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P17846

- CYSI_ECOLI

UniProt

P17846 - CYSI_ECOLI

Protein

Sulfite reductase [NADPH] hemoprotein beta-component

Gene

cysI

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.

    Catalytic activityi

    H2S + 3 NADP+ + 3 H2O = sulfite + 3 NADPH.

    Cofactori

    Binds 1 siroheme per subunit.
    Binds 1 4Fe-4S cluster per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi434 – 4341Iron-sulfur (4Fe-4S)
    Metal bindingi440 – 4401Iron-sulfur (4Fe-4S)
    Metal bindingi479 – 4791Iron-sulfur (4Fe-4S)
    Metal bindingi483 – 4831Iron (siroheme axial ligand)
    Metal bindingi483 – 4831Iron-sulfur (4Fe-4S)

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: EcoCyc
    2. heme binding Source: EcoCyc
    3. metal ion binding Source: UniProtKB-KW
    4. NADP binding Source: InterPro
    5. sulfite reductase (NADPH) activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. cysteine biosynthetic process Source: UniProtKB-KW
    2. hydrogen sulfide biosynthetic process Source: UniProtKB-HAMAP
    3. sulfate assimilation Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Cysteine biosynthesis

    Keywords - Ligandi

    4Fe-4S, Heme, Iron, Iron-sulfur, Metal-binding, NADP

    Enzyme and pathway databases

    BioCyciEcoCyc:BETACOMP-MONOMER.
    ECOL316407:JW2733-MONOMER.
    MetaCyc:BETACOMP-MONOMER.
    UniPathwayiUPA00140; UER00207.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sulfite reductase [NADPH] hemoprotein beta-component (EC:1.8.1.2)
    Short name:
    SiR-HP
    Short name:
    SiRHP
    Gene namesi
    Name:cysI
    Ordered Locus Names:b2763, JW2733
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10190. cysI.

    Subcellular locationi

    GO - Cellular componenti

    1. sulfite reductase complex (NADPH) Source: EcoCyc

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 570569Sulfite reductase [NADPH] hemoprotein beta-componentPRO_0000199896Add
    BLAST

    Proteomic databases

    PaxDbiP17846.

    Expressioni

    Gene expression databases

    GenevestigatoriP17846.

    Interactioni

    Subunit structurei

    Alpha(8)-beta8. The alpha component is a flavoprotein, the beta component is a hemoprotein.

    Protein-protein interaction databases

    DIPiDIP-9380N.
    IntActiP17846. 10 interactions.
    STRINGi511145.b2763.

    Structurei

    Secondary structure

    1
    570
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi82 – 854
    Helixi87 – 893
    Beta strandi90 – 923
    Helixi93 – 10614
    Beta strandi107 – 1093
    Beta strandi112 – 1143
    Beta strandi120 – 1223
    Turni127 – 1293
    Helixi133 – 1386
    Turni139 – 1413
    Beta strandi143 – 1453
    Turni147 – 1493
    Helixi164 – 1663
    Helixi167 – 18014
    Turni205 – 2073
    Beta strandi218 – 2214
    Helixi230 – 2323
    Beta strandi233 – 25321
    Beta strandi272 – 2787
    Helixi279 – 2813
    Helixi282 – 29615
    Helixi302 – 3043
    Helixi307 – 3148
    Helixi316 – 32712
    Beta strandi347 – 3504
    Beta strandi352 – 3543
    Beta strandi355 – 3606
    Helixi363 – 3653
    Helixi375 – 38511
    Beta strandi387 – 3926
    Beta strandi398 – 4047
    Helixi405 – 4073
    Helixi408 – 41710
    Turni418 – 4214
    Helixi426 – 4294
    Beta strandi431 – 4333
    Turni437 – 4393
    Turni448 – 4503
    Helixi451 – 46414
    Beta strandi474 – 4796
    Helixi486 – 4883
    Beta strandi489 – 4979
    Beta strandi500 – 5056
    Beta strandi509 – 5113
    Beta strandi516 – 5238
    Helixi524 – 54118
    Helixi548 – 5547
    Helixi564 – 5674

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AOPX-ray1.60A74-570[»]
    2AOPX-ray1.75A74-570[»]
    2GEPX-ray1.90A74-570[»]
    3AOPX-ray2.10A74-570[»]
    3GEOX-ray2.10A74-570[»]
    4AOPX-ray1.80A74-570[»]
    4G38X-ray1.56A1-570[»]
    4G39X-ray2.40A1-570[»]
    4GEPX-ray2.00A74-570[»]
    4HTRX-ray1.60A64-570[»]
    5AOPX-ray2.20A74-570[»]
    5GEPX-ray2.10A74-570[»]
    6GEPX-ray1.80A74-570[»]
    7GEPX-ray2.40A74-570[»]
    8GEPX-ray2.20A74-570[»]
    ProteinModelPortaliP17846.
    SMRiP17846. Positions 81-570.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP17846.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0155.
    HOGENOMiHOG000218418.
    KOiK00381.
    OMAiELHQEAY.
    OrthoDBiEOG6W9XFB.
    PhylomeDBiP17846.

    Family and domain databases

    Gene3Di3.90.480.10. 2 hits.
    HAMAPiMF_01540. CysI.
    InterProiIPR011786. CysI.
    IPR005117. NiRdtase/SiRdtase_haem-b_fer.
    IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
    IPR006066. NO2/SO3_Rdtase_FeS/sirohaem_BS.
    [Graphical view]
    PfamiPF01077. NIR_SIR. 1 hit.
    PF03460. NIR_SIR_ferr. 2 hits.
    [Graphical view]
    PRINTSiPR00397. SIROHAEM.
    SUPFAMiSSF55124. SSF55124. 2 hits.
    TIGRFAMsiTIGR02041. CysI. 1 hit.
    PROSITEiPS00365. NIR_SIR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P17846-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEKHPGPLV VEGKLTDAER MKHESNYLRG TIAEDLNDGL TGGFKGDNFL    50
    LIRFHGMYQQ DDRDIRAERA EQKLEPRHAM LLRCRLPGGV ITTKQWQAID 100
    KFAGENTIYG SIRLTNRQTF QFHGILKKNV KPVHQMLHSV GLDALATAND 150
    MNRNVLCTSN PYESQLHAEA YEWAKKISEH LLPRTRAYAE IWLDQEKVAT 200
    TDEEPILGQT YLPRKFKTTV VIPPQNDIDL HANDMNFVAI AENGKLVGFN 250
    LLVGGGLSIE HGNKKTYART ASEFGYLPLE HTLAVAEAVV TTQRDWGNRT 300
    DRKNAKTKYT LERVGVETFK AEVERRAGIK FEPIRPYEFT GRGDRIGWVK 350
    GIDDNWHLTL FIENGRILDY PARPLKTGLL EIAKIHKGDF RITANQNLII 400
    AGVPESEKAK IEKIAKESGL MNAVTPQREN SMACVSFPTC PLAMAEAERF 450
    LPSFIDNIDN LMAKHGVSDE HIVMRVTGCP NGCGRAMLAE VGLVGKAPGR 500
    YNLHLGGNRI GTRIPRMYKE NITEPEILAS LDELIGRWAK EREAGEGFGD 550
    FTVRAGIIRP VLDPARDLWD 570
    Length:570
    Mass (Da):63,998
    Last modified:January 23, 2007 - v4
    Checksum:i03B41FEE6AB349C6
    GO

    Sequence cautioni

    The sequence AAA23651.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA68816.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231H → L in AAA23651. (PubMed:2670946)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M23008 Genomic DNA. Translation: AAA23651.1. Different initiation.
    U29579 Genomic DNA. Translation: AAA69273.1.
    U00096 Genomic DNA. Translation: AAC75805.1.
    AP009048 Genomic DNA. Translation: BAE76840.1.
    Y07525 Genomic DNA. Translation: CAA68816.1. Different initiation.
    PIRiG65057. RDECSH.
    RefSeqiNP_417243.1. NC_000913.3.
    YP_490972.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75805; AAC75805; b2763.
    BAE76840; BAE76840; BAE76840.
    GeneIDi12933282.
    947231.
    KEGGiecj:Y75_p2701.
    eco:b2763.
    PATRICi32120938. VBIEscCol129921_2861.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M23008 Genomic DNA. Translation: AAA23651.1 . Different initiation.
    U29579 Genomic DNA. Translation: AAA69273.1 .
    U00096 Genomic DNA. Translation: AAC75805.1 .
    AP009048 Genomic DNA. Translation: BAE76840.1 .
    Y07525 Genomic DNA. Translation: CAA68816.1 . Different initiation.
    PIRi G65057. RDECSH.
    RefSeqi NP_417243.1. NC_000913.3.
    YP_490972.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AOP X-ray 1.60 A 74-570 [» ]
    2AOP X-ray 1.75 A 74-570 [» ]
    2GEP X-ray 1.90 A 74-570 [» ]
    3AOP X-ray 2.10 A 74-570 [» ]
    3GEO X-ray 2.10 A 74-570 [» ]
    4AOP X-ray 1.80 A 74-570 [» ]
    4G38 X-ray 1.56 A 1-570 [» ]
    4G39 X-ray 2.40 A 1-570 [» ]
    4GEP X-ray 2.00 A 74-570 [» ]
    4HTR X-ray 1.60 A 64-570 [» ]
    5AOP X-ray 2.20 A 74-570 [» ]
    5GEP X-ray 2.10 A 74-570 [» ]
    6GEP X-ray 1.80 A 74-570 [» ]
    7GEP X-ray 2.40 A 74-570 [» ]
    8GEP X-ray 2.20 A 74-570 [» ]
    ProteinModelPortali P17846.
    SMRi P17846. Positions 81-570.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9380N.
    IntActi P17846. 10 interactions.
    STRINGi 511145.b2763.

    Proteomic databases

    PaxDbi P17846.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75805 ; AAC75805 ; b2763 .
    BAE76840 ; BAE76840 ; BAE76840 .
    GeneIDi 12933282.
    947231.
    KEGGi ecj:Y75_p2701.
    eco:b2763.
    PATRICi 32120938. VBIEscCol129921_2861.

    Organism-specific databases

    EchoBASEi EB0187.
    EcoGenei EG10190. cysI.

    Phylogenomic databases

    eggNOGi COG0155.
    HOGENOMi HOG000218418.
    KOi K00381.
    OMAi ELHQEAY.
    OrthoDBi EOG6W9XFB.
    PhylomeDBi P17846.

    Enzyme and pathway databases

    UniPathwayi UPA00140 ; UER00207 .
    BioCyci EcoCyc:BETACOMP-MONOMER.
    ECOL316407:JW2733-MONOMER.
    MetaCyc:BETACOMP-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P17846.
    PROi P17846.

    Gene expression databases

    Genevestigatori P17846.

    Family and domain databases

    Gene3Di 3.90.480.10. 2 hits.
    HAMAPi MF_01540. CysI.
    InterProi IPR011786. CysI.
    IPR005117. NiRdtase/SiRdtase_haem-b_fer.
    IPR006067. NO2/SO3_Rdtase_4Fe4S_dom.
    IPR006066. NO2/SO3_Rdtase_FeS/sirohaem_BS.
    [Graphical view ]
    Pfami PF01077. NIR_SIR. 1 hit.
    PF03460. NIR_SIR_ferr. 2 hits.
    [Graphical view ]
    PRINTSi PR00397. SIROHAEM.
    SUPFAMi SSF55124. SSF55124. 2 hits.
    TIGRFAMsi TIGR02041. CysI. 1 hit.
    PROSITEi PS00365. NIR_SIR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the cysJIH regions of Salmonella typhimurium and Escherichia coli B. DNA sequences of cysI and cysH and a model for the siroheme-Fe4S4 active center of sulfite reductase hemoprotein based on amino acid homology with spinach nitrite reductase."
      Ostrowski J., Wu J.-Y., Rueger D.C., Miller B.E., Siegel L.M., Kredich N.M.
      J. Biol. Chem. 264:15726-15737(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: B.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    4. "Characterisation of the gene cysH and of its product phospho-adenylylsulphate reductase from Escherichia coli."
      Krone F.A., Westphal G., Schwenn J.D.
      Mol. Gen. Genet. 225:314-319(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 344-570.
      Strain: K12.
    5. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13.
      Strain: K12 / EMG2.
    6. "Sulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions."
      Crane B.R., Siegel L.M., Getzoff E.D.
      Science 270:59-67(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
    7. "Structures of the siroheme- and Fe4S4-containing active center of sulfite reductase in different states of oxidation: heme activation via reduction-gated exogenous ligand exchange."
      Crane B.R., Siegel L.M., Getzoff E.D.
      Biochemistry 36:12101-12119(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).

    Entry informationi

    Entry nameiCYSI_ECOLI
    AccessioniPrimary (citable) accession number: P17846
    Secondary accession number(s): Q2MA66
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 141 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3