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P0AEA8

- CYSG_ECOLI

UniProt

P0AEA8 - CYSG_ECOLI

Protein

Siroheme synthase

Gene

cysG

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 85 (01 Oct 2014)
      Sequence version 1 (06 Dec 2005)
      Previous versions | rss
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    Functioni

    Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme.5 PublicationsUniRule annotation

    Catalytic activityi

    S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1.UniRule annotation
    S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2.UniRule annotation
    Precorrin-2 + NAD+ = sirohydrochlorin + NADH.UniRule annotation
    Siroheme + 2 H+ = sirohydrochlorin + Fe2+.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei225 – 2251S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotation
    Active sitei248 – 2481Proton acceptorUniRule annotation
    Active sitei270 – 2701Proton donorUniRule annotation
    Binding sitei306 – 3061S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotation
    Binding sitei382 – 3821S-adenosyl-L-methionine; via amide nitrogenUniRule annotation
    Binding sitei411 – 4111S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygenUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi22 – 232NADUniRule annotation
    Nucleotide bindingi43 – 442NADUniRule annotation

    GO - Molecular functioni

    1. NAD binding Source: InterPro
    2. precorrin-2 dehydrogenase activity Source: EcoCyc
    3. sirohydrochlorin ferrochelatase activity Source: EcoCyc
    4. uroporphyrin-III C-methyltransferase activity Source: EcoCyc

    GO - Biological processi

    1. cobalamin biosynthetic process Source: UniProtKB-HAMAP
    2. response to osmotic stress Source: EcoCyc
    3. siroheme biosynthetic process Source: EcoCyc

    Keywords - Molecular functioni

    Lyase, Methyltransferase, Oxidoreductase, Transferase

    Keywords - Biological processi

    Cobalamin biosynthesis, Porphyrin biosynthesis

    Keywords - Ligandi

    NAD, S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciEcoCyc:SIROHEMESYN-MONOMER.
    ECOL316407:JW3331-MONOMER.
    MetaCyc:SIROHEMESYN-MONOMER.
    UniPathwayiUPA00148; UER00211.
    UPA00148; UER00222.
    UPA00262; UER00211.
    UPA00262; UER00222.
    UPA00262; UER00376.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Siroheme synthaseUniRule annotation
    Including the following 3 domains:
    Uroporphyrinogen-III C-methyltransferaseUniRule annotation (EC:2.1.1.107UniRule annotation)
    Short name:
    Urogen III methylaseUniRule annotation
    Alternative name(s):
    SUMTUniRule annotation
    Uroporphyrinogen III methylaseUniRule annotation
    Short name:
    UROMUniRule annotation
    Precorrin-2 dehydrogenaseUniRule annotation (EC:1.3.1.76UniRule annotation)
    Sirohydrochlorin ferrochelataseUniRule annotation (EC:4.99.1.4UniRule annotation)
    Gene namesi
    Name:cysGUniRule annotation
    Ordered Locus Names:b3368, JW3331
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10188. cysG.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi21 – 211G → D: It has methyltransferase and ferrochelatase activities but a greatly reduced dehydrogenase activity. It is able to bind AdoMet. 1 Publication
    Mutagenesisi224 – 2241G → A: It abolishes methyltransferase activity, but has dehydrogenase and ferrochelatase activities. It is unable to bind AdoMet. 1 Publication
    Mutagenesisi227 – 2271D → A: It has all activities of CysG. 1 Publication
    Mutagenesisi248 – 2481D → A: It abolishes methyltransferase activity, but has dehydrogenase and ferrochelatase activities. It is able to bind AdoMet.
    Mutagenesisi270 – 2701K → I: It has all activities of CysG. It is able to bind AdoMet. 1 Publication
    Mutagenesisi298 – 2981R → L: It abolishes methyltransferase activity, but has dehydrogenase and ferrochelatase activities. It is unable to bind AdoMet. 1 Publication
    Mutagenesisi303 – 3031D → A: It has all activities of CysG. It is able to bind AdoMet. 1 Publication
    Mutagenesisi309 – 3091R → L: It abolishes methyltransferase activity, but has dehydrogenase and ferrochelatase activities. It is able to bind AdoMet. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 457457Siroheme synthasePRO_0000150378Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei128 – 1281PhosphoserineUniRule annotation

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP0AEA8.
    PRIDEiP0AEA8.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AEA8.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    nadEP188431EBI-1132623,EBI-548960

    Protein-protein interaction databases

    IntActiP0AEA8. 1 interaction.
    STRINGi511145.b3368.

    Structurei

    3D structure databases

    ProteinModelPortaliP0AEA8.
    SMRiP0AEA8. Positions 1-457.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni4 – 204201Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelataseBy similarityAdd
    BLAST
    Regioni216 – 448233Uroporphyrinogen-III C-methyltransferaseUniRule annotationAdd
    BLAST
    Regioni301 – 3033S-adenosyl-L-methionine bindingUniRule annotation
    Regioni331 – 3322S-adenosyl-L-methionine bindingUniRule annotation

    Sequence similaritiesi

    In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family.UniRule annotation
    In the C-terminal section; belongs to the precorrin methyltransferase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0007.
    HOGENOMiHOG000290518.
    KOiK02302.
    OMAiQASFIMP.
    OrthoDBiEOG6DRPFR.
    PhylomeDBiP0AEA8.

    Family and domain databases

    Gene3Di1.10.8.210. 1 hit.
    3.30.950.10. 1 hit.
    3.40.1010.10. 1 hit.
    3.40.50.720. 1 hit.
    HAMAPiMF_01646. Siroheme_synth.
    InterProiIPR000878. 4pyrrol_Mease.
    IPR014777. 4pyrrole_Mease_sub1.
    IPR014776. 4pyrrole_Mease_sub2.
    IPR006366. CobA/CysG_C.
    IPR016040. NAD(P)-bd_dom.
    IPR012409. Sirohaem_synth.
    IPR019478. Sirohaem_synthase_dimer_dom.
    IPR006367. Sirohaem_synthase_N.
    IPR003043. Uropor_MeTrfase_CS.
    [Graphical view]
    PfamiPF10414. CysG_dimeriser. 1 hit.
    PF13241. NAD_binding_7. 1 hit.
    PF00590. TP_methylase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036426. Sirohaem_synth. 1 hit.
    SUPFAMiSSF53790. SSF53790. 1 hit.
    TIGRFAMsiTIGR01469. cobA_cysG_Cterm. 1 hit.
    TIGR01470. cysG_Nterm. 1 hit.
    PROSITEiPS00839. SUMT_1. 1 hit.
    PS00840. SUMT_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P0AEA8-1 [UniParc]FASTAAdd to Basket

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    MDHLPIFCQL RDRDCLIVGG GDVAERKARL LLDAGARLTV NALAFIPQFT    50
    AWADAGMLTL VEGPFDESLL DTCWLAIAAT DDDALNQRVS EAAEARRIFC 100
    NVVDAPKAAS FIMPSIIDRS PLMVAVSSGG TSPVLARLLR EKLESLLPLH 150
    LGQVAKYAGQ LRGRVKQQFA TMGERRRFWE KLFVNDRLAQ SLANNDQKAI 200
    TETTEQLINE PLDHRGEVVL VGAGPGDAGL LTLKGLQQIQ QADVVVYDRL 250
    VSDDIMNLVR RDADRVFVGK RAGYHCVPQE EINQILLREA QKGKRVVRLK 300
    GGDPFIFGRG GEELETLCNA GIPFSVVPGI TAASGCSAYS GIPLTHRDYA 350
    QSVRLITGHL KTGGELDWEN LAAEKQTLVF YMGLNQAATI QQKLIEHGMP 400
    GEMPVAIVEN GTAVTQRVID GTLTQLGELA QQMNSPSLII IGRVVGLRDK 450
    LNWFSNH 457
    Length:457
    Mass (Da):49,951
    Last modified:December 6, 2005 - v1
    Checksum:iDDDE0DC90C5CF2F4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261R → P in CAA32419. (PubMed:2543955)Curated
    Sequence conflicti26 – 261R → P in AAA58165. (PubMed:2200672)Curated
    Sequence conflicti90 – 912SE → RQ in CAA32419. (PubMed:2543955)Curated
    Sequence conflicti90 – 912SE → RQ in AAA58165. (PubMed:2200672)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14202 Genomic DNA. Translation: CAA32419.1.
    U18997 Genomic DNA. Translation: AAA58165.1.
    U00096 Genomic DNA. Translation: AAC76393.1.
    AP009048 Genomic DNA. Translation: BAE77922.1.
    PIRiC65131.
    RefSeqiNP_417827.1. NC_000913.3.
    YP_492063.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC76393; AAC76393; b3368.
    BAE77922; BAE77922; BAE77922.
    GeneIDi12933484.
    947880.
    KEGGiecj:Y75_p3807.
    eco:b3368.
    PATRICi32122170. VBIEscCol129921_3462.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14202 Genomic DNA. Translation: CAA32419.1 .
    U18997 Genomic DNA. Translation: AAA58165.1 .
    U00096 Genomic DNA. Translation: AAC76393.1 .
    AP009048 Genomic DNA. Translation: BAE77922.1 .
    PIRi C65131.
    RefSeqi NP_417827.1. NC_000913.3.
    YP_492063.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P0AEA8.
    SMRi P0AEA8. Positions 1-457.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P0AEA8. 1 interaction.
    STRINGi 511145.b3368.

    Proteomic databases

    PaxDbi P0AEA8.
    PRIDEi P0AEA8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76393 ; AAC76393 ; b3368 .
    BAE77922 ; BAE77922 ; BAE77922 .
    GeneIDi 12933484.
    947880.
    KEGGi ecj:Y75_p3807.
    eco:b3368.
    PATRICi 32122170. VBIEscCol129921_3462.

    Organism-specific databases

    EchoBASEi EB0185.
    EcoGenei EG10188. cysG.

    Phylogenomic databases

    eggNOGi COG0007.
    HOGENOMi HOG000290518.
    KOi K02302.
    OMAi QASFIMP.
    OrthoDBi EOG6DRPFR.
    PhylomeDBi P0AEA8.

    Enzyme and pathway databases

    UniPathwayi UPA00148 ; UER00211 .
    UPA00148 ; UER00222 .
    UPA00262 ; UER00211 .
    UPA00262 ; UER00222 .
    UPA00262 ; UER00376 .
    BioCyci EcoCyc:SIROHEMESYN-MONOMER.
    ECOL316407:JW3331-MONOMER.
    MetaCyc:SIROHEMESYN-MONOMER.

    Miscellaneous databases

    PROi P0AEA8.

    Gene expression databases

    Genevestigatori P0AEA8.

    Family and domain databases

    Gene3Di 1.10.8.210. 1 hit.
    3.30.950.10. 1 hit.
    3.40.1010.10. 1 hit.
    3.40.50.720. 1 hit.
    HAMAPi MF_01646. Siroheme_synth.
    InterProi IPR000878. 4pyrrol_Mease.
    IPR014777. 4pyrrole_Mease_sub1.
    IPR014776. 4pyrrole_Mease_sub2.
    IPR006366. CobA/CysG_C.
    IPR016040. NAD(P)-bd_dom.
    IPR012409. Sirohaem_synth.
    IPR019478. Sirohaem_synthase_dimer_dom.
    IPR006367. Sirohaem_synthase_N.
    IPR003043. Uropor_MeTrfase_CS.
    [Graphical view ]
    Pfami PF10414. CysG_dimeriser. 1 hit.
    PF13241. NAD_binding_7. 1 hit.
    PF00590. TP_methylase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036426. Sirohaem_synth. 1 hit.
    SUPFAMi SSF53790. SSF53790. 1 hit.
    TIGRFAMsi TIGR01469. cobA_cysG_Cterm. 1 hit.
    TIGR01470. cysG_Nterm. 1 hit.
    PROSITEi PS00839. SUMT_1. 1 hit.
    PS00840. SUMT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of binding sequences for the Escherichia coli transcription activators, FNR and CRP: location of bases involved in discrimination between FNR and CRP."
      Bell A.I., Gaston K.L., Cole J.A., Busby S.J.W.
      Nucleic Acids Res. 17:3865-3874(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Nucleotide sequence, organisation and structural analysis of the products of genes in the nirB-cysG region of the Escherichia coli K-12 chromosome."
      Peakman T., Crouzet J., Mayaux J.F., Busby S.J.W., Mohan S., Harborne N., Wootton J., Nicolson R., Cole J.A.
      Eur. J. Biochem. 191:315-323(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "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.
    5. "Enzymatic synthesis of dihydrosirohydrochlorin (precorrin-2) and of a novel pyrrocorphin by uroporphyrinogen III methylase."
      Warren M.J., Stolowich N.J., Santander P.J., Roessner C.A., Sowa B.A., Scott A.I.
      FEBS Lett. 261:76-80(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-18, FUNCTION, CATALYTIC ACTIVITY.
    6. "The Escherichia coli cysG gene encodes S-adenosylmethionine-dependent uroporphyrinogen III methylase."
      Warren M.J., Roessner C.A., Santander P.J., Scott A.I.
      Biochem. J. 265:725-729(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A METHYLTRANSFERASE, CATALYTIC ACTIVITY, SUBUNIT.
    7. "The Escherichia coli cysG gene encodes the multifunctional protein, siroheme synthase."
      Spencer J.B., Stolowich N.J., Roessner C.A., Scott A.I.
      FEBS Lett. 335:57-60(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AND CATALYTIC ACTIVITY.
    8. "Evidence for a covalent intermediate in the S-adenosyl-L-methionine-dependent transmethylation reaction catalysed by sirohaem synthase."
      Woodcock S.C., Warren M.J.
      Biochem. J. 313:415-421(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Effect of mutations in the transmethylase and dehydrogenase/chelatase domains of sirohaem synthase (CysG) on sirohaem and cobalamin biosynthesis."
      Woodcock S.C., Raux E., Levillayer F., Thermes C., Rambach A., Warren M.J.
      Biochem. J. 330:121-129(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-21; GLY-224; ASP-227; LYS-270; ARG-298; ASP-303 AND ARG-309.

    Entry informationi

    Entry nameiCYSG_ECOLI
    AccessioniPrimary (citable) accession number: P0AEA8
    Secondary accession number(s): P11098, P76685, Q2M734
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2005
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 85 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Multifunctional enzyme, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3