Reviewed, UniProtKB/Swiss-Prot A7FNS9 (CYSG2_YERP3)

Names and origin

Protein names

Recommended name:
    Siroheme synthase 2
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:	cysG2
Ordered Locus Names:	YpsIP31758_3959

Organism

Yersinia pseudotuberculosis serotype O:1b (strain IP 31758) [Complete proteome] [HAMAP]

Taxonomic identifier

349747 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia

Protein attributes

Sequence length	473 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 – 473	473	Siroheme synthase 2		PRO_0000330581
Regions
	Region	218 – 457	240	Uroporphyrinogen-III C-methyltransferase

Sequences

	Sequence		Length	Mass (Da)
	A7FNS9-1 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: 3A220E0A0E63E7FA	FASTA	473	51,918
	10 20 30 40 50 60 MDYFPIFCQL QHKACLLVGG GEIAERKARL LLDAGALVTV NACEFTPQFH HWADQGQLSL 70 80 90 100 110 120 ISGEFVPELL ADKWLVIAAT DQLSVNALVY QSANQQRIFC NVVDDPKRTS FIMPSIIDRS 130 140 150 160 170 180 PIMIAVSSGG KAPVLARLLR EKLEALLPQH LGQLAQLAGN LRQRVKQHFA AMTERRRFWE 190 200 210 220 230 240 KLLTHDRLAQ SLANNDHVQA DQHVEQLFSA PLTDRGEVVL VGAGPGDAGL LTLKGLQQIQ 250 260 270 280 290 300 QADVVVYDRL VSDEVMNLVR RDAERIFVGK QSGHHCVPQE QINQILLQQA QSGKRVVRLK 310 320 330 340 350 360 GGDPFIFGRG GEELEELAGY GIPFSVVPGI TAASGCSAYS GIPLTHRDHA QSVRLVTGHA 370 380 390 400 410 420 KKEGQLDWAN LAAEKQTLVF YMGLSQAGEI QQQLIQHGMP ATTQVALVEN GTSRHQRVVS 430 440 450 460 470 GELSQLALLS QQVSSPSLII VGSVVSLREK LNWFSSRHHD DQPKVTECVA HVG

References

[1]

"The complete genome sequence of Yersinia pseudotuberculosis IP31758, the causative agent of Far East scarlet-like fever." Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G., Fayolle C., Lindler L.E., Carniel E., Ravel J. PLoS Genet. 3:1508-1523(2007) [PubMed: 17784789] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000720 Genomic DNA. Translation: ABS46625.1.
RefSeq	YP_001402907.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5384901.
GenomeReviews	Gene locus YpsIP31758_3959 in contig CP000720_GR.
KEGG	ypi:YpsIP31758_3959.
Organism-specific databases
CMR	Search...
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

CYSG2_YERP3

Accession

Primary (citable) accession number: A7FNS9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	September 11, 2007
Last modified:	November 25, 2008
This is version 14 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)