Reviewed, UniProtKB/Swiss-Prot Q1CLS2 (CYSG1_YERPN)

Names and origin

Protein names

Recommended name:
    Siroheme synthase 1
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:	cysG1
Ordered Locus Names:	YPN_0726

Organism

Yersinia pestis bv. Antiqua (strain Nepal516) [Complete proteome] [HAMAP]

Taxonomic identifier

377628 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia

Protein attributes

Sequence length	472 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (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. S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2. Precorrin-2 + NAD(+) = sirohydrochlorin + NADH. Siroheme + 2 H(+) = sirohydrochlorin + Fe(2+).
Pathway	Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. Cofactor biosynthesis; adenosylcobalamin biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. Porphyrin metabolism; siroheme biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. Porphyrin metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1. 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	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 – 472	472	Siroheme synthase 1		PRO_0000330574
Regions
	Region	217 – 457	241	Uroporphyrinogen-III C-methyltransferase

Sequences

	Sequence		Length	Mass (Da)
	Q1CLS2-1 [UniParc]. Last modified July 11, 2006. Version 1. Checksum: 1BD7DB7E5ADE5222	FASTA	472	50,904
	10 20 30 40 50 60 MDYLPLFADL KQRPVLIVGG GEVAARKIEL LHRAGAQVWV VAQTLSSELE QQYQDGRIHW 70 80 90 100 110 120 LAQDFLPEQL DNVFLVIAAT NDTVLNAAVF AAADQRCILA NVVDDQPLCS FIFPSIVDRS 130 140 150 160 170 180 PLVVAISSSG QAPVLARILR EKLEALLPTR LSDMAAIAGR WRGRVKQHMA SMGERRRFWE 190 200 210 220 230 240 HAFSGRFASL ISRGQLTEAE NELQLSLEGQ HRALGEVALV GAGPGDAGLL TLRGLQVMQQ 250 260 270 280 290 300 ADVVLYDHLV SPEVLDLVRR DAERICVGKR AGAHSVTQEA TNQLLVTLAQ QGKRVVRLKG 310 320 330 340 350 360 GDPFIFGRGG EELQVVAQAG IPFQVVPGVT AAAGATAYAG IPLTHRDHAQ SVTFITGHCR 370 380 390 400 410 420 PDGDDLDWQT LARGRQTLAI YMGTVKAAAI SQQLIAHGRS STTPVAVIGR GTRVDQQVLI 430 440 450 460 470 GTLAQLESLA QQAPTPALLV IGEVVNLHHQ IAWFGQQPQT ESAISPSVVN LA

References

[1]

"Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516: evidence of gene reduction in an emerging pathogen." Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M., Worsham P., Chu M.C., Andersen G.L. J. Bacteriol. 188:4453-4463(2006) [PubMed: 16740952] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000305 Genomic DNA. Translation: ABG17058.1.
PIR	AI0408.
RefSeq	YP_646658.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4123560.
GenomeReviews	Gene locus YPN_0726 in contig CP000305_GR.
KEGG	ypn:YPN_0726.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1CLS2.
Enzyme and pathway databases
BioCyc	YPES377628:YPN_0726-MON.
Family and domain databases
HAMAP	MF_01646. [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]
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	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

CYSG1_YERPN

Accession

Primary (citable) accession number: Q1CLS2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	July 11, 2006
Last modified:	November 25, 2008
This is version 25 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)