Reviewed, UniProtKB/Swiss-Prot Q65T49 (CYSG_MANSM)

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:	MS1254

Organism

Mannheimia succiniciproducens (strain MBEL55E) [Complete proteome] [HAMAP]

Taxonomic identifier

221988 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Mannheimia

Protein attributes

Sequence length	476 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 – 476	476	Siroheme synthase		PRO_0000330520
Regions
	Region	216 – 456	241	Uroporphyrinogen-III C-methyltransferase

Sequences

	Sequence		Length	Mass (Da)
	Q65T49-1 [UniParc]. Last modified April 29, 2008. Version 2. Checksum: 7A4219457822899E	FASTA	476	52,268
	10 20 30 40 50 60 MNYFPVFADL NNRPVLVVGG GTIAARKVNL LLKANAEVRI TAQKLNAELT ALVEQDRIIW 70 80 90 100 110 120 IAKEFHGEQI RNVFLVVAAT DDEQLNEQVF QVAESRQKLV NVVDDQARCS FIFPSIIDRS 130 140 150 160 170 180 PIQVAVSSGG AAPVLARLLR EKLEALLPQH LGVMADISGK WRHKVKQQLK TITERRRFWE 190 200 210 220 230 240 SLFNGRFSRL LKNRQIEAAK KELELQLTKD YQGGSVSLVG AGPGDAGLLT LKGLQEIQQA 250 260 270 280 290 300 DVVLYDALVS AEILDLVRRD AELIFVGKRA QGRQVAQQET NQLLADLALQ GKRVVRLKGG 310 320 330 340 350 360 DPFVFGRGGE ELEVLAQQGI PFSVVPGITA AIGATAYAGI PLTHRDYAQS AVFVTGHRKA 370 380 390 400 410 420 DASDIEWQTL ARSNQTLVIY MGTLKAATIA QSLQQYGRAA STPVAVISQG TQETQHTQIG 430 440 450 460 470 TLKNLAELAE KAPTPALIVV GEVVSLHEKL AWFGEDKFAQ KRPHFTLDSL RIERVA

References

[1]

"The genome sequence of the capnophilic rumen bacterium Mannheimia succiniciproducens." Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H., Jeong H., Hur C.G., Kim J.J. Nat. Biotechnol. 22:1275-1281(2004) [PubMed: 15378067] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016827 Genomic DNA. Translation: AAU37861.1. Different initiation.
RefSeq	YP_088446.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3076502.
GenomeReviews	Gene locus MS1254 in contig AE016827_GR.
KEGG	msu:MS1254.
NMPDR	fig|221988.1.peg.1175.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q65T49.
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

CYSG_MANSM

Accession

Primary (citable) accession number: Q65T49

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	April 29, 2008
Last modified:	November 25, 2008
This is version 30 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)