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UniProtKB/Swiss-Prot entry A5F3I5


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

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Entry information
Entry name CYSI_VIBC3
Primary accession number A5F3I5
Secondary accession numbers None
Integrated into Swiss-Prot on February 26, 2008
Sequence was last modified on June 12, 2007 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 13)
Name and origin of the protein
Protein name Sulfite reductase [NADPH] hemoprotein beta-component
Synonyms SIR-HP
SIRHP
EC 1.8.1.2
Gene name
Name: cysI
OrderedLocusNames: VC0395_A2796
From
Vibrio cholerae serotype O1 (strain ATCC 39541 / Ogawa 395 / O395) [TaxID: 345073] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae; Vibrio.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Heidelberg J.;
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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
CP000627; ABQ21061.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_001218654.1; -.
3D structure databases
ModBase A5F3I5.
Ontologies
GO
GO:0009337; Cellular component: sulfite reductase complex (NADPH) (inferred from electronic annotation from InterPro).
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from InterPro).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037; Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0004783; Molecular function: sulfite reductase (NADPH) activity (inferred from electronic annotation from HAMAP).
GO:0019344; Biological process: cysteine biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0000103; Biological process: sulfate assimilation (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01540; -; 1.
PBIL [Tree]
InterPro IPR011786; CysI.
IPR006066; Nir_Si_BS.
IPR006067; Nir_Sir_4Fe4S.
IPR005117; NiRdtase/SiRdtase_haem-b_fer.
Graphical view of domain structure.
Pfam PF01077; NIR_SIR; 1.
PF03460; NIR_SIR_ferr; 2.
Pfam graphical view of domain structure.
PRINTS PR00397; SIROHAEM.
TIGRFAMs TIGR02041; CysI; 1.
PROSITE PS00365; NIR_SIR; 1.
Genome annotation databases
GeneID 5135522; -.
GenomeReviews CP000627_GR; VC0395_A2796.
KEGG vco:VC0395_A2796; -.
CMR A5F3I5; VC0395_A2796.
Other
ProtoNet A5F3I5.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
4Fe-4S; Amino-acid biosynthesis; Complete proteome; Cysteine biosynthesis; Heme; Iron; Iron-sulfur; Metal-binding; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   577  577     Sulfite reductase [NADPH] hemoprotein beta-component. PRO_1000073552
METAL   440   440        Iron-sulfur (4Fe-4S) (By similarity). 
METAL   446   446        Iron-sulfur (4Fe-4S) (By similarity). 
METAL   486   486        Iron-sulfur (4Fe-4S) (By similarity). 
METAL   490   490        Iron (siroheme axial ligand) (By similarity). 
METAL   490   490        Iron-sulfur (4Fe-4S) (By similarity). 
Sequence information
Length: 577 AA [This is the length of the unprocessed precursor] Molecular weight: 64371 Da [This is the MW of the unprocessed precursor] CRC64: 807070BF8B98E6DA [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSANQNPSVQ EVLGEVLGPW SDNERLKRES HFLRGTIEQD LQDRITGGFT ADNFQLIRFH 

        70         80         90        100        110        120 
GMYQQDDRDI RAERSKQKLE PLHNVMLRAR MPGGIITPHQ WLAIDKFATE HTLYGSIRLT 

       130        140        150        160        170        180 
TRQTFQFHGV LKPNIKLMHQ TLNSIGIDSI ATAGDVNRNV LCTSNPVESQ LHLQAYEWAK 

       190        200        210        220        230        240 
KISEHLLPKT RAYAEIWLDG EKIEGPDEEP ILGSNYLPRK FKTTVVIPPH NDVDVHANDL 

       250        260        270        280        290        300 
NFVAIGENGQ LIGFNVLVGG GLAMTHGDTS TYPRRADDFG FIPLEKTLEV AAAVVSTQRD 

       310        320        330        340        350        360 
WGNRSNRKNA KTKYTLDRVG VEVFKAEVEK RAGITFAPSR AYEFTSRGDR IGWVEGIDGK 

       370        380        390        400        410        420 
HHLTLFIENG RILDFPGKPL KTGVAEIAKV HQGDFRMTAN QNLIVAGVPA DQKQQIEQLA 

       430        440        450        460        470        480 
RSHGLIDDGV SEQRINSMAC VAFPTCPLAM AEAERFLPSF VTEVEGILAK HALPKEENII 

       490        500        510        520        530        540 
LRVTGCPNGC GRAMLAEIGL VGKAPGRYNL HLGGNRNGTR IPKMYKENIT DTQILQEIDE 

       550        560        570 
LVGRWASERL DGEGFGDFTI RAGIIEEVII SKRDFYA 

A5F3I5 in FASTA format

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