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A1AGQ2

- CYSG_ECOK1

UniProt

A1AGQ2 - CYSG_ECOK1

Protein

Siroheme synthase

Gene

cysG

Organism
Escherichia coli O1:K1 / APEC
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 1 (23 Jan 2007)
      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.UniRule 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: UniProtKB-HAMAP
    3. sirohydrochlorin ferrochelatase activity Source: UniProtKB-EC
    4. uroporphyrin-III C-methyltransferase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. cobalamin biosynthetic process Source: UniProtKB-HAMAP
    2. siroheme biosynthetic process Source: UniProtKB-HAMAP

    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

    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:Ecok1_33480
    ORF Names:APECO1_3088
    OrganismiEscherichia coli O1:K1 / APEC
    Taxonomic identifieri405955 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000008216: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 457457Siroheme synthasePRO_0000330509Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi405955.APECO1_3088.

    Structurei

    3D structure databases

    ProteinModelPortaliA1AGQ2.
    SMRiA1AGQ2. Positions 1-457.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 204204precorrin-2 dehydrogenase / sirohydrochlorin ferrochelataseUniRule annotationAdd
    BLAST
    Regioni216 – 457242Uroporphyrinogen-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.

    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.

    A1AGQ2-1 [UniParc]FASTAAdd to Basket

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    MDHLPIFCQL RDRDCLIVGG GDVAERKARL LLDAGARLTV NALAFIPQFT    50
    AWADAGMLTL VEGPFDESLL DTCWLAIAAT DDDALNQRVS EAAESRRIFC 100
    NVVDAPKAAS FIMPSIIDRS PLMVAVSSGG TSPVLARLLR EKLESLLPLH 150
    LGQVAKYAGQ LRGRVKQQFA TMGERRRFWE KLFVNDRLAQ SLANNDQKAI 200
    TETTEQLINE PLDHRGEVVL VGAGPGDAGL LTLKGLQQIQ QADVVVYDRL 250
    VSDDIMNLIR RDADRVFVGK RAGYHCVPQE EINQILLREA QKGKRVVRLK 300
    GGDPFIFGRG GEELETLCNA GIPFSVVPGI TAASGCSAYS GIPLTHRDYA 350
    QSVRLITGHL KTGGELDWEN LAAEKQTLVF YMGLNQAATI QQKLIEYGMP 400
    GEMPVAIVEN GTAVTQRVID GTLTQLGELA QQMNSPSLII IGRVVGLRDK 450
    LNWFSNH 457
    Length:457
    Mass (Da):50,007
    Last modified:January 23, 2007 - v1
    Checksum:i2F28420F1C1C7AF7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000468 Genomic DNA. Translation: ABJ02842.1.
    RefSeqiYP_858966.1. NC_008563.1.

    Genome annotation databases

    EnsemblBacteriaiABJ02842; ABJ02842; APECO1_3088.
    GeneIDi4493156.
    KEGGiecv:APECO1_3088.
    PATRICi18219119. VBIEscCol127180_3787.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000468 Genomic DNA. Translation: ABJ02842.1 .
    RefSeqi YP_858966.1. NC_008563.1.

    3D structure databases

    ProteinModelPortali A1AGQ2.
    SMRi A1AGQ2. Positions 1-457.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 405955.APECO1_3088.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABJ02842 ; ABJ02842 ; APECO1_3088 .
    GeneIDi 4493156.
    KEGGi ecv:APECO1_3088.
    PATRICi 18219119. VBIEscCol127180_3787.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00148 ; UER00211 .
    UPA00148 ; UER00222 .
    UPA00262 ; UER00211 .
    UPA00262 ; UER00222 .
    UPA00262 ; UER00376 .

    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. "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7 shares strong similarities with human extraintestinal pathogenic E. coli genomes."
      Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.
      J. Bacteriol. 189:3228-3236(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiCYSG_ECOK1
    AccessioniPrimary (citable) accession number: A1AGQ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 29, 2008
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 64 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, Multifunctional enzyme

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3