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:	YE3968

From

Yersinia enterocolitica serotype O:8 / biotype 1B (strain 8081)

[TaxID: 393305]

[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.0020206; PubMed=17173484 [NCBI, ExPASy, EBI, Israel, Japan]
Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L., Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T., Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S., Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J., Prentice M.B.;
"The complete genome sequence and comparative genome analysis of the high pathogenicity Yersinia enterocolitica strain 8081.";
PLoS Genet. 2:2039-2051(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

AM286415; CAL13987.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001008113.1; -.

3D structure databases

SMR

A1JSB7; 1-456.

ModBase

A1JSB7.

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

A1JSB7.

Genome annotation databases

4716180; -.

AM286415_GR; YE3968.

yen:YE3968; -.

fig|630.2.peg.3898; -.

CMR

A1JSB7; YE3968.

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`	`1 472`	`472`	`Siroheme synthase 2.`	`PRO_0000330571`
`REGION`	`218 457`	`240`	`Uroporphyrinogen-III C-methyltransferase.`

Sequence information

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

Molecular weight: 51812 Da [This is the MW of the unprocessed precursor]

CRC64: 51BE67EF4B78F238 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDYFPIFCQL QNKACLLVGG GEVAERKARL LLDAGAAVTV NACEFTEQFH DWAEQGLLSL 

        70         80         90        100        110        120 
VSGEFAPELL AEKWLVIAAT DQVAVNALVY QSANQQRVFC NVVDDPKRTS FIMPSIIDRS 

       130        140        150        160        170        180 
PIMIAISSGG KAPVLARLLR EKLEAMLPQH LGQLAQLAGN LRQRVKQHFA AMTDRRRFWE 

       190        200        210        220        230        240 
KLLTHDRLAQ SLANEDQVQV EQHVEQLFNA PLSDRGEVVL VGAGPGDAGL LTLKGLQQIQ 

       250        260        270        280        290        300 
QADVVVYDRL VSDEVMNLVR RDAERIFVGK ESGRHTVPQD QINQILLQQA QQGKRVVRLK 

       310        320        330        340        350        360 
GGDPFIFGRG GEELETLADY NIPFSVVPGI TAASGCSAYS GIPLTHRDHA QSVRLITGHA 

       370        380        390        400        410        420 
KKDSQLDWAN LAAEKQTLVF YMGLSQAGEI QQQLIRHGMP AATPVALVEN GTSRHQRVVS 

       430        440        450        460        470 
GELSQLALLS QQVSSPSLII VGSVVSLREK LNWFSSAEHG KTGMKEQVER VG

A1JSB7 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