Reviewed, UniProtKB/Swiss-Prot A6TF07 (CYSG2_KLEP7)

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:	KPN78578_37170
ORF Names:	KPN_03754

Organism

Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) [Complete proteome] [HAMAP]

Taxonomic identifier

272620 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Klebsiella

Protein attributes

Sequence length	457 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 – 457	457	Siroheme synthase 2		PRO_0000330519
Regions
	Region	218 – 457	240	Uroporphyrinogen-III C-methyltransferase

Sequences

	Sequence		Length	Mass (Da)
	A6TF07-1 [UniParc]. Last modified April 29, 2008. Version 2. Checksum: A62522225BC5253E	FASTA	457	49,979
	10 20 30 40 50 60 MDHLPIFCQL RQRDCLLVGG GDVAERKARL LLDAGANVTV NALDFTPQFQ VWADSQMLTL 70 80 90 100 110 120 VQGEFIPSLL DNCWLAIAAT DDETVNQQVS EAAEARRIFC NVVDAPRQAS FIMPSIIDRS 130 140 150 160 170 180 PLMVAVSSGG TSPVLARLLR EKLESILPLH LGQLARYAGH LRARVKQQFA TVGERRRFWE 190 200 210 220 230 240 KLFVNDRLAQ SLANDDRQAV ADTTEQLLTE PLEHRGEVVL VGAGPGDAGL LTLKGLQQIQ 250 260 270 280 290 300 QADVVVYDRL VSDDIMNLVR RDADRVFVGK RSGYHCVPQE EINQILLREA QKGRRVVRLK 310 320 330 340 350 360 GGDPFIFGRG GEELETLCEA GIPFSVVPGI TAASGCSAYS GIPLTHRDFA QGVRLVTGHL 370 380 390 400 410 420 KTGGELDWAN LAVEKQTLVF YMGLNQAPAI REKLIAHGMA EDMPAAIVEN GTAVTQKVVS 430 440 450 GTLGQLDILA QQMASPALII VGRVVGLRDK LNWFSNH

References

[1]	McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P., Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K. Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000647 Genomic DNA. Translation: ABR79141.1. Different initiation.
RefSeq	YP_001337408.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5341883.
GenomeReviews	Gene locus KPN78578_37170 in contig CP000647_GR.
KEGG	kpn:KPN_03754.
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_KLEP7

Accession

Primary (citable) accession number: A6TF07

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	April 29, 2008
Last modified:	November 25, 2008
This is version 15 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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