Reviewed, UniProtKB/Swiss-Prot Q820Q4 (CYSG_NITEU)

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:	NE0532

Organism

Nitrosomonas europaea [Complete proteome] [HAMAP]

Taxonomic identifier

915 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Nitrosomonadales › Nitrosomonadaceae › Nitrosomonas

Protein attributes

Sequence length	475 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 – 475	475	Siroheme synthase		PRO_0000330526
Regions
	Region	220 – 462	243	Uroporphyrinogen-III C-methyltransferase

Sequences

	Sequence		Length	Mass (Da)
	Q820Q4-1 [UniParc]. Last modified April 29, 2008. Version 2. Checksum: 9F4AC3F7723AD9A5	FASTA	475	52,234
	10 20 30 40 50 60 MDYLPVFLNI KQRDCLVVGG GEIAVRKIRL LLRAHARIHV VSPAISEELS NLLLQSPVIT 70 80 90 100 110 120 HTAESFRPDH LQDRALAIAA TNDHEVNRAV SAAARKAGIP VNVVDNPDLC TFIMPSILDR 130 140 150 160 170 180 SPIIVAVSSG GTSPILARLL RSRLEALIPS AYGRLAEYAA RFRDKVRQRF IHQENRRFFW 190 200 210 220 230 240 ERMLQGPFAE MVFAGRDQAA QDYLSEALEN STDQFPTGEV YLVGAGPGDP DLLTFRAMRL 250 260 270 280 290 300 MQQADVVIYD RLVSPAILDM VRQDATRIYV GKVRNQHTLP QTSINELLVK LAQEGKHVLR 310 320 330 340 350 360 LKGGDPFIFG RGGEEIETLS QHHIPFQVVP GITAASGVAS YAGIPLTHRD HAQSCVFVTG 370 380 390 400 410 420 HLKDNTIQLD WPALARPNQT IVVYMGLLGV TELCRQLIAH GLQATTPAAI VQQGTTPNQR 430 440 450 460 470 VLTGTLETLP DIIQQNPLKP PTLIIVGNVV KLHQKLAWFN STSEPMGTSS GPGYP

References

[1]

"Complete genome sequence of the ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaea." Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J. J. Bacteriol. 185:2759-2773(2003) [PubMed: 12700255] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 19718 / IFO 14298.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL954747 Genomic DNA. Translation: CAD84443.1. Different initiation.
RefSeq	NP_840617.1.
3D structure databases
HSSP	HSSP built from PDB template 1PJT based on UniProtKB P25924.
ModBase	Search...
Genome annotation databases
GeneID	1081471.
GenomeReviews	Gene locus NE0532 in contig AL954747_GR.
KEGG	neu:NE0532.
NMPDR	fig|228410.1.peg.516.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q820Q4.
Enzyme and pathway databases
BioCyc	NEUR228410:NE0532-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_NITEU

Accession

Primary (citable) accession number: Q820Q4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	April 29, 2008
Last modified:	November 25, 2008
This is version 32 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)