Reviewed, UniProtKB/Swiss-Prot A7MJ67 (CYSG1_ENTS8)

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:	ESA_00538

Organism

Enterobacter sakazakii (strain ATCC BAA-894) [Complete proteome] [HAMAP]

Taxonomic identifier

290339 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Cronobacter

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_0000330502
Regions
	Region	217 – 457	241	Uroporphyrinogen-III C-methyltransferase

Sequences

	Sequence		Length	Mass (Da)
	A7MJ67-1 [UniParc]. Last modified October 2, 2007. Version 1. Checksum: 28F682F12075C41B	FASTA	471	50,673
	10 20 30 40 50 60 MEYLPLFAQL KQRPVLVVGG GEVALRKIAL LRRAGACVSV VAKKLHPELA ALEQEGALRW 70 80 90 100 110 120 LAQSFEPAQL DAVFLVIAAT SDAALNRRVF DEANARQRLV NVVDDQPLCS FIFPSIVDRS 130 140 150 160 170 180 PLIVAISSSG NAPVLARLLR EKIESLLPAS LGRMAEVAGG FRDRIKARIP TTDGRRRFWE 190 200 210 220 230 240 KAFRGRFASL MAAGDTRAAE AVLEAELDAP QGPQGEIILV GAGPGDAGLL TLRGLQVMQQ 250 260 270 280 290 300 ADVVLYDHLV SDGVLDLVRR DADRICVGKR AGAHAVAQHE TNQMLIDFAR EGKTVVRLKG 310 320 330 340 350 360 GDPFIFGRGG EELEAAKAAG VPFQVVPGVT AASGATAYAG IPLTHRDYAQ SAVFVTGHYK 370 380 390 400 410 420 PDSEPFDWAL LAKSRQTLAI YMGTMKAAEI SQQLIAHGRD ATTPVAVISR GTREDQRVLT 430 440 450 460 470 GTLDTLNILA KDAPMPALLV VGEVVQLHQQ LAWFQHSTDA ENLRSSVVNL A

References

[1]	McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Fulton B., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R. Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000783 Genomic DNA. Translation: ABU75829.1.
RefSeq	YP_001436665.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5551809.
GenomeReviews	Gene locus ESA_00538 in contig CP000783_GR.
KEGG	esa:ESA_00538.
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_ENTS8

Accession

Primary (citable) accession number: A7MJ67

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	October 2, 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)