Reviewed, UniProtKB/Swiss-Prot A6TD45 (CYSG1_KLEP7)

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:	KPN78578_30550
ORF Names:	KPN_03115

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	471 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 – 471	471	Siroheme synthase 1		PRO_0000330518
Regions
	Region	217 – 457	241	Uroporphyrinogen-III C-methyltransferase

Sequences

	Sequence		Length	Mass (Da)
	A6TD45-1 [UniParc]. Last modified April 29, 2008. Version 2. Checksum: 9C9883AF252ED47A	FASTA	471	50,986
	10 20 30 40 50 60 MDYLPLFAEL KQRPVLVIGG GEIAERKIKF LLRAQAQVQV VAETLSPALA DLAARQALSW 70 80 90 100 110 120 RATEFSDSLV DDVFLVIAAT EDDALNQRVF AAANARYRLV NVVDNQALCS FVFPSIVDRS 130 140 150 160 170 180 PLLVAISSSG KAPVLSRILR EKIEALLPTN LGRLAESASY WRNHLKTRLT TTEARRRFWE 190 200 210 220 230 240 RVFTGRFASL MVAGNSAEAE KALQDELDKP ERETGEIILV GAGPGDAGLL TLRGLQAIQQ 250 260 270 280 290 300 ADVVFHDHLV TQPVLELVRR DAELICVGKR AGEHSVPQHE TNQLLVEAAK AGKTVVRLKG 310 320 330 340 350 360 GDPFIFGRGA EELQAAAEAG IPFQVVPGVT AAAGATAYAG IPLTHRDYAQ SAVFVTGHYK 370 380 390 400 410 420 PDSAPFDWSL LAKSQQTLAI YMGTMKAAEI SAQLIAHGRD SDTPVAVISR GTRDDQQTIT 430 440 450 460 470 GTLQQLEHLA KDAPMPALLV VGEVVQLHQQ LAWFQHTSSA EGFNASVVNL A

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: ABR78516.1. Different initiation.
RefSeq	YP_001336746.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5341891.
GenomeReviews	Gene locus KPN78578_30550 in contig CP000647_GR.
KEGG	kpn:KPN_03115.
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

CYSG1_KLEP7

Accession

Primary (citable) accession number: A6TD45

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)