Uroporphyrinogen-III C-methyltransferase
     (Urogen III methylase)
     (EC 2.1.1.107)
     (SUMT)
     (Uroporphyrinogen III methylase)
     (UROM)
Precorrin-2 dehydrogenase
     (EC 1.3.1.76)
Sirohydrochlorin ferrochelatase
     (EC 4.99.1.4)

Gene name

	Name:	cysG1
	OrderedLocusNames:	YpsIP31758_3305

From

Yersinia pseudotuberculosis serotype O:1b (strain IP 31758)

[TaxID: 349747]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Yersinia.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1371/journal.pgen.0030142; PubMed=17784789 [NCBI, ExPASy, EBI, Israel, Japan]
Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G., Fayolle C., Lindler L.E., Carniel E., Ravel J.;
"The complete genome sequence of Yersinia pseudotuberculosis IP31758, the causative agent of Far East scarlet-like fever.";
PLoS Genet. 3:1508-1523(2007).

Comments

FUNCTION: Multifunctional enzyme that catalyze 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 consist 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.
CATALYTIC ACTIVITY: S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2.
CATALYTIC ACTIVITY: Precorrin-2 + NAD⁺ = sirohydrochlorin + NADH.
CATALYTIC ACTIVITY: Siroheme + 2 H⁺ = sirohydrochlorin + Fe²⁺.
PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1 .
PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; sirohydrochlorin from precorrin-2: step 1/1 .
PATHWAY: Porphyrin metabolism; siroheme biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1 .
PATHWAY: Porphyrin metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1 .
PATHWAY: Porphyrin metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1 .
SIMILARITY: Belongs to the precorrin methyltransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CP000720; ABS48251.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001402262.1; -.

3D structure databases

ModBase

A7FLY4.

Ontologies

GO:0004325;	Molecular function: ferrochelatase activity (inferred from electronic annotation from HAMAP).
GO:0043115;	Molecular function: precorrin-2 dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0004851;	Molecular function: uroporphyrin-III C-methyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0009236;	Biological process: cobalamin biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0019354;	Biological process: siroheme biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01646; -; 1.
PBIL [Tree]

InterPro

IPR000878; 4pyrrol_Mease.
IPR014777; 4pyrrole_Mease_sub1.
IPR014776; 4pyrrole_Mease_sub2.
IPR006366; CobA_cysG_C.
IPR006367; CysG_synth_N.
IPR016040; NAD(P)-bd.
IPR003043; Uropor_MeTrfase_CS.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.1010.10; 4pyrrole_Mease_sub1; 1.
G3DSA:3.30.950.10; 4pyrrole_Mease_sub2; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF00590; TP_methylase; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01469; cobA_cysG_Cterm; 1.
TIGR01470; cysG_Nterm; 1.

PROSITE

PS00839; SUMT_1; 1.
PS00840; SUMT_2; 1.

BLOCKS

A7FLY4.

Genome annotation databases

GeneID

5386338; -.

GenomeReviews

CP000720_GR; YpsIP31758_3305.

KEGG

ypi:YpsIP31758_3305; -.

NMPDR

fig|349747.3.peg.3407; -.

CMR

A7FLY4; YpsIP31758_3305.

Other

ProtoNet

A7FLY4.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cobalamin biosynthesis; Complete proteome; Lyase; Methyltransferase; Multifunctional enzyme; NAD; Oxidoreductase; Porphyrin biosynthesis; S-adenosyl-L-methionine; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 472`	`472`	`Siroheme synthase 1.`	`PRO_0000330580`
`REGION`	`217 457`	`241`	`Uroporphyrinogen-III C-methyltransferase.`

Sequence information

Length: 472 AA [This is the length of the unprocessed precursor]

Molecular weight: 50901 Da [This is the MW of the unprocessed precursor]

CRC64: D2D7DB7E4BCF4F98 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDYLPLFADL KQRPVLIVGG GEVAARKIEL LHRAGAQVWV VAQTLSSELE QQYQDGRIHW 

        70         80         90        100        110        120 
LAQDFLPEQL DNVFLVIAAT NDTVLNAAVF AAADQRCILA NVVDDQPLCS FIFPSIVDRS 

       130        140        150        160        170        180 
PLVVAISSSG QAPVLARILR EKLEALLPTR LSDMAAIAGR WRGRVKQHMA SMGERRRFWE 

       190        200        210        220        230        240 
HAFSGRFASL ISRGQLTEAE NELQLSLEGQ HRALGEVALV GAGPGDAGLL TLRGLQVMQQ 

       250        260        270        280        290        300 
ADVVLYDHLV SPEVLDLVRR DAERICVGKR AGAHSVTQEA TNQLLVTLAQ QGKRVVRLKG 

       310        320        330        340        350        360 
GDPFIFGRGG EELQVVAQAG IPFQVVPGVT AAAGATAYAG IPLTHRDHAQ SVTFITGHCR 

       370        380        390        400        410        420 
PDGDDLDWQA LARGRQTLAI YMGTVKAAAI SQQLIAHGRS STTPVAVIGR GTRVDQQVLI 

       430        440        450        460        470 
GTLAQLESLA QQAPTPALLV IGEVVNLHHQ IAWFGQQPQT ESAINPSVVN LA

A7FLY4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools