Reviewed, UniProtKB/Swiss-Prot A9LZ77 (CYSG_NEIM0)

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:	NMCC_1074

Organism

Neisseria meningitidis serogroup C (strain 053442) [Complete proteome] [HAMAP]

Taxonomic identifier

374833 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	480 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 – 480	480	Siroheme synthase		PRO_0000330523
Regions
	Region	216 – 456	241	Uroporphyrinogen-III C-methyltransferase

Sequences

	Sequence		Length	Mass (Da)
	A9LZ77-1 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: EAD97FA6BA13CBAF	FASTA	480	51,867
	10 20 30 40 50 60 MNYFPIFANL AGRPVLVVGG GSVAARKISL LLDAGAQVRV VANQLNAELS ALAAENKILW 70 80 90 100 110 120 LAEEFRAEHI RTVFLIIAAS SDQALNRRVF QLAESCQKPV NVVDDRDYCS FIFPSIINRN 130 140 150 160 170 180 PIQIAVSSSG SAPVLARLLR EKLEALLPHS LGDMAEISGR WRDAVKAKLK SVTERRRFWE 190 200 210 220 230 240 KQFNGRFAAL VKNQQTAQAE QELAKQLEQN YQGGFVSLVG AGPGDAGLLT LKGLQEIQQA 250 260 270 280 290 300 DVVLYDALVS DGILSLVRRD AERIFVGKRA RGDRTPQEDT NALMVRLARE GRRVVRLKGG 310 320 330 340 350 360 DPFVFGRGGE ELETLARHQI PFSVVPGITA AVGATAYAGI PLTHRDYAQS AVFVTGHRKA 370 380 390 400 410 420 DAPDIEWQTL ARSRQTLVIY MGALKAALIA ERLQQHGRSP DTPAAVISQG TLPAQKTATG 430 440 450 460 470 480 TLANLAELAE TAPNPALIVI GEVVGLHEKL AWFGENGEGE NRVGQAYPAL GGLNAGQRAA

References

[1]

"Characterization of ST-4821 complex, a unique Neisseria meningitidis clone." Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z., Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z., Liang X., Xu J., Jin Q. Genomics 91:78-87(2008) [PubMed: 18031983] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000381 Genomic DNA. Translation: ABX73254.1.
RefSeq	YP_001599210.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5795216.
GenomeReviews	Gene locus NMCC_1074 in contig CP000381_GR.
KEGG	nmn:NMCC_1074.
Organism-specific databases
CMR	Search...
Family and domain databases
HAMAP	MF_01646. [Tree]
InterPro	IPR014777. 4pyrrole_Mease_sub1. IPR014776. 4pyrrole_Mease_sub2. IPR006366. CobA_cysG_C. IPR006367. CysG_synth_N. IPR016040. NAD(P)-bd. [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.
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_NEIM0

Accession

Primary (citable) accession number: A9LZ77

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	February 5, 2008
Last modified:	November 25, 2008
This is version 11 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)