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:	YPN_0726

From

Yersinia pestis bv. Antiqua (strain Nepal516)

[TaxID: 377628]

[HAMAP proteome]

Taxonomy

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

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.00124-06; PubMed=16740952 [NCBI, ExPASy, EBI, Israel, Japan]
Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
"Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516: evidence of gene reduction in an emerging pathogen.";
J. Bacteriol. 188:4453-4463(2006).

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

CP000305; ABG17058.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

AI0408; AI0408.

RefSeq

YP_646658.1; -.

3D structure databases

ModBase

Q1CLS2.

Ontologies

GO:0043115;	Molecular function: precorrin-2 dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0051266;	Molecular function: sirohydrochlorin ferrochelatase activity (inferred from electronic annotation from EC).
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

Q1CLS2.

Genome annotation databases

GeneID

4123560; -.

GenomeReviews

CP000305_GR; YPN_0726.

KEGG

ypn:YPN_0726; -.

Phylogenomic databases

HOGENOM

Q1CLS2; -.

Genome annotation databases

CMR

Q1CLS2; YPN_0726.

Other

ProtoNet

Q1CLS2.

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_0000330574`
`REGION`	`217 457`	`241`	`Uroporphyrinogen-III C-methyltransferase.`

Sequence information

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

Molecular weight: 50904 Da [This is the MW of the unprocessed precursor]

CRC64: 1BD7DB7E5ADE5222 [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 
PDGDDLDWQT LARGRQTLAI YMGTVKAAAI SQQLIAHGRS STTPVAVIGR GTRVDQQVLI 

       430        440        450        460        470 
GTLAQLESLA QQAPTPALLV IGEVVNLHHQ IAWFGQQPQT ESAISPSVVN LA

Q1CLS2 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