Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P25924

- CYSG_SALTY

UniProt

P25924 - CYSG_SALTY

Protein

Siroheme synthase

Gene

cysG

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.1 PublicationUniRule annotation

    Catalytic activityi

    S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1.1 PublicationUniRule annotation
    S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2.1 PublicationUniRule annotation
    Precorrin-2 + NAD+ = sirohydrochlorin + NADH.1 PublicationUniRule annotation
    Siroheme + 2 H+ = sirohydrochlorin + Fe2+.1 PublicationUniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei225 – 2251S-adenosyl-L-methionine; via carbonyl oxygen
    Active sitei248 – 2481Proton acceptorUniRule annotation
    Active sitei270 – 2701Proton donorUniRule annotation
    Binding sitei306 – 3061S-adenosyl-L-methionine; via carbonyl oxygen
    Binding sitei382 – 3821S-adenosyl-L-methionine; via amide nitrogen
    Binding sitei411 – 4111S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen
    Binding sitei437 – 4371S-adenosyl-L-methionine; via carbonyl oxygen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi22 – 232NAD1 PublicationUniRule annotation
    Nucleotide bindingi43 – 442NAD1 PublicationUniRule 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

    BioCyciMetaCyc:STM3477-MONOMER.
    SENT99287:GCTI-3499-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:STM3477
    OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
    Taxonomic identifieri99287 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
    ProteomesiUP000001014: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi128 – 1281S → A: Abolishes the methyltransferase activity and increases 3 and 4-fold the dehydrogenase and ferrochelatase activities, respectively. 1 Publication
    Mutagenesisi128 – 1281S → D: Abolishes the methyltransferase activity and reduces 10 and 5-fold the dehydrogenase and ferrochelatase activities, respectively. 1 Publication
    Mutagenesisi250 – 2501L → A: Abolishes the dehydrogenase and ferrochelatase activities and reduces 6-fold the methyltransferase activity. 1 Publication
    Mutagenesisi270 – 2701K → I: Abolishes the methyltransferase, dehydrogenase and ferrochelatase activities. 1 Publication
    Mutagenesisi385 – 3851N → A: Abolishes the dehydrogenase and ferrochelatase activities and reduces 10-fold the methyltransferase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 457457Siroheme synthasePRO_0000150380Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei128 – 1281Phosphoserine1 PublicationUniRule annotation

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP25924.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi99287.STM3477.

    Structurei

    Secondary structure

    1
    457
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85
    Beta strandi14 – 185
    Helixi22 – 3312
    Beta strandi36 – 449
    Helixi47 – 537
    Turni54 – 563
    Beta strandi59 – 646
    Helixi67 – 704
    Beta strandi74 – 785
    Helixi83 – 9513
    Beta strandi99 – 1024
    Beta strandi108 – 1125
    Beta strandi115 – 1195
    Beta strandi122 – 1276
    Helixi133 – 14614
    Helixi151 – 16818
    Helixi172 – 18211
    Helixi186 – 1938
    Helixi197 – 20812
    Beta strandi217 – 2226
    Beta strandi224 – 2263
    Helixi228 – 2303
    Helixi233 – 2419
    Beta strandi243 – 2475
    Helixi253 – 2564
    Beta strandi263 – 2675
    Helixi280 – 29112
    Beta strandi295 – 3028
    Turni304 – 3063
    Beta strandi307 – 3093
    Helixi310 – 3145
    Turni315 – 3217
    Beta strandi324 – 3274
    Helixi332 – 3398
    Turni347 – 3493
    Beta strandi351 – 3566
    Helixi368 – 3725
    Beta strandi373 – 38210
    Beta strandi384 – 3863
    Helixi387 – 39610
    Beta strandi404 – 4107
    Beta strandi417 – 4226
    Helixi423 – 4253
    Helixi426 – 4294
    Turni430 – 4323
    Beta strandi435 – 4428
    Helixi443 – 4497

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PJQX-ray2.21A/B1-457[»]
    1PJSX-ray2.40A/B1-457[»]
    1PJTX-ray2.80A/B1-457[»]
    ProteinModelPortaliP25924.
    SMRiP25924. Positions 1-457.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25924.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni4 – 202199Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelataseAdd
    BLAST
    Regioni216 – 448233Uroporphyrinogen-III C-methyltransferaseAdd
    BLAST
    Regioni301 – 3033S-adenosyl-L-methionine binding
    Regioni331 – 3322S-adenosyl-L-methionine binding

    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

    HOGENOMiHOG000290518.
    KOiK02302.
    OMAiQASFIMP.
    OrthoDBiEOG6DRPFR.
    PhylomeDBiP25924.

    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.

    P25924-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDHLPIFCQL RDRDCLIVGG GDVAERKARL LLEAGARLTV NALTFIPQFT    50
    VWANEGMLTL VEGPFDETLL DSCWLAIAAT DDDTVNQRVS DAAESRRIFC 100
    NVVDAPKAAS FIMPSIIDRS PLMVAVSSGG TSPVLARLLR EKLESLLPQH 150
    LGQVARYAGQ LRARVKKQFA TMGERRRFWE KFFVNDRLAQ SLANADEKAV 200
    NATTERLFSE PLDHRGEVVL VGAGPGDAGL LTLKGLQQIQ QADIVVYDRL 250
    VSDDIMNLVR RDADRVFVGK RAGYHCVPQE EINQILLREA QKGKRVVRLK 300
    GGDPFIFGRG GEELETLCHA GIPFSVVPGI TAASGCSAYS GIPLTHRDYA 350
    QSVRLVTGHL KTGGELDWEN LAAEKQTLVF YMGLNQAATI QEKLIAFGMQ 400
    ADMPVALVEN GTSVKQRVVH GVLTQLGELA QQVESPALII VGRVVALRDK 450
    LNWFSNH 457
    Length:457
    Mass (Da):50,147
    Last modified:May 1, 1992 - v1
    Checksum:i359C8CAF4B78092D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64606 Genomic DNA. Translation: AAA27041.1.
    AE006468 Genomic DNA. Translation: AAL22339.1.
    PIRiB39200.
    RefSeqiNP_462380.1. NC_003197.1.

    Genome annotation databases

    EnsemblBacteriaiAAL22339; AAL22339; STM3477.
    GeneIDi1255000.
    KEGGistm:STM3477.
    PATRICi32385755. VBISalEnt20916_3675.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64606 Genomic DNA. Translation: AAA27041.1 .
    AE006468 Genomic DNA. Translation: AAL22339.1 .
    PIRi B39200.
    RefSeqi NP_462380.1. NC_003197.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PJQ X-ray 2.21 A/B 1-457 [» ]
    1PJS X-ray 2.40 A/B 1-457 [» ]
    1PJT X-ray 2.80 A/B 1-457 [» ]
    ProteinModelPortali P25924.
    SMRi P25924. Positions 1-457.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 99287.STM3477.

    Proteomic databases

    PRIDEi P25924.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAL22339 ; AAL22339 ; STM3477 .
    GeneIDi 1255000.
    KEGGi stm:STM3477.
    PATRICi 32385755. VBISalEnt20916_3675.

    Phylogenomic databases

    HOGENOMi HOG000290518.
    KOi K02302.
    OMAi QASFIMP.
    OrthoDBi EOG6DRPFR.
    PhylomeDBi P25924.

    Enzyme and pathway databases

    UniPathwayi UPA00148 ; UER00211 .
    UPA00148 ; UER00222 .
    UPA00262 ; UER00211 .
    UPA00262 ; UER00222 .
    UPA00262 ; UER00376 .
    BioCyci MetaCyc:STM3477-MONOMER.
    SENT99287:GCTI-3499-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P25924.
    PROi P25924.

    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. "High-level expression of Escherichia coli NADPH-sulfite reductase: requirement for a cloned cysG plasmid to overcome limiting siroheme cofactor."
      Wu J.Y., Siegel L.M., Kredich N.M.
      J. Bacteriol. 173:325-333(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: LT2 / SGSC1412 / ATCC 700720.
    3. "CysG structure reveals tetrapyrrole-binding features and novel regulation of siroheme biosynthesis."
      Stroupe M.E., Leech H.K., Daniels D.S., Warren M.J., Getzoff E.D.
      Nat. Struct. Biol. 10:1064-1073(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF WILD-TYPE AND OF MUTANT ALA-128 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE AND NAD, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF SER-128; LEU-250; LYS-270 AND ASN-385, ACTIVE SITE, SUBUNIT, PHOSPHORYLATION AT SER-128.

    Entry informationi

    Entry nameiCYSG_SALTY
    AccessioniPrimary (citable) accession number: P25924
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: May 1, 1992
    Last modified: October 1, 2014
    This is version 117 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

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3