Siroheme synthase - Salmonella typhimurium

Names and origin

Protein names

Recommended name:
    Siroheme synthase
Including the following 3 domains:
    1- Recommended name:
            Uroporphyrinogen-III C-methyltransferase
                Short name=Urogen III methylase
              EC=2.1.1.107
        Alternative name(s):
            SUMT
            Uroporphyrinogen III methylase
              Short name=UROM
    2- Recommended name:
            Precorrin-2 dehydrogenase
              EC=1.3.1.76
    3- Recommended name:
            Sirohydrochlorin ferrochelatase
              EC=4.99.1.4

Gene names

Name:	cysG
Ordered Locus Names:	STM3477

Organism

Salmonella typhimurium [Complete proteome] [HAMAP]

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

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Protein attributes

Sequence length	457 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Multifunctional enzyme that catalyzes 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 consists of the NAD-dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme. HAMAP MF_01646
Catalytic activity	S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1. HAMAP MF_01646 S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2. HAMAP MF_01646 Precorrin-2 + NAD⁺ = sirohydrochlorin + NADH. HAMAP MF_01646 Siroheme + 2 H⁺ = sirohydrochlorin + Fe²⁺. HAMAP MF_01646
Pathway	Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. HAMAP MF_01646 Cofactor biosynthesis; adenosylcobalamin biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. Porphyrin metabolism; siroheme biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. HAMAP MF_01646 Porphyrin metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1. HAMAP MF_01646 Porphyrin metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
Sequence similarities	Belongs to the precorrin methyltransferase family.

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Ontologies

Keywords
Biological process	Cobalamin biosynthesis Porphyrin biosynthesis
Ligand	NAD S-adenosyl-L-methionine
Molecular function	Lyase Methyltransferase Oxidoreductase Transferase
Technical term	3D-structure Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	cobalamin biosynthetic process Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW siroheme biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	binding Inferred from electronic annotation. Source: InterPro precorrin-2 dehydrogenase activity Inferred from electronic annotation. Source: HAMAP sirohydrochlorin ferrochelatase activity Inferred from electronic annotation. Source: EC uroporphyrin-III C-methyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 457

457

Siroheme synthase HAMAP MF_01646

PRO_0000150380

Regions

Region

218 – 457

240

Uroporphyrinogen-III C-methyltransferase HAMAP MF_01646

Secondary structure

1

.

457

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P25924-1 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 359C8CAF4B78092D
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FASTA

457

50,147

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"High-level expression of Escherichia coli NADPH-sulfite reductase: requirement for a cloned cysG plasmid to overcome limiting siroheme cofactor." Wu J.Y., Siegel L.M., Kredich N.M. J. Bacteriol. 173:325-333(1991) [PubMed: 1987123] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." 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. Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

M64606 Genomic DNA. Translation: AAA27041.1.
AE008859 Genomic DNA. Translation: AAL22339.1.

PIR

B39200.

RefSeq

NP_462380.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PJQ	X-ray	2.21	A/B	1-457	[»]
1PJS	X-ray	2.40	A/B	1-457	[»]
1PJT	X-ray	2.80	A/B	1-457	[»]

ModBase

Search...

Genome annotation databases

GeneID

1255000.

GenomeReviews

Gene locus STM3477 in contig AE006468_GR.

KEGG

stm:STM3477.

NMPDR

fig|99287.1.peg.3357.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

P25924.

OMA

P25924. MCRRDAE.

Enzyme and pathway databases

BioCyc

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

BRENDA

1.3.1.76. 2.
2.1.1.107. 2.
4.99.1.4. 2.

Family and domain databases

HAMAP

MF_01646.
[Tree]

InterPro

IPR000878. 4pyrrol_Mease.
IPR014777. 4pyrrole_Mease_sub1.
IPR014776. 4pyrrole_Mease_sub2.
IPR006366. CobA_cysG_C.
IPR016040. NAD(P)-bd_dom.
IPR019478. Sirohaem_synthase_dimer_dom.
IPR006367. Sirohaem_synthase_N.
IPR003043. Uropor_MeTrfase_CS.
[Graphical view]

Gene3D

G3DSA:3.40.1010.10. 4pyrrole_Mease_sub1. 1 hit.
G3DSA:3.30.950.10. 4pyrrole_Mease_sub2. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

Pfam

PF10414. CysG_dimeriser. 1 hit.
PF00590. TP_methylase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01469. cobA_cysG_Cterm. 1 hit.
TIGR01470. cysG_Nterm. 1 hit.

PROSITE

PS00839. SUMT_1. 1 hit.
PS00840. SUMT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

CYSG_SALTY

Accession

Primary (citable) accession number: P25924

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	June 16, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families