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:	cysG
	OrderedLocusNames:	BP1055

From

Bordetella pertussis

[TaxID: 520]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Alcaligenaceae; Bordetella.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
DOI=10.1038/ng1227; PubMed=12910271 [NCBI, ExPASy, EBI, Israel, Japan]
Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica.";
Nat. Genet. 35:32-40(2003).

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

BX640414; CAE41354.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_879840.1; -.

3D structure databases

HSSP

P25924; 1PJT. [HSSP ENTRY / PDB]

ModBase

Q7VZ77.

Enzyme and pathway databases

BioCyc

BPER257313:BP1055-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

Q7VZ77.

Genome annotation databases

2664362; -.

BX470248_GR; BP1055.

bpe:BP1055; -.

fig|257313.1.peg.918; -.

Phylogenomic databases

HOGENOM

Q7VZ77; -.

Genome annotation databases

CMR

Q7VZ77; BP1055.

Other

ProtoNet

Q7VZ77.

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`	`1 473`	`473`	`Siroheme synthase.`	`PRO_0000330499`
`REGION`	`218 461`	`244`	`Uroporphyrinogen-III C-methyltransferase.`

Sequence information

Length: 473 AA [This is the length of the unprocessed precursor]

Molecular weight: 50524 Da [This is the MW of the unprocessed precursor]

CRC64: E68DF9621CA27612 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTLFPIFADL TGRRVLVVGG GAVAVRKTQA LLQAGAEVVV GAPRLDPALA ALAEQGGIAR 

        70         80         90        100        110        120 
LDGGFEPAWL AGAWLVVAAT DDRAVNAAVS EAARARRVFC NVVDDAELSS FQVPSVVDRS 

       130        140        150        160        170        180 
PLIVAISSSG VAPVLARRLR ERIESLFDHS LGQLAALAAR YRPRIRAARP DLGQRRRFYD 

       190        200        210        220        230        240 
WLLDGPVAAR LRQQQPGLAE QELEQALRAP QAAPRGSVVL VGAGPGDPGL LTLKALRALN 

       250        260        270        280        290        300 
EADIILYDRL VSEGVLALAR RDAERVPVGK LPGKGHDATQ ARIHALMLAQ ARAGRRVVRL 

       310        320        330        340        350        360 
KGGDAFIFGR GGEELEYLRA HGVPYEVVPG ITAALACAAY AGMPLTHRDH AQSVRMVTAH 

       370        380        390        400        410        420 
CRADQDTLDW AGLARDQQTL AFYMGVGQLD YVTARLLEHG RAPATPFALI ENGSRPEQRV 

       430        440        450        460        470 
VTGTLADLPE IARRRGVRPP ALLVIGEVAA LADTLQWFGQ HQRGLPGPQA LAA

Q7VZ77 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