Reviewed, UniProtKB/Swiss-Prot Q3JCS0 (CYSG_NITOC)

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:	Noc_0863

Organism

Nitrosococcus oceani (strain ATCC 19707 / NCIMB 11848) [Complete proteome] [HAMAP]

Taxonomic identifier

323261 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Chromatiaceae › Nitrosococcus

Protein attributes

Sequence length	468 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 – 468	468	Siroheme synthase		PRO_0000330525
Regions
	Region	218 – 460	243	Uroporphyrinogen-III C-methyltransferase

Sequences

	Sequence		Length	Mass (Da)
	Q3JCS0-1 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: 3D2650A5EDC9433E	FASTA	468	51,081
	10 20 30 40 50 60 MQYLPIFLNI RGQQCLVVGG GTVAVRKVAL LRQAGAEVKV IAPKLHEQLQ EWADKGKITA 70 80 90 100 110 120 QQASFSETEI KSCYLVIAAT DDSSLNEQVY HLATAQGVLV NVADCPRFCD FILPSIVDRS 130 140 150 160 170 180 PVIVAVSSGG ASPVLARLLR ARLETLIPQA YGRLGQFAAR YRSRIKQRIT GIRARRIFWE 190 200 210 220 230 240 KVLQGSIAER IFAGQEEEAE GALEAALEGG FVPEQGEVYL VGAGPGDPDL LTFRALRLMQ 250 260 270 280 290 300 QADVVFHDRL VSPEVLALVR REAERIYVGK KRSWHAVRQE EINMMLVRSA REGKRVLRLK 310 320 330 340 350 360 GGDPFIFGRG GEEIATLAAE NIPFQVVPGI TAASGCASYA GIPLTHRDHA HACIFVTGQL 370 380 390 400 410 420 KEGRLSLNWQ ALVQPQQTIV VYMGLSGLEI LCQELIAHGM PAVTPAALVQ QGTTSRQRVL 430 440 450 460 TGTLATLPDI VQGEDIHAPT LVIIGGVVAL YPQLAWFKVP DREPLDAR

References

[1]

"Complete genome sequence of the marine, chemolithoautotrophic, ammonia-oxidizing bacterium Nitrosococcus oceani ATCC 19707." Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J., Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T., Vergez L.M., Ward B.B. Appl. Environ. Microbiol. 72:6299-6315(2006) [PubMed: 16957257] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000127 Genomic DNA. Translation: ABA57376.1.
RefSeq	YP_342906.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3707168.
GenomeReviews	Gene locus Noc_0863 in contig CP000127_GR.
KEGG	noc:Noc_0863.
NMPDR	fig|323261.3.peg.917.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q3JCS0.
Enzyme and pathway databases
BioCyc	NOCE323261:NOC_0863-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. 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. False negative. PS00840. SUMT_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYSG_NITOC

Accession

Primary (citable) accession number: Q3JCS0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	November 8, 2005
Last modified:	November 25, 2008
This is version 24 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)