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A4SHL4

- CYSG1_AERS4

UniProt

A4SHL4 - CYSG1_AERS4

Protein

Siroheme synthase 1

Gene

cysG1

Organism
Aeromonas salmonicida (strain A449)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (15 May 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 sitei383 – 3831S-adenosyl-L-methionine; via amide nitrogenUniRule annotation
    Binding sitei412 – 4121S-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

    BioCyciASAL382245:GJJN-190-MONOMER.
    UniPathwayiUPA00148; UER00211.
    UPA00148; UER00222.
    UPA00262; UER00211.
    UPA00262; UER00222.
    UPA00262; UER00376.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Siroheme synthase 1UniRule annotation
    Including the following 3 domains:
    Uroporphyrinogen-III C-methyltransferase 1UniRule annotation (EC:2.1.1.107UniRule annotation)
    Short name:
    Urogen III methylase 1UniRule annotation
    Alternative name(s):
    SUMT 1UniRule annotation
    Uroporphyrinogen III methylase 1UniRule annotation
    Short name:
    UROM 1UniRule annotation
    Precorrin-2 dehydrogenase 1UniRule annotation (EC:1.3.1.76UniRule annotation)
    Sirohydrochlorin ferrochelatase 1UniRule annotation (EC:4.99.1.4UniRule annotation)
    Gene namesi
    Name:cysG1UniRule annotation
    Ordered Locus Names:ASA_0192
    OrganismiAeromonas salmonicida (strain A449)
    Taxonomic identifieri382245 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas
    ProteomesiUP000000225: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 468468Siroheme synthase 1PRO_0000330489Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi382245.ASA_0192.

    Structurei

    3D structure databases

    ProteinModelPortaliA4SHL4.
    SMRiA4SHL4. Positions 1-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 204204precorrin-2 dehydrogenase / sirohydrochlorin ferrochelataseUniRule annotationAdd
    BLAST
    Regioni216 – 468253Uroporphyrinogen-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.
    OMAiRAMATRD.
    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.

    A4SHL4-1 [UniParc]FASTAAdd to Basket

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    MDYLPIFCRL DNKPVLLVGG GEVAERKARL LLDAGARLTV VSPALDPELA    50
    ALATSGTIDW LAAEFEPAHL TGKWLVVAAT DRREVNALVY QSANQAGIFA 100
    NVVDDPKRSS FIMPSIIDRS PLMVAISSGG KAPVLARLLR EKLEALLPQH 150
    LGAVAAFAGG LRARVKARFA SMGERRQFWE RLLSADRLGQ ALARGDKASA 200
    NQLADTLFAE ETGAKGEVIL VGAGPGDPGL LTLHALRHMQ QADLVVYDQL 250
    VSDEVMALVR RDARRIFVGK QAGNHCVPQE GINQLLLEEA SKGQRVVRLK 300
    GGDPFIFGRG GEELETLVGS GVGFQVVPGI TAASGCAAYA GIPLTHRDHA 350
    QSVRFVTAHG KGGTQDLDWP LLARDQQTLV FYMGLSSCAT IRQKLTAHGK 400
    AGTTPVALIE RGTQLNQRVI RGTLDQLPEL AVGVESPALI MVGSVVTLAD 450
    KLAWFGQTNH GVQAAALA 468
    Length:468
    Mass (Da):49,834
    Last modified:May 15, 2007 - v1
    Checksum:i41162FD6A3A0A080
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000644 Genomic DNA. Translation: ABO88386.1.
    RefSeqiYP_001140134.1. NC_009348.1.

    Genome annotation databases

    EnsemblBacteriaiABO88386; ABO88386; ASA_0192.
    GeneIDi4998078.
    KEGGiasa:ASA_0192.
    PATRICi20786673. VBIAerSal2987_0200.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000644 Genomic DNA. Translation: ABO88386.1 .
    RefSeqi YP_001140134.1. NC_009348.1.

    3D structure databases

    ProteinModelPortali A4SHL4.
    SMRi A4SHL4. Positions 1-460.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 382245.ASA_0192.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABO88386 ; ABO88386 ; ASA_0192 .
    GeneIDi 4998078.
    KEGGi asa:ASA_0192.
    PATRICi 20786673. VBIAerSal2987_0200.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00148 ; UER00211 .
    UPA00148 ; UER00222 .
    UPA00262 ; UER00211 .
    UPA00262 ; UER00222 .
    UPA00262 ; UER00376 .
    BioCyci ASAL382245:GJJN-190-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. "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into the evolution of a fish pathogen."
      Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C., Brown L.L.
      BMC Genomics 9:427-427(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: A449.

    Entry informationi

    Entry nameiCYSG1_AERS4
    AccessioniPrimary (citable) accession number: A4SHL4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 29, 2008
    Last sequence update: May 15, 2007
    Last modified: October 1, 2014
    This is version 57 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