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A7MKK9 (CYSG2_CROS8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Siroheme synthase 2

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:cysG2
Ordered Locus Names:ESA_04366
OrganismCronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii) [Complete proteome] [HAMAP]
Taxonomic identifier290339 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCronobacter

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Multifunctional enzyme that catalyzes the SAM-dependent methylation of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 and then position C-12 or C-18 to form trimethylpyrrocorphin 2. It also catalyzes the conversion of precorrin-2 into siroheme. This reaction consists of the NAD-dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme By similarity. HAMAP MF_01646

Catalytic activity

S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1. HAMAP MF_01646

S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2. HAMAP MF_01646

Precorrin-2 + NAD+ = sirohydrochlorin + NADH. HAMAP MF_01646

Siroheme + 2 H+ = sirohydrochlorin + Fe2+. HAMAP MF_01646

Pathway

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

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

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

Porphyrin metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1. HAMAP MF_01646

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

Sequence similarities

Belongs to the precorrin methyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 457457Siroheme synthase 2 HAMAP MF_01646
PRO_0000330503

Regions

Region218 – 457240Uroporphyrinogen-III C-methyltransferase HAMAP MF_01646

Sequences

Sequence LengthMass (Da)Tools
A7MKK9 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: 612890921BD2F761

FASTA45750,052
        10         20         30         40         50         60 
MDHLPIFCQL RHRACLLVGG GDVAERKARL LLEAGAALTV NALAFAPQFK AWAKQGMLRL 

        70         80         90        100        110        120 
VQGEFNASLL DDCWLAIAAT DDDAVNNQVS EAAEARRIFC NVVDAPKQAS FIMPSIIDRS 

       130        140        150        160        170        180 
PLMVAISSGG TSPVLARLLR EKLEALLPQH LGKVAGYAGQ LRRRVKQTFT SMSERRRFWE 

       190        200        210        220        230        240 
KFFVNDRLAQ SLANDDEQAV TRITETLLSE PLDDRGEVVL VGAGPGDPGL LTLKGLQQIQ 

       250        260        270        280        290        300 
QADIVVYDRL VSDEIMNLVR RDADRVFVGK RAGYHCVPQE EINQILLREA QRGKRVVRLK 

       310        320        330        340        350        360 
GGDPFIFGRG GEELETLCDA GIPFSVVPGI TAASGCSAYA GLPLTHRDYA QSVRLITGHL 

       370        380        390        400        410        420 
KNGGEFDWHN LAAEKQTLVF YMGLNQAAAI QEKLIEHGMD PQMPVALVEN GTSVKQRVVA 

       430        440        450 
GVLTELGALA QRVESPSLII VGRVVALRDK LNWFSSK 

« Hide

References

[1]"Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic hybridization analysis with other Cronobacter species."
Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L., Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A., Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K., McClelland M., Forsythe S.J.
PLoS ONE 5:E9556-E9556(2010) [PubMed: 20221447] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-894.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000783 Genomic DNA. Translation: ABU79545.1.
RefSeqYP_001440381.1. NC_009778.1.

3D structure databases

ProteinModelPortalA7MKK9.
SMRA7MKK9. Positions 1-456.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7MKK9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5548171.
GenomeReviewsGene locus ESA_04366 in contig CP000783_GR.
KEGGesa:ESA_04366.
PATRIC20400327. VBICroSak107175_3891.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHBG730212.
OMAMCRRDAE.
ProtClustDBPRK10637.

Family and domain databases

HAMAPMF_01646. Siroheme_synth.
[Tree]
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]
Gene3DG3DSA:3.40.1010.10. 4pyrrole_Mease_sub1. 1 hit.
G3DSA:3.30.950.10. 4pyrrole_Mease_sub2. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:1.10.8.210. Sirohaem_synthase_dimer_dom. 1 hit.
KOK02302.
PfamPF10414. CysG_dimeriser. 1 hit.
PF00590. TP_methylase. 1 hit.
[Graphical view]
PIRSFPIRSF036426. Sirohaem_synth. 1 hit.
SUPFAMSSF53790. Cor/por_Metransf. 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...

Entry information

Entry nameCYSG2_CROS8
AccessionPrimary (citable) accession number: A7MKK9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: October 2, 2007
Last modified: January 25, 2012
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families