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:	cysG2
	OrderedLocusNames:	ECA4081

From

Erwinia carotovora subsp. atroseptica (Pectobacterium atrosepticum)

[TaxID: 29471]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Pectobacterium.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SCRI 1043 / ATCC BAA-672;
DOI=10.1073/pnas.0402424101; PubMed=15263089 [NCBI, ExPASy, EBI, Israel, Japan]
Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J., Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K., Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J., Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H., Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S., Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
"Genome sequence of the enterobacterial phytopathogen Erwinia carotovora subsp. atroseptica and characterization of virulence factors.";
Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).

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

BX950851; CAG76978.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_052168.1; -.

3D structure databases

ModBase

Q6CZS0.

Enzyme and pathway databases

BioCyc

ECAR218491:ECA4081-MONOMER; -.

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

Q6CZS0.

Genome annotation databases

GeneID

2882115; -.

GenomeReviews

BX950851_GR; ECA4081.

KEGG

eca:ECA4081; -.

NMPDR

fig|218491.3.peg.2912; -.

Phylogenomic databases

HOGENOM

Q6CZS0; -.

Genome annotation databases

CMR

Q6CZS0; ECA4081.

Other

ProtoNet

Q6CZS0.

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`	`1 459`	`459`	`Siroheme synthase 2.`	`PRO_0000330506`
`REGION`	`218 457`	`240`	`Uroporphyrinogen-III C-methyltransferase.`

Sequence information

Length: 459 AA [This is the length of the unprocessed precursor]

Molecular weight: 50607 Da [This is the MW of the unprocessed precursor]

CRC64: 0CC2A1827080646F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDYLPIFCQL HDKPCLLVGG GEIAERKARL LLDAGAVITV NALDFNDQFR AWEKDAQLTL 

        70         80         90        100        110        120 
VHSTFDPALL NEVWLVIAAT DNQDVNNHVY ASASERRIFC NVVDSPERAS FIMPSIIDRS 

       130        140        150        160        170        180 
PLMVAVSSGG TAPVLARLLR EKLESILPQN LGKLAAFAGE LRSRVKIRFC KMSARRRFWE 

       190        200        210        220        230        240 
KLFVHDRLAQ ALASEDRERV QQLTELLFSA PLDDRGEVTL VGAGPGDAGL LTLKGLQHLQ 

       250        260        270        280        290        300 
QADIVVYDRL VSKEILNLSR RDAERIFVGK ASGYHSVPQD QINQLLEEKA RAGHRVVRLK 

       310        320        330        340        350        360 
GGDPFIFGRG AEELEYLQQA GVPFSVVPGI TAASGCSAYS GIPLTHRDHS QGVRLITGHV 

       370        380        390        400        410        420 
KHDTDLDWSS LAAEKQTLVF YMGLQQAEHI QNKLIEQQLP ETVPVAIIEN GTSTKQRVLS 

       430        440        450 
GQLSQLGELA QQASSPSLII IGNVVGLREK LSWFSDQTA

Q6CZS0 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