340        350        360 
SETITIKNDV ITIFDALQNH FELTNNTKNI IKSYANFSKN KFLKDIISND SDLENYTINT 

       370        380        390        400        410        420 
PLIKMIHDHP LKLSSQQLIG LLRPLTPRLY SISSSQEEID NEIHITVGVV KKLISGHVYL 

       430        440        450        460        470        480 
GGASGYLSQS LKSDDIIKIF IQTNDNFRLP INKNTPIIMI SSGTGIAPFR AFMQQRDNDN 

       490        500        510        520        530        540 
ADGKNWLFFG NPNFTEDFLY QVEWQKYIKK GLITNMNLAW SQDQKNKIYV QDRIRENSQE 

       550        560        570        580        590        600 
IWSWIEEGAQ IYVCGNASKM AKDVEKALLD IISHNAHLNL EESQEFLNNL RLNKRYKRDV 


Y
P57503 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!