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Reviewed, UniProtKB/Swiss-Prot A8G9Y3 (CYSG1_SERP5)

Last modified June 16, 2009. Version 16. 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 1
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: cysG1
Ordered Locus Names: Spro_0817
OrganismSerratia proteamaculans (strain 568) [Complete proteome] [HAMAP]
Taxonomic identifier399741 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

Protein attributes

Sequence length476 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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 – 476476Siroheme synthase 1 HAMAP MF_01646
PRO_0000330557

Regions

Region221 – 461241Uroporphyrinogen-III C-methyltransferase HAMAP MF_01646

Sequences

Sequence LengthMass (Da)Tools
A8G9Y3-1 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 2DAB7E09F9A3B2B9

FASTA47651,267
        10         20         30         40         50         60 
MDYLPIFADL KQRPVLVVGG GEVAARKVDL LLRAGAEIRI VAQSLSPILE QLSQQGQIHW 

        70         80         90        100        110        120 
LGQAFAAEQL DEVFLVIAAT DDSALNAEVF SEADKRRVLA NVVDDQPRCS FIFPSIIDRS 

       130        140        150        160        170        180 
PLVVAVSSSG QAPVLARMLR EKLEALLPAS LGQMAEVAGR WRGQVKQRLN AIGERRRFWE 

       190        200        210        220        230        240 
KTFGGRFATL VANGQTAEAQ RQLEQDLEQF AQGSEGTQGE IALVGAGPGD VGLLTLRGLQ 

       250        260        270        280        290        300 
VMQQADVVLY DHLVSDEILD LVRRDAERIC VGKRAGAHSV IQEETNRLLV ELAQQGKRVV 

       310        320        330        340        350        360 
RLKGGDPFIF GRGGEELQVA AAAGIPFQVV PGVTAAAGAT AYAGIPLTHR DHAQSVTFIT 

       370        380        390        400        410        420 
GHCRPDGDGL DWADLARARQ TLAIYMGTMK AADISQRLIA HGRAATTPVA VISRGTRADQ 

       430        440        450        460        470 
LVQTGTLQQL EQLAQQAPLP ALLVIGEVVE LHHQIAWFGH QPQAEGVSRP AVVNLA 

« Hide

References

[1]"Complete sequence of chromosome of Serratia proteamaculans 568."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. expand/collapse author list , Taghavi S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000826 Genomic DNA. Translation: ABV39923.1.
RefSeqYP_001477051.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5603444.
GenomeReviewsGene locus Spro_0817 in contig CP000826_GR.
KEGGspe:Spro_0817.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAA8G9Y3. DYAQSAV.

Family and domain databases

HAMAPMF_01646.
[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 nameCYSG1_SERP5
AccessionPrimary (citable) accession number: A8G9Y3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: November 13, 2007
Last modified: June 16, 2009
This is version 16 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