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A4VLU6

- CYSG_PSEU5

UniProt

A4VLU6 - CYSG_PSEU5

Protein

Siroheme synthase

Gene

cysG

Organism
Pseudomonas stutzeri (strain A1501)
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 2 (29 Apr 2008)
      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

    BioCyciPSTU379731:GJER-2283-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:PST_2288
    OrganismiPseudomonas stutzeri (strain A1501)
    Taxonomic identifieri379731 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000000233: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 465465Siroheme synthasePRO_0000330542Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi379731.PST_2288.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 203203precorrin-2 dehydrogenase / sirohydrochlorin ferrochelataseUniRule annotationAdd
    BLAST
    Regioni216 – 465250Uroporphyrinogen-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.
    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.
    PROSITEiPS00840. SUMT_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A4VLU6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEYLPLFHNL KGRTVLIVGG GEIALRKARL LSEAGARLRV VAPSIEAQLV    50
    ELVQAGAGEC LDRGYARQDL QGCVLAIAAT DDEPLNATVS QHANALGVPV 100
    NVVDSPQLCS VIFPAIVDRS PLVVAVSSGG DAPVLARLIR ARIETWIPAA 150
    YGQLAGLAKQ FRAQVKARFA NVQQRRVFWE EVFQGPIAEQ ALAGRTAEAE 200
    RLLAEKLAGV APKALGEVYL VGAGPGDPDL LTFRALRLMQ QADVVLYDRL 250
    VAPAIIDLCR RDADRIYVGK QRADHAVPQE QINQQLVTLA KQGKRVLRLK 300
    GGDPFIFGRG GEEIEELAAH GVPFQVVPGI TAASGCAAYA GIPLTHRDHA 350
    QSVRFVTGHL KDGSCDLPWS ELAAPAQTLV FYMGLVGLPV ICQQLIAHGR 400
    SAETPAALVQ QGTTSNQRVF TATLGTLAGR IAQEDVQAPT LLIVGEVVQL 450
    REKLAWFEGA QAAGR 465
    Length:465
    Mass (Da):49,692
    Last modified:April 29, 2008 - v2
    Checksum:i55ED316A54895278
    GO

    Sequence cautioni

    The sequence ABP79947.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000304 Genomic DNA. Translation: ABP79947.1. Different initiation.
    RefSeqiYP_001172789.1. NC_009434.1.

    Genome annotation databases

    EnsemblBacteriaiABP79947; ABP79947; PST_2288.
    GeneIDi5098368.
    KEGGipsa:PST_2288.
    PATRICi19965068. VBIPseStu31643_2297.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000304 Genomic DNA. Translation: ABP79947.1 . Different initiation.
    RefSeqi YP_001172789.1. NC_009434.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 379731.PST_2288.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABP79947 ; ABP79947 ; PST_2288 .
    GeneIDi 5098368.
    KEGGi psa:PST_2288.
    PATRICi 19965068. VBIPseStu31643_2297.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00148 ; UER00211 .
    UPA00148 ; UER00222 .
    UPA00262 ; UER00211 .
    UPA00262 ; UER00222 .
    UPA00262 ; UER00376 .
    BioCyci PSTU379731:GJER-2283-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 PS00840. SUMT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete genome sequence of the metabolically versatile and root-associated nitrogen-fixing bacterium Pseudomonas stutzeri A1501."
      Yan Y., Yang J., Dou Y., Ping S., Chen M., Yao Z., Li H., Lu W., Zhang W., Peng J., Liu W., He S., Geng L., Zhang X., Yang F., Li D., Lin Z., Wang Y.
      , Elmerich C., Lin M., Jin Q.
      Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: A1501.

    Entry informationi

    Entry nameiCYSG_PSEU5
    AccessioniPrimary (citable) accession number: A4VLU6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 29, 2008
    Last sequence update: April 29, 2008
    Last modified: October 1, 2014
    This is version 57 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

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

    External Data

    Dasty 3