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 names

	Name:	cysG1
	OrderedLocusNames:	NMB1156
and
	Name:	cysG2
	OrderedLocusNames:	NMB1194

From

Neisseria meningitidis serogroup B

[TaxID: 491]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae; Neisseria.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=MC58 / Serogroup B;
McVeigh T., Wilkie S.E., Woodcock S.C., Mortuza G., Peters S.E., Warren M.J.;
"Sirohaem synthase from Neisseria meningitidis.";
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MC58 / Serogroup B;
DOI=10.1126/science.287.5459.1809; PubMed=10710307 [NCBI, ExPASy, EBI, Israel, Japan]
Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.;
"Complete genome sequence of Neisseria meningitidis serogroup B strain MC58.";
Science 287:1809-1815(2000).

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

Y10177; CAA71251.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE002098; AAF41542.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE002098; AAF41577.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D81111; D81111.
T46867; T46867.

RefSeq

NP_274184.1; -.
NP_274220.1; -.

3D structure databases

HSSP

O87696; 1CBF. [HSSP ENTRY / PDB]

ModBase

P95370.

Enzyme and pathway databases

BioCyc

NMEN122586:NMB_1156-MON; -.
NMEN122586:NMB_1194-MON; -.

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.
IPR006366; CobA_cysG_C.
IPR006367; CysG_synth_N.
IPR003043; Uropor_MeTrfase_CS.
Graphical view of domain structure.

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

P95370.

Genome annotation databases

GeneID

903577; -.
903614; -.

GenomeReviews

AE002098_GR; NMB1156.
AE002098_GR; NMB1194.

KEGG

nme:NMB1156; -.
nme:NMB1194; -.

TIGR

NMB1156; -.
NMB1194; -.

Phylogenomic databases

HOGENOM

P95370; -.

Other

ProtoNet

P95370.

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`	`1 483`	`483`	`Siroheme synthase.`	`PRO_0000150382`
`REGION`	`219 459`	`241`	`Uroporphyrinogen-III C-methyltransferase.`
`CONFLICT`	`475 483`		`GLNAGQRAA -> D (in Ref. 1; CAA71251).`

Sequence information

Length: 483 AA [This is the length of the unprocessed precursor]

Molecular weight: 52111 Da [This is the MW of the unprocessed precursor]

CRC64: 279C4F458B19582F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNYFPIFANL AGRPVLVVGG GAVAARKISL LLKAGAEVRV AAKHLNAELS ALAAENKILW 

        70         80         90        100        110        120 
LAEEFRAEHI RTVFLIIAAS SDQALNRRVF HLAESCQKPV NVVDDRDHCS FIFPSVIDRN 

       130        140        150        160        170        180 
PVQIAVSSSG SAPVLARLLR ERLEALLPPS LGDMAEISGR WRDAVKGKLK SVTERRRFWE 

       190        200        210        220        230        240 
KQFNGRFAAL VKNRQNTLAE RELAGQLEQS RQNDQGGSVS LVGAGPGDAG LLTLKGLQEI 

       250        260        270        280        290        300 
QQADVVLYDA LVSDGILSLV RRDAERIFVG KRARGERTPQ EDTNALMVRL AREGRRVVRL 

       310        320        330        340        350        360 
KGGDPFVFGR GGEELETLAR HQIPFSVVPG ITAAVGATAY AGIPLTHRDY AQSAVFVTGH 

       370        380        390        400        410        420 
RKADAPDIEW QTLARSRQTL VIYMGALKAA LIAERLQQHG RSPDTPAAVI SQGTLPAQKT 

       430        440        450        460        470        480 
ATGTLANLAE LAETAPNPAL IVIGEVVGLH EKLAWFGENG EGENRVGQTY PALGGLNAGQ 


RAA

P95370 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