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A9H259

- CYSG_GLUDA

UniProt

A9H259 - CYSG_GLUDA

Protein

Siroheme synthase

Gene

cysG

Organism
Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 1 (05 Feb 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 sitei233 – 2331S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotation
    Active sitei256 – 2561Proton acceptorUniRule annotation
    Active sitei278 – 2781Proton donorUniRule annotation
    Binding sitei314 – 3141S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotation
    Binding sitei392 – 3921S-adenosyl-L-methionine; via amide nitrogenUniRule annotation
    Binding sitei421 – 4211S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygenUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi28 – 292NADUniRule annotation
    Nucleotide bindingi49 – 502NADUniRule 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

    BioCyciGDIA272568:GJPS-171-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:GDI0165, Gdia_2235
    OrganismiGluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5)
    Taxonomic identifieri272568 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconacetobacter
    ProteomesiUP000000736: Chromosome, UP000001176: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 470470Siroheme synthasePRO_0000330513Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi272568.GDI_0165.

    Structurei

    3D structure databases

    ProteinModelPortaliA9H259.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 213213precorrin-2 dehydrogenase / sirohydrochlorin ferrochelataseUniRule annotationAdd
    BLAST
    Regioni224 – 470247Uroporphyrinogen-III C-methyltransferaseUniRule annotationAdd
    BLAST
    Regioni309 – 3113S-adenosyl-L-methionine bindingUniRule annotation
    Regioni339 – 3402S-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.
    OMAiLHQQLAW.
    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.

    A9H259-1 [UniParc]FASTAAdd to Basket

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    MSDATDPGWF PLALRLRGAR VVVVGGGGIA LNKVRLLLAH AARIDILAPR    50
    LEDTLAAWQA EGRITHIAGE ATPDRVRALL PGSRLVYAAT DDRAVNRAVA 100
    AQADALNIPV CAVDDPEPSS FITPAQIHRG PVRIAISTGG AAPVLARRLR 150
    ERIEAVMPAG LDALARFLQA ERAHVVAACP DIGRRRRVWE DFLDGPGGEA 200
    AQRGEHAAAR QVLDHLLAGA QTGGEVWLVG AGPGDPDLLT LRALHLMQNA 250
    DSVLYDQLLP PALMDRVRRD AERVFVGKQR DRHTMPQDDI NAELIRRARA 300
    GERVLRLKGG DPFIFGRGGE EIEALMAAGI PFQVVPGITA ASGCAAYAGI 350
    PLTHRDCAQS CLFVTGHARR DGTLDLPWDS MARPGQTIAI YMGVTALPDL 400
    CTMLVRHGLP PDWPAAVVER GTRPDQRVLT GTLADLPALA RAHAVGSPAL 450
    VLVGQVVRHR VVTPPPLSGT 470
    Length:470
    Mass (Da):50,124
    Last modified:February 5, 2008 - v1
    Checksum:i70D8FF743EA97B96
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM889285 Genomic DNA. Translation: CAP54108.1.
    CP001189 Genomic DNA. Translation: ACI51990.1.
    RefSeqiYP_001600455.1. NC_010125.1.
    YP_002276605.1. NC_011365.1.

    Genome annotation databases

    EnsemblBacteriaiACI51990; ACI51990; Gdia_2235.
    CAP54108; CAP54108; GDI0165.
    GeneIDi5788693.
    6975664.
    KEGGigdi:GDI_0165.
    gdj:Gdia_2235.
    PATRICi22052918. VBIGluDia203729_2239.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM889285 Genomic DNA. Translation: CAP54108.1 .
    CP001189 Genomic DNA. Translation: ACI51990.1 .
    RefSeqi YP_001600455.1. NC_010125.1.
    YP_002276605.1. NC_011365.1.

    3D structure databases

    ProteinModelPortali A9H259.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 272568.GDI_0165.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACI51990 ; ACI51990 ; Gdia_2235 .
    CAP54108 ; CAP54108 ; GDI0165 .
    GeneIDi 5788693.
    6975664.
    KEGGi gdi:GDI_0165.
    gdj:Gdia_2235.
    PATRICi 22052918. VBIGluDia203729_2239.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00148 ; UER00211 .
    UPA00148 ; UER00222 .
    UPA00262 ; UER00211 .
    UPA00262 ; UER00222 .
    UPA00262 ; UER00376 .
    BioCyci GDIA272568:GJPS-171-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 the sugarcane nitrogen-fixing endophyte Gluconacetobacter diazotrophicus Pal5."
      Bertalan M., Albano R., de Padua V., Rouws L., Rojas C., Hemerly A., Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V., Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D.
      , Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F., Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L., Figueiredo D., Montano H., Junior J., de Souza Filho G., Martin Quintana Flores V., Ferreira B., Branco A., Gonzalez P., Guillobel H., Lemos M., Seibel L., Macedo J., Alves-Ferreira M., Sachetto-Martins G., Coelho A., Santos E., Amaral G., Neves A., Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C., Urmenyi T., Rael Pereira A., Silva R., Rondinelli E., von Kruger W., Martins O., Baldani J.I., Ferreira P.C.
      BMC Genomics 10:450-450(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 49037 / DSM 5601 / PAl5.
    2. "Two genome sequences of the same bacterial strain, Gluconacetobacter diazotrophicus PAl 5, suggest a new standard in genome sequence submission."
      Giongo A., Tyler H.L., Zipperer U.N., Triplett E.W.
      Stand. Genomic Sci. 2:309-317(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 49037 / DSM 5601 / PAl5.

    Entry informationi

    Entry nameiCYSG_GLUDA
    AccessioniPrimary (citable) accession number: A9H259
    Secondary accession number(s): B5ZEK0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 29, 2008
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 55 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, 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