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:	Spro_0817

From

Serratia proteamaculans (strain 568)

[TaxID: 399741]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Serratia.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., Taghavi S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
"Complete sequence of chromosome of Serratia proteamaculans 568.";
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.

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

CP000826; ABV39923.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001477051.1; -.

3D structure databases

ModBase

A8G9Y3.

Ontologies

GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
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:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

ProtoNet

A8G9Y3.

Genome annotation databases

GeneID

5603444; -.

GenomeReviews

CP000826_GR; Spro_0817.

KEGG

spe:Spro_0817; -.

CMR

A8G9Y3; Spro_0817.

Other

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`	`1 476`	`476`	`Siroheme synthase 1.`	`PRO_0000330557`
`REGION`	`221 461`	`241`	`Uroporphyrinogen-III C-methyltransferase.`

Sequence information

Length: 476 AA [This is the length of the unprocessed precursor]

Molecular weight: 51267 Da [This is the MW of the unprocessed precursor]

CRC64: 2DAB7E09F9A3B2B9 [This is a checksum on the sequence]

        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

A8G9Y3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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