Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P25924 (CYSG_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Siroheme synthase

Including the following 3 domains:

  1. Uroporphyrinogen-III C-methyltransferase
    Short name=Urogen III methylase
    EC=2.1.1.107
    Alternative name(s):
    SUMT
    Uroporphyrinogen III methylase
    Short name=UROM
  2. Precorrin-2 dehydrogenase
    EC=1.3.1.76
  3. Sirohydrochlorin ferrochelatase
    EC=4.99.1.4
Gene names
Name:cysG
Ordered Locus Names:STM3477
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3

Catalytic activity

S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1. Ref.3

S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2. Ref.3

Precorrin-2 + NAD+ = sirohydrochlorin + NADH. Ref.3

Siroheme + 2 H+ = sirohydrochlorin + Fe2+. Ref.3

Pathway

Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. HAMAP-Rule MF_01646

Cofactor biosynthesis; adenosylcobalamin biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.

Porphyrin-containing compound metabolism; siroheme biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. HAMAP-Rule MF_01646

Porphyrin-containing compound metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1.

Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.

Subunit structure

Homodimer. Ref.3

Sequence similarities

In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family.

In the C-terminal section; belongs to the precorrin methyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 457457Siroheme synthase HAMAP-Rule MF_01646
PRO_0000150380

Regions

Nucleotide binding22 – 232NAD HAMAP-Rule MF_01646
Nucleotide binding43 – 442NAD HAMAP-Rule MF_01646
Region4 – 202199Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase HAMAP-Rule MF_01646
Region216 – 448233Uroporphyrinogen-III C-methyltransferase HAMAP-Rule MF_01646
Region301 – 3033S-adenosyl-L-methionine binding HAMAP-Rule MF_01646
Region331 – 3322S-adenosyl-L-methionine binding HAMAP-Rule MF_01646

Sites

Active site2481Proton acceptor Potential
Active site2701Proton donor Potential
Binding site2251S-adenosyl-L-methionine; via carbonyl oxygen
Binding site3061S-adenosyl-L-methionine; via carbonyl oxygen
Binding site3821S-adenosyl-L-methionine; via amide nitrogen
Binding site4111S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen
Binding site4371S-adenosyl-L-methionine; via carbonyl oxygen

Amino acid modifications

Modified residue1281Phosphoserine Ref.3

Experimental info

Mutagenesis1281S → A: Abolishes the methyltransferase activity and increases 3 and 4-fold the dehydrogenase and ferrochelatase activities, respectively. Ref.3
Mutagenesis1281S → D: Abolishes the methyltransferase activity and reduces 10 and 5-fold the dehydrogenase and ferrochelatase activities, respectively. Ref.3
Mutagenesis2501L → A: Abolishes the dehydrogenase and ferrochelatase activities and reduces 6-fold the methyltransferase activity. Ref.3
Mutagenesis2701K → I: Abolishes the methyltransferase, dehydrogenase and ferrochelatase activities. Ref.3
Mutagenesis3851N → A: Abolishes the dehydrogenase and ferrochelatase activities and reduces 10-fold the methyltransferase activity. Ref.3

Secondary structure

..................................................................................... 457
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P25924 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 359C8CAF4B78092D

FASTA45750,147
        10         20         30         40         50         60 
MDHLPIFCQL RDRDCLIVGG GDVAERKARL LLEAGARLTV NALTFIPQFT VWANEGMLTL 

        70         80         90        100        110        120 
VEGPFDETLL DSCWLAIAAT DDDTVNQRVS DAAESRRIFC NVVDAPKAAS FIMPSIIDRS 

       130        140        150        160        170        180 
PLMVAVSSGG TSPVLARLLR EKLESLLPQH LGQVARYAGQ LRARVKKQFA TMGERRRFWE 

       190        200        210        220        230        240 
KFFVNDRLAQ SLANADEKAV NATTERLFSE PLDHRGEVVL VGAGPGDAGL LTLKGLQQIQ 

       250        260        270        280        290        300 
QADIVVYDRL VSDDIMNLVR RDADRVFVGK RAGYHCVPQE EINQILLREA QKGKRVVRLK 

       310        320        330        340        350        360 
GGDPFIFGRG GEELETLCHA GIPFSVVPGI TAASGCSAYS GIPLTHRDYA QSVRLVTGHL 

       370        380        390        400        410        420 
KTGGELDWEN LAAEKQTLVF YMGLNQAATI QEKLIAFGMQ ADMPVALVEN GTSVKQRVVH 

       430        440        450 
GVLTQLGELA QQVESPALII VGRVVALRDK LNWFSNH 

« Hide

References

« Hide 'large scale' references
[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]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64606 Genomic DNA. Translation: AAA27041.1.
AE006468 Genomic DNA. Translation: AAL22339.1.
PIRB39200.
RefSeqNP_462380.1. NC_003197.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PJQX-ray2.21A/B1-457[»]
1PJSX-ray2.40A/B1-457[»]
1PJTX-ray2.80A/B1-457[»]
ProteinModelPortalP25924.
SMRP25924. Positions 1-457.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM3477.

Proteomic databases

PRIDEP25924.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL22339; AAL22339; STM3477.
GeneID1255000.
KEGGstm:STM3477.
PATRIC32385755. VBISalEnt20916_3675.

Phylogenomic databases

HOGENOMHOG000290518.
KOK02302.
OMAQASFIMP.
OrthoDBEOG6DRPFR.
PhylomeDBP25924.

Enzyme and pathway databases

BioCycMetaCyc:STM3477-MONOMER.
SENT99287:GCTI-3499-MONOMER.
UniPathwayUPA00148; UER00211.
UPA00148; UER00222.
UPA00262; UER00211.
UPA00262; UER00222.
UPA00262; UER00376.

Family and domain databases

Gene3D1.10.8.210. 1 hit.
3.30.950.10. 1 hit.
3.40.1010.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPMF_01646. Siroheme_synth.
InterProIPR000878. 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]
PfamPF10414. CysG_dimeriser. 1 hit.
PF13241. NAD_binding_7. 1 hit.
PF00590. TP_methylase. 1 hit.
[Graphical view]
PIRSFPIRSF036426. Sirohaem_synth. 1 hit.
SUPFAMSSF53790. SSF53790. 1 hit.
TIGRFAMsTIGR01469. cobA_cysG_Cterm. 1 hit.
TIGR01470. cysG_Nterm. 1 hit.
PROSITEPS00839. SUMT_1. 1 hit.
PS00840. SUMT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP25924.
PROP25924.

Entry information

Entry nameCYSG_SALTY
AccessionPrimary (citable) accession number: P25924
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: July 9, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways