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:	STM3477

From

Salmonella typhimurium

[TaxID: 602]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Salmonella.

Protein existence

1: Evidence at protein level;

References

[1]

NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1987123 [NCBI, ExPASy, EBI, Israel, Japan]
Wu J.Y., Siegel L.M., Kredich N.M.;
"High-level expression of Escherichia coli NADPH-sulfite reductase: requirement for a cloned cysG plasmid to overcome limiting siroheme cofactor.";
J. Bacteriol. 173:325-333(1991).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LT2 / SGSC1412 / ATCC 700720;
DOI=10.1038/35101614; PubMed=11677609 [NCBI, ExPASy, EBI, Israel, Japan]
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.;
"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
Nature 413:852-856(2001).

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.
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

M64606; AAA27041.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE008859; AAL22339.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B39200; B39200.

RefSeq

NP_462380.1; -.

3D structure databases

PDB

1PJQ; X-ray; 2.21 A; A/B=1-457.	[ExPASy / RCSB / EBI]
1PJS; X-ray; 2.40 A; A/B=1-457.	[ExPASy / RCSB / EBI]
1PJT; X-ray; 2.80 A; A/B=1-457.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1PJQ; -.
1PJS; -.
1PJT; -.

ModBase

P25924.

Enzyme and pathway databases

BioCyc

MetaCyc:STM3477-MON; -.
STYP99287:STM3477-MON; -.

Organism-specific databases

StyGene

SG10074; cysG.

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

P25924.

Genome annotation databases

GeneID

1255000; -.

GenomeReviews

AE006468_GR; STM3477.

KEGG

stm:STM3477; -.

NMPDR

fig|99287.1.peg.3357; -.

Phylogenomic databases

HOGENOM

P25924; -.

Genome annotation databases

CMR

P25924; STM3477.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; 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`	`1 457`	`457`	`Siroheme synthase.`	`PRO_0000150380`
`REGION`	`218 457`	`240`	`Uroporphyrinogen-III C-methyltransferase.`
`STRAND`	`4 8`	`5`
`STRAND`	`14 18`	`5`
`HELIX`	`22 33`	`12`
`STRAND`	`36 44`	`9`
`HELIX`	`47 53`	`7`
`TURN`	`54 56`	`3`
`STRAND`	`59 64`	`6`
`HELIX`	`67 70`	`4`
`STRAND`	`74 78`	`5`
`HELIX`	`83 95`	`13`
`STRAND`	`99 102`	`4`
`STRAND`	`108 112`	`5`
`STRAND`	`115 119`	`5`
`STRAND`	`122 127`	`6`
`HELIX`	`133 146`	`14`
`HELIX`	`151 168`	`18`
`HELIX`	`172 182`	`11`
`HELIX`	`186 193`	`8`
`HELIX`	`197 208`	`12`
`STRAND`	`217 222`	`6`
`STRAND`	`224 226`	`3`
`HELIX`	`228 230`	`3`
`HELIX`	`233 241`	`9`
`STRAND`	`243 247`	`5`
`HELIX`	`253 256`	`4`
`STRAND`	`263 267`	`5`
`HELIX`	`280 291`	`12`
`STRAND`	`295 302`	`8`
`TURN`	`304 306`	`3`
`STRAND`	`307 309`	`3`
`HELIX`	`310 314`	`5`
`TURN`	`315 321`	`7`
`STRAND`	`324 327`	`4`
`HELIX`	`332 339`	`8`
`TURN`	`347 349`	`3`
`STRAND`	`351 356`	`6`
`HELIX`	`368 372`	`5`
`STRAND`	`373 382`	`10`
`STRAND`	`384 386`	`3`
`HELIX`	`387 396`	`10`
`STRAND`	`404 410`	`7`
`STRAND`	`417 422`	`6`
`HELIX`	`423 425`	`3`
`HELIX`	`426 429`	`4`
`STRAND`	`435 442`	`8`
`HELIX`	`443 449`	`7`

Sequence information

Length: 457 AA [This is the length of the unprocessed precursor]

Molecular weight: 50147 Da [This is the MW of the unprocessed precursor]

CRC64: 359C8CAF4B78092D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDHLPIFCQL RDRDCLIVGG GDVAERKARL LLEAGARLTV NALTFIPQFT VWANEGMLTL 

        70         80         90        100        110        120 
VEGPFDETLL DSCWLAIAAT DDDTVNQRVS DAAESRRIFC NVVDAPKAAS FIMPSIIDRS 

       130        140        150        160        170        180 
PLMVAVSSGG TSPVLARLLR EKLESLLPQH LGQVARYAGQ LRARVKKQFA TMGERRRFWE 

       190        200        210        220        230        240 
KFFVNDRLAQ SLANADEKAV NATTERLFSE PLDHRGEVVL VGAGPGDAGL LTLKGLQQIQ 

       250        260        270        280        290        300 
QADIVVYDRL VSDDIMNLVR RDADRVFVGK RAGYHCVPQE EINQILLREA QKGKRVVRLK 

       310        320        330        340        350        360 
GGDPFIFGRG GEELETLCHA GIPFSVVPGI TAASGCSAYS GIPLTHRDYA QSVRLVTGHL 

       370        380        390        400        410        420 
KTGGELDWEN LAAEKQTLVF YMGLNQAATI QEKLIAFGMQ ADMPVALVEN GTSVKQRVVH 

       430        440        450 
GVLTQLGELA QQVESPALII VGRVVALRDK LNWFSNH

P25924 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