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Q2KWB0

- CYSG_BORA1

UniProt

Q2KWB0 - CYSG_BORA1

Protein

Siroheme synthase

Gene

cysG

Organism
Bordetella avium (strain 197N)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 61 (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 sitei307 – 3071S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotation
    Binding sitei384 – 3841S-adenosyl-L-methionine; via amide nitrogenUniRule annotation
    Binding sitei413 – 4131S-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

    BioCyciBAVI360910:GCKI-869-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:BAV0848
    OrganismiBordetella avium (strain 197N)
    Taxonomic identifieri360910 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
    ProteomesiUP000001977: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 461461Siroheme synthasePRO_0000330496Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi360910.BAV0848.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2KWB0.
    SMRiQ2KWB0. Positions 1-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 203203precorrin-2 dehydrogenase / sirohydrochlorin ferrochelataseUniRule annotationAdd
    BLAST
    Regioni216 – 461246Uroporphyrinogen-III C-methyltransferaseUniRule annotationAdd
    BLAST
    Regioni302 – 3043S-adenosyl-L-methionine bindingUniRule annotation
    Regioni332 – 3332S-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.
    PROSITEiPS00839. SUMT_1. 1 hit.
    PS00840. SUMT_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q2KWB0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLFPIFSDI KGRCVLVVGG GAVATRKAQA LLEAGAAVSV GAPTLTPELA    50
    RLAQGQTITH LQGEFDADWL KDAWLIIAAT DDRTVNTRVY EAACARRQFC 100
    NVVDDPALSS FQVPSIVDRS PLIVAISSSG LAPVLARRLR ERLESLFDHS 150
    LGALAELAAR YRPAIRAARA DLKERRRFYD WLLDGPVAAA LRRAQPQQAQ 200
    EALDEALARP ALSQDGRVVL VGAGPGDPGL LTLKGLRALN EADVILHDRL 250
    VSAEVLALAR RDAERITVGK RLGENHNATQ ARIHELMVEH ARAGRRVVRL 300
    KGGDAFIFGR GGEELEHLRA HGVDYEVVPG ITAALACAAY AGIPLTHRDY 350
    AQSVHLVTAH CRADEEALDW DGLARGQQTL AFYMGVGQLD ILSARLVAHG 400
    RPGSTPFALI ENGSRPSQRV VMGRLSQLAE RAREQAVASP ALLIVGEVAA 450
    LADRLAWFGK P 461
    Length:461
    Mass (Da):49,690
    Last modified:April 29, 2008 - v2
    Checksum:i75798D4607AAB25E
    GO

    Sequence cautioni

    The sequence CAJ48459.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM167904 Genomic DNA. Translation: CAJ48459.1. Different initiation.
    RefSeqiYP_785377.1. NC_010645.1.

    Genome annotation databases

    GeneIDi6267920.
    KEGGibav:BAV0848.
    PATRICi21127876. VBIBorAvi43433_0864.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM167904 Genomic DNA. Translation: CAJ48459.1 . Different initiation.
    RefSeqi YP_785377.1. NC_010645.1.

    3D structure databases

    ProteinModelPortali Q2KWB0.
    SMRi Q2KWB0. Positions 1-460.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 360910.BAV0848.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 6267920.
    KEGGi bav:BAV0848.
    PATRICi 21127876. VBIBorAvi43433_0864.

    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 BAVI360910:GCKI-869-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. "Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
      Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
      J. Bacteriol. 188:6002-6015(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 197N.

    Entry informationi

    Entry nameiCYSG_BORA1
    AccessioniPrimary (citable) accession number: Q2KWB0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 29, 2008
    Last sequence update: April 29, 2008
    Last modified: October 1, 2014
    This is version 61 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