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Reviewed, UniProtKB/Swiss-Prot Q8FCW8 (CYSG_ECOL6)

Last modified February 9, 2010. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Siroheme synthase
Including the following 3 domains:
    1- Recommended name:
            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- Recommended name:
            Precorrin-2 dehydrogenase
              EC=1.3.1.76
    3- Recommended name:
            Sirohydrochlorin ferrochelatase
              EC=4.99.1.4
Gene names
Name: cysG
Ordered Locus Names: c4144
OrganismEscherichia coli O6 [Complete proteome] [HAMAP]
Taxonomic identifier217992 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

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 HAMAP MF_01646
PRO_0000330510

Regions

Region218 – 457240Uroporphyrinogen-III C-methyltransferase HAMAP MF_01646

Sequences

Sequence LengthMass (Da)Tools
Q8FCW8-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: C76E0DC91D4DF2E5

FASTA45749,977
        10         20         30         40         50         60 
MDHLPIFCQL RDRDCLIVGG GDVAERKARL LLDAGARLTV NALAFIPQFT AWADAGMLTL 

        70         80         90        100        110        120 
VEGPFDESLL DTCWLAIAAT DDDALNQRVS EAAEARRIFC NVVDAPKAAS FIMPSIIDRS 

       130        140        150        160        170        180 
PLMVAVSSGG TSPVLARLLR EKLESLLPLH LGQVAKYAGQ LRGRVKQQFA TMGERRRFWE 

       190        200        210        220        230        240 
KLFVNDRLAQ SLANNDQKAI TETTEQLINE PLDHRGEVVL VGAGPGDAGL LTLKGLQQIQ 

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

       310        320        330        340        350        360 
GGDPFIFGRG GEELETLCNA GIPFSVVPGI TAASGCSAYS GIPLTHRDYA QSVRLITGHL 

       370        380        390        400        410        420 
KTGGELDWEN LAAEKQTLVF YMGLNQAATI QQKLIEYGMP GEMPVAIVEN GTAVTQRVID 

       430        440        450 
GTLTQLGELA QQMNSPSLII IGRVVGLRDK LNWFSNH 

« Hide

References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN82582.1.
RefSeqNP_756008.1.

3D structure databases

HSSPHSSP built from PDB template 1PJQ based on UniProtKB P25924.
SMRQ8FCW8. Positions 1-457.
ModBaseSearch...

Genome annotation databases

GeneID1036683.
GenomeReviewsGene locus c4144 in contig AE014075_GR.
KEGGecc:c4144.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG730212.
OMAMCRRDAE.

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.
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.
PfamPF10414. CysG_dimeriser. 1 hit.
PF00590. TP_methylase. 1 hit.
[Graphical view]
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 nameCYSG_ECOL6
AccessionPrimary (citable) accession number: Q8FCW8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: March 1, 2003
Last modified: February 9, 2010
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents