Reviewed, UniProtKB/Swiss-Prot A1AVU5 (CYSG_RUTMC)

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:	Rmag_0270

Organism

Ruthia magnifica subsp. Calyptogena magnifica [Complete proteome] [HAMAP]

Taxonomic identifier

413404 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › sulfur-oxidizing symbionts

Protein attributes

Sequence length	472 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Multifunctional enzyme that catalyzes 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 consists 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. HAMAP MF_01646 S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2. HAMAP MF_01646 Precorrin-2 + NAD+ = sirohydrochlorin + NADH. HAMAP MF_01646 Siroheme + 2 H+ = sirohydrochlorin + Fe2+. HAMAP MF_01646
Pathway	Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. HAMAP MF_01646 Cofactor biosynthesis; adenosylcobalamin biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. Porphyrin metabolism; siroheme biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. HAMAP MF_01646 Porphyrin metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1. HAMAP MF_01646 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 – 472	472	Siroheme synthase HAMAP MF_01646		PRO_0000330550
Regions
	Region	218 – 460	243	Uroporphyrinogen-III C-methyltransferase HAMAP MF_01646

Sequences

	Sequence		Length	Mass (Da)
	A1AVU5-1 [UniParc]. Last modified January 23, 2007. Version 1. Checksum: 652623FA74F2E4AA	FASTA	472	52,011
	10 20 30 40 50 60 MNYLPIFIDI KQKPCLVVGG GDIAYRKINF LLKAHGQVTC IAKSSCKNVV KLASDNKIIY 70 80 90 100 110 120 FEKSFEASDI KEQVLIVSAT DNTSLNKQVS ELSNQNNIPV NVVDSPDLCT FIMPSIVDRS 130 140 150 160 170 180 PIVIAISSAG KAPVLARLIR AKLESTLPHA YGKLAELAGN FRDKVKEKFS NIEDRRYFWE 190 200 210 220 230 240 KTFSGIIAEK VFSGKIQEAK ADLQVQLDGS TKTQVGEVYL VGGGPGDPDL LTFKALRLMQ 250 260 270 280 290 300 QADVVLYDRL VSNGVMGLVR RDAQLIYVGK ERDNHVVPQG DINQLLVNLA KQGRRVCRLK 310 320 330 340 350 360 GGDPFIFGRG GEEIETLAEN GISFQVVPGI TAASGCSTYS GIPLTHRDYS QSCRFVTGHL 370 380 390 400 410 420 KDGSMNLPWH ELSVEQQTIV FYMALNGARH LSEQLITHGM SPDMPVALVE KGTTPEQKVY 430 440 450 460 470 TTTLKKLPDL VKNEIIHAPT LIIIGEVVTL REKLNWFDAK LASSKKSYLF GG

References

[1]

"The Calyptogena magnifica chemoautotrophic symbiont genome." Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J., Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M., Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M. Science 315:998-1000(2007) [PubMed: 17303757] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000488 Genomic DNA. Translation: ABL02052.1.
RefSeq	YP_903523.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4555165.
GenomeReviews	Gene locus Rmag_0270 in contig CP000488_GR.
KEGG	rma:Rmag_0270.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	A1AVU5. WHELSVE.
Family and domain databases
HAMAP	MF_01646. [Tree]
InterPro	IPR000878. 4pyrrol_Mease. IPR014777. 4pyrrole_Mease_sub1. IPR014776. 4pyrrole_Mease_sub2. IPR006366. CobA_cysG_C. IPR016040. NAD(P)-bd_dom. IPR019478. Sirohaem_synthase_dimer_dom. IPR006367. Sirohaem_synthase_N. 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	PF10414. CysG_dimeriser. 1 hit. 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_RUTMC

Accession

Primary (citable) accession number: A1AVU5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 23 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)