Reviewed, UniProtKB/Swiss-Prot P0AEA8 (CYSG_ECOLI)

Names and origin

Protein names

Recommended name:
    Siroheme synthase
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:	cysG
Ordered Locus Names:	b3368, JW3331

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	457 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Multifunctional enzyme that catalyzes 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 consists of the NAD-dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme. Ref.5 Ref.6 Ref.7
Catalytic activity	S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1. HAMAP MF_01646 S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2. HAMAP MF_01646 Precorrin-2 + NAD+ = sirohydrochlorin + NADH. HAMAP MF_01646 Siroheme + 2 H+ = sirohydrochlorin + Fe2+. HAMAP MF_01646
Pathway	Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. HAMAP MF_01646 Cofactor biosynthesis; adenosylcobalamin biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. Porphyrin metabolism; siroheme biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. HAMAP MF_01646 Porphyrin metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1. HAMAP MF_01646 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 Direct protein sequencing 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	precorrin-2 dehydrogenase activity Inferred from electronic annotation. Source: HAMAP protein binding Inferred from physical interaction. Source: IntAct sirohydrochlorin ferrochelatase activity Inferred from electronic annotation. Source: EC uroporphyrin-III C-methyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
nadE	P18843	1	EBI-1132623,EBI-548960

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 457	457	Siroheme synthase HAMAP MF_01646		PRO_0000150378
Regions
	Region	218 – 457	240	Uroporphyrinogen-III C-methyltransferase HAMAP MF_01646
Experimental info
	Sequence conflict	26	1	R → P Ref.1
	Sequence conflict	26	1	R → P Ref.2
	Sequence conflict	90 – 91	2	SE → RQ Ref.1
	Sequence conflict	90 – 91	2	SE → RQ Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P0AEA8-1 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: DDDE0DC90C5CF2F4	FASTA	457	49,951
	10 20 30 40 50 60 MDHLPIFCQL RDRDCLIVGG GDVAERKARL LLDAGARLTV NALAFIPQFT AWADAGMLTL 70 80 90 100 110 120 VEGPFDESLL DTCWLAIAAT DDDALNQRVS EAAEARRIFC NVVDAPKAAS FIMPSIIDRS 130 140 150 160 170 180 PLMVAVSSGG TSPVLARLLR EKLESLLPLH LGQVAKYAGQ LRGRVKQQFA TMGERRRFWE 190 200 210 220 230 240 KLFVNDRLAQ SLANNDQKAI TETTEQLINE PLDHRGEVVL VGAGPGDAGL LTLKGLQQIQ 250 260 270 280 290 300 QADVVVYDRL VSDDIMNLVR RDADRVFVGK RAGYHCVPQE EINQILLREA QKGKRVVRLK 310 320 330 340 350 360 GGDPFIFGRG GEELETLCNA GIPFSVVPGI TAASGCSAYS GIPLTHRDYA QSVRLITGHL 370 380 390 400 410 420 KTGGELDWEN LAAEKQTLVF YMGLNQAATI QQKLIEHGMP GEMPVAIVEN GTAVTQRVID 430 440 450 GTLTQLGELA QQMNSPSLII IGRVVGLRDK LNWFSNH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of binding sequences for the Escherichia coli transcription activators, FNR and CRP: location of bases involved in discrimination between FNR and CRP." Bell A.I., Gaston K.L., Cole J.A., Busby S.J.W. Nucleic Acids Res. 17:3865-3874(1989) [PubMed: 2543955] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Nucleotide sequence, organisation and structural analysis of the products of genes in the nirB-cysG region of the Escherichia coli K-12 chromosome." Peakman T., Crouzet J., Mayaux J.F., Busby S.J.W., Mohan S., Harborne N., Wootton J., Nicolson R., Cole J.A. Eur. J. Biochem. 191:315-323(1990) [PubMed: 2200672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Enzymatic synthesis of dihydrosirohydrochlorin (precorrin-2) and of a novel pyrrocorphin by uroporphyrinogen III methylase." Warren M.J., Stolowich N.J., Santander P.J., Roessner C.A., Sowa B.A., Scott A.I. FEBS Lett. 261:76-80(1990) [PubMed: 2407558] [Abstract] Cited for: FUNCTION, PROTEIN SEQUENCE OF 1-18.
[6]	"The Escherichia coli cysG gene encodes S-adenosylmethionine-dependent uroporphyrinogen III methylase." Warren M.J., Roessner C.A., Santander P.J., Scott A.I. Biochem. J. 265:725-729(1990) [PubMed: 2407234] [Abstract] Cited for: FUNCTION.
[7]	"The Escherichia coli cysG gene encodes the multifunctional protein, siroheme synthase." Spencer J.B., Stolowich N.J., Roessner C.A., Scott A.I. FEBS Lett. 335:57-60(1993) [PubMed: 8243665] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X14202 Genomic DNA. Translation: CAA32419.1. U18997 Genomic DNA. Translation: AAA58165.1. U00096 Genomic DNA. Translation: AAC76393.1. AP009048 Genomic DNA. Translation: BAE77922.1.
PIR	C65131.
RefSeq	AP_004421.1. NP_417827.1.
3D structure databases
HSSP	HSSP built from PDB template 1CBF based on UniProtKB O87696.
SMR	P0AEA8. Positions 1-457.
ModBase	Search...
Protein-protein interaction databases
IntAct	P0AEA8. 1 interaction.
Genome annotation databases
GeneID	947880.
GenomeReviews	Gene locus JW3331 in contig AP009048_GR. Gene locus b3368 in contig U00096_GR.
KEGG	ecj:JW3331. eco:b3368.
Organism-specific databases
EchoBASE	EB0185.
EcoGene	EG10188. cysG.
CMR	Search...
Phylogenomic databases
HOGENOM	P0AEA8.
OMA	P0AEA8. MCRRDAE.
Enzyme and pathway databases
BioCyc	EcoCyc:SIROHEMESYN-MON. MetaCyc:SIROHEMESYN-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. IPR016040. NAD(P)-bd_dom. IPR019478. Sirohaem_synthase_dimer_dom. IPR006367. Sirohaem_synthase_N. 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	PF10414. CysG_dimeriser. 1 hit. 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

CYSG_ECOLI

Accession

Primary (citable) accession number: P0AEA8
Secondary accession number(s): P11098, P76685, Q2M734

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2005
Last sequence update:	December 6, 2005
Last modified:	June 16, 2009
This is version 39 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)