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Q1C2P9

- CYSG_YERPA

UniProt

Q1C2P9 - CYSG_YERPA

Protein

Siroheme synthase

Gene

cysG

Organism
Yersinia pestis bv. Antiqua (strain Antiqua)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (11 Jul 2006)
      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 sitei222 – 2221S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotation
    Active sitei245 – 2451Proton acceptorUniRule annotation
    Active sitei267 – 2671Proton donorUniRule annotation
    Binding sitei303 – 3031S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotation
    Binding sitei379 – 3791S-adenosyl-L-methionine; via amide nitrogenUniRule annotation
    Binding sitei408 – 4081S-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

    BioCyciYPES360102:GHZU-3381-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:YPA_3311
    OrganismiYersinia pestis bv. Antiqua (strain Antiqua)
    Taxonomic identifieri360102 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
    ProteomesiUP000001971: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 470470Siroheme synthasePRO_0000330573Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi360102.YPA_3311.

    Structurei

    3D structure databases

    ProteinModelPortaliQ1C2P9.
    SMRiQ1C2P9. Positions 1-453.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 201201precorrin-2 dehydrogenase / sirohydrochlorin ferrochelataseUniRule annotationAdd
    BLAST
    Regioni213 – 470258Uroporphyrinogen-III C-methyltransferaseUniRule annotationAdd
    BLAST
    Regioni298 – 3003S-adenosyl-L-methionine bindingUniRule annotation
    Regioni328 – 3292S-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.

    Q1C2P9-1 [UniParc]FASTAAdd to Basket

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    MDYFPIFCQL QHKACLLVGG GEIAERKARL LLDAGALVTV NACEFTPQFH    50
    HWADQGQLSL ISGEFVPELL ADKWLVIAAT DQLSVNALVY QSANQQRIFC 100
    NVVDDPKRTS FIMPSIIDRS PIMIAVSSGG KAPVLARLLR EKLEALLPQH 150
    LGQLAGNLRQ RVKQHFTVMT ERRRFWEKLL THDRLAQSLA NNDHVQADQH 200
    VEQLFSAPLT DRGEVVLVGA GPGDAGLLTL KGLQQIQQAD VVVYDRLVSD 250
    EVMNLVRRDA ERIFVGKQSG HHCVPQEQIN QILLQQAQSG KRVVRLKGGD 300
    PFIFGRGGEE LEELAGYGIP FSVVPGITAA SGCSAYSGIP LTHRDHAQSV 350
    RLVTGHAKKE GQLDWANLAA EKQTLVFYMG LSQAGEIQQQ LIQHGMPATT 400
    QVALVENGTS RHQRVVSGEL SQLALLSQQV SSPSLIIVGS VVSLREKLNW 450
    FSSRHHDDQP KVTECVAHVG 470
    Length:470
    Mass (Da):51,664
    Last modified:July 11, 2006 - v1
    Checksum:iD28E9E9C1182F316
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000308 Genomic DNA. Translation: ABG15273.1.
    RefSeqiYP_653218.1. NC_008150.1.

    Genome annotation databases

    EnsemblBacteriaiABG15273; ABG15273; YPA_3311.
    GeneIDi4118424.
    KEGGiypa:YPA_3311.
    PATRICi18586488. VBIYerPes1796_4039.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000308 Genomic DNA. Translation: ABG15273.1 .
    RefSeqi YP_653218.1. NC_008150.1.

    3D structure databases

    ProteinModelPortali Q1C2P9.
    SMRi Q1C2P9. Positions 1-453.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 360102.YPA_3311.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABG15273 ; ABG15273 ; YPA_3311 .
    GeneIDi 4118424.
    KEGGi ypa:YPA_3311.
    PATRICi 18586488. VBIYerPes1796_4039.

    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 .
    BioCyci YPES360102:GHZU-3381-MONOMER.

    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. "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516: evidence of gene reduction in an emerging pathogen."
      Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M., Worsham P., Chu M.C., Andersen G.L.
      J. Bacteriol. 188:4453-4463(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Antiqua.

    Entry informationi

    Entry nameiCYSG_YERPA
    AccessioniPrimary (citable) accession number: Q1C2P9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 29, 2008
    Last sequence update: July 11, 2006
    Last modified: October 1, 2014
    This is version 67 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