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A4SRH0

- CYSG2_AERS4

UniProt

A4SRH0 - CYSG2_AERS4

Protein

Siroheme synthase 2

Gene

cysG2

Organism
Aeromonas salmonicida (strain A449)
Status
Reviewed - Annotation score: 5 out of 5- Protein inferred from homologyi
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    • History
      Entry version 58 (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 sitei223 – 2231S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotation
    Active sitei246 – 2461Proton acceptorUniRule annotation
    Active sitei268 – 2681Proton donorUniRule annotation
    Binding sitei381 – 3811S-adenosyl-L-methionine; via amide nitrogenUniRule annotation
    Binding sitei410 – 4101S-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-3511-MONOMER.
    UniPathwayiUPA00148; UER00211.
    UPA00148; UER00222.
    UPA00262; UER00211.
    UPA00262; UER00222.
    UPA00262; UER00376.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Siroheme synthase 2UniRule annotation
    Including the following 3 domains:
    Uroporphyrinogen-III C-methyltransferase 2UniRule annotation (EC:2.1.1.107UniRule annotation)
    Short name:
    Urogen III methylase 2UniRule annotation
    Alternative name(s):
    SUMT 2UniRule annotation
    Uroporphyrinogen III methylase 2UniRule annotation
    Short name:
    UROM 2UniRule annotation
    Precorrin-2 dehydrogenase 2UniRule annotation (EC:1.3.1.76UniRule annotation)
    Sirohydrochlorin ferrochelatase 2UniRule annotation (EC:4.99.1.4UniRule annotation)
    Gene namesi
    Name:cysG2UniRule annotation
    Ordered Locus Names:ASA_3524
    OrganismiAeromonas salmonicida (strain A449)
    Taxonomic identifieri382245 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas
    ProteomesiUP000000225: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 480480Siroheme synthase 2PRO_0000330490Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei126 – 1261PhosphoserineUniRule annotation

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Protein-protein interaction databases

    STRINGi382245.ASA_3524.

    Structurei

    3D structure databases

    ProteinModelPortaliA4SRH0.
    SMRiA4SRH0. Positions 1-455.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 202202precorrin-2 dehydrogenase / sirohydrochlorin ferrochelataseUniRule annotationAdd
    BLAST
    Regioni214 – 480267Uroporphyrinogen-III C-methyltransferaseUniRule annotationAdd
    BLAST
    Regioni299 – 3013S-adenosyl-L-methionine bindingUniRule annotation
    Regioni329 – 3302S-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.
    OrthoDBiEOG6BGNXZ.

    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.

    A4SRH0-1 [UniParc]FASTAAdd to Basket

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    MDYLPMFARL EGRPVLLVGG GEVALRKARL LLAAGARLTL VSPEIEPEFA    50
    EFAGRFTHLV ERFTPAHLAG QLLVVAATDN LEVNALVYQS ANQLGLFVNV 100
    VDDPKRSSFI FPSIIDRSPL MVAVSSGGKA PVLVRLLRER LESLLPRHLG 150
    GLTELSGRVR DKAKQVLSSI SDRRRFWERA FASNTLAGLI EKQDWQSAET 200
    WLNDGLDKAQ SEVGEVVLVG AGPGDPGLLT LKALQQIQQA EVVLYDQLVS 250
    PEILDLVRRD ATLVSVGKKA GAHSVPQEET NRLLVEYARA GNRVVRLKGG 300
    DPFMFGCGGE ELEVLAAEGI PFSVVPGITA AAGATAYAGI PLTHRDHAQS 350
    AVFITGHCQK EGKEPDWQQL AVTQQTLVIY MGLMRSEHIQ QQLVSHGRSC 400
    TTPIAIIEWG TTARQRVLTG TLAELAVLAQ QAVSPSLIVI GEVVSLRKQL 450
    AWFGEKSGEK RDVQAGTDMN GCDLKLVNLA 480
    Length:480
    Mass (Da):51,976
    Last modified:April 29, 2008 - v2
    Checksum:i73EA4371971ABAA8
    GO

    Sequence cautioni

    The sequence ABO91492.1 differs from that shown. Reason: Frameshift at position 22.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000644 Genomic DNA. Translation: ABO91492.1. Frameshift.
    RefSeqiYP_001143240.1. NC_009348.1.

    Genome annotation databases

    EnsemblBacteriaiABO91492; ABO91492; ASA_3524.
    GeneIDi4995755.
    KEGGiasa:ASA_3524.
    PATRICi20793502. VBIAerSal2987_3511.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000644 Genomic DNA. Translation: ABO91492.1 . Frameshift.
    RefSeqi YP_001143240.1. NC_009348.1.

    3D structure databases

    ProteinModelPortali A4SRH0.
    SMRi A4SRH0. Positions 1-455.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 382245.ASA_3524.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABO91492 ; ABO91492 ; ASA_3524 .
    GeneIDi 4995755.
    KEGGi asa:ASA_3524.
    PATRICi 20793502. VBIAerSal2987_3511.

    Phylogenomic databases

    eggNOGi COG0007.
    HOGENOMi HOG000290518.
    KOi K02302.
    OrthoDBi EOG6BGNXZ.

    Enzyme and pathway databases

    UniPathwayi UPA00148 ; UER00211 .
    UPA00148 ; UER00222 .
    UPA00262 ; UER00211 .
    UPA00262 ; UER00222 .
    UPA00262 ; UER00376 .
    BioCyci ASAL382245:GJJN-3511-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 nameiCYSG2_AERS4
    AccessioniPrimary (citable) accession number: A4SRH0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 29, 2008
    Last sequence update: April 29, 2008
    Last modified: October 1, 2014
    This is version 58 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

    Documents

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

    External Data

    Dasty 3