Reviewed, UniProtKB/Swiss-Prot P95370 (CYSG_NEIMB)

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:	cysG1
Ordered Locus Names:	NMB1156
AND
Name:	cysG2
Ordered Locus Names:	NMB1194

Organism

Neisseria meningitidis serogroup B [Complete proteome] [HAMAP]

Taxonomic identifier

491 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	483 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 – 483	483	Siroheme synthase		PRO_0000150382
Regions
	Region	219 – 459	241	Uroporphyrinogen-III C-methyltransferase
Experimental info
	Sequence conflict	475 – 483	9	GLNAGQRAA → D in CAA71251. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P95370-1 [UniParc]. Last modified December 1, 2000. Version 3. Checksum: 279C4F458B19582F	FASTA	483	52,111
	10 20 30 40 50 60 MNYFPIFANL AGRPVLVVGG GAVAARKISL LLKAGAEVRV AAKHLNAELS ALAAENKILW 70 80 90 100 110 120 LAEEFRAEHI RTVFLIIAAS SDQALNRRVF HLAESCQKPV NVVDDRDHCS FIFPSVIDRN 130 140 150 160 170 180 PVQIAVSSSG SAPVLARLLR ERLEALLPPS LGDMAEISGR WRDAVKGKLK SVTERRRFWE 190 200 210 220 230 240 KQFNGRFAAL VKNRQNTLAE RELAGQLEQS RQNDQGGSVS LVGAGPGDAG LLTLKGLQEI 250 260 270 280 290 300 QQADVVLYDA LVSDGILSLV RRDAERIFVG KRARGERTPQ EDTNALMVRL AREGRRVVRL 310 320 330 340 350 360 KGGDPFVFGR GGEELETLAR HQIPFSVVPG ITAAVGATAY AGIPLTHRDY AQSAVFVTGH 370 380 390 400 410 420 RKADAPDIEW QTLARSRQTL VIYMGALKAA LIAERLQQHG RSPDTPAAVI SQGTLPAQKT 430 440 450 460 470 480 ATGTLANLAE LAETAPNPAL IVIGEVVGLH EKLAWFGENG EGENRVGQTY PALGGLNAGQ RAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sirohaem synthase from Neisseria meningitidis." McVeigh T., Wilkie S.E., Woodcock S.C., Mortuza G., Peters S.E., Warren M.J. Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: MC58 / Serogroup B.
[2]	"Complete genome sequence of Neisseria meningitidis serogroup B strain MC58." Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., White O. , Fleischmann R.D., Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C. Science 287:1809-1815(2000) [PubMed: 10710307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MC58 / Serogroup B.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y10177 Genomic DNA. Translation: CAA71251.1. AE002098 Genomic DNA. Translation: AAF41542.1. AE002098 Genomic DNA. Translation: AAF41577.1.
PIR	D81111. T46867.
RefSeq	NP_274184.1. NP_274220.1.
3D structure databases
HSSP	HSSP built from PDB template 1CBF based on UniProtKB O87696.
ModBase	Search...
Genome annotation databases
GeneID	903577. 903614.
GenomeReviews	Gene locus NMB1156 in contig AE002098_GR. Gene locus NMB1194 in contig AE002098_GR.
KEGG	nme:NMB1156. nme:NMB1194.
TIGR	NMB1156. NMB1194.
Phylogenomic databases
HOGENOM	P95370.
Enzyme and pathway databases
BioCyc	NMEN122586:NMB_1156-MON. NMEN122586:NMB_1194-MON.
Family and domain databases
HAMAP	MF_01646. [Tree]
InterPro	IPR000878. 4pyrrol_Mease. IPR006366. CobA_cysG_C. IPR006367. CysG_synth_N. IPR003043. Uropor_MeTrfase_CS. [Graphical view]
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

CYSG_NEIMB

Accession

Primary (citable) accession number: P95370
Secondary accession number(s): Q9JQK6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	December 1, 2000
Last modified:	November 25, 2008
This is version 70 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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