Reviewed, UniProtKB/Swiss-Prot P25924 (CYSG_SALTY)

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

Protein attributes

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

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.

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...

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

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457

Helix Strand Turn

Details...

Beta strand

4 – 8

5

Beta strand

14 – 18

5

Helix

22 – 33

12

Beta strand

36 – 44

9

Helix

47 – 53

7

Turn

54 – 56

3

Beta strand

59 – 64

6

Helix

67 – 70

4

Beta strand

74 – 78

5

Helix

83 – 95

13

Beta strand

99 – 102

4

Beta strand

108 – 112

5

Beta strand

115 – 119

5

Beta strand

122 – 127

6

Helix

133 – 146

14

Helix

151 – 168

18

Helix

172 – 182

11

Helix

186 – 193

8

Helix

197 – 208

12

Beta strand

217 – 222

6

Beta strand

224 – 226

3

Helix

228 – 230

3

Helix

233 – 241

9

Beta strand

243 – 247

5

Helix

253 – 256

4

Beta strand

263 – 267

5

Helix

280 – 291

12

Beta strand

295 – 302

8

Turn

304 – 306

3

Beta strand

307 – 309

3

Helix

310 – 314

5

Turn

315 – 321

7

Beta strand

324 – 327

4

Helix

332 – 339

8

Turn

347 – 349

3

Beta strand

351 – 356

6

Helix

368 – 372

5

Beta strand

373 – 382

10

Beta strand

384 – 386

3

Helix

387 – 396

10

Beta strand

404 – 410

7

Beta strand

417 – 422

6

Helix

423 – 425

3

Helix

426 – 429

4

Beta strand

435 – 442

8

Helix

443 – 449

7

Sequences

	Sequence		Length	Mass (Da)
	P25924-1 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 359C8CAF4B78092D	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

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. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., 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.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M64606 Genomic DNA. Translation: AAA27041.1.
AE006468 Genomic DNA. Translation: AAL22339.1.

PIR

B39200.

RefSeq

NP_462380.1.

3D structure databases

PDBPDBe

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...

Proteomic databases

PRIDE

P25924.

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

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...

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:	November 3, 2009
This is version 81 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)