Reviewed, UniProtKB/Swiss-Prot Q6F8G6 (CYSG_ACIAD)

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:	ACIAD2934

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	457 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 – 457	457	Siroheme synthase HAMAP MF_01646		PRO_0000330484
Regions
	Region	218 – 457	240	Uroporphyrinogen-III C-methyltransferase HAMAP MF_01646

Sequences

	Sequence		Length	Mass (Da)
	Q6F8G6-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: F3076FEFEA6830A2	FASTA	457	50,431
	10 20 30 40 50 60 MEIFPISLKL QQQRCLIVGG GHIAYRKAIL LVKAGAILDI VAPDIDPQLM SLIEQSAGTA 70 80 90 100 110 120 YVKLFEDHDL DRVYRLVIAA TDNADVNKRV FEQAELRNLL VNSVDDIPNC RFMVPAIIDR 130 140 150 160 170 180 SPLLISVASN GASPVLSRQL RTQIETLVPH GMGKLAEFSG QWRSRVKAQI TNPDERRIFW 190 200 210 220 230 240 EELYASPLKE QVFNDNLDIA NQMMTQSLAE WTAPKGEVYL VGAGPGDPEL LTLKALRLMQ 250 260 270 280 290 300 QADVVIYDRL VSAPILELCR RDAEKVYVGK ARSNHSVPQE GINALLVKYA QAGKRVCRLK 310 320 330 340 350 360 GGDPFIFGRG GEEIQELFAA GIPFQVVPGI TAASGCSAYA GIPLTHRDYA QSVRFLTGHL 370 380 390 400 410 420 KEGSPELPWS ELVYENQTLV LYMGLVGLEH ICQQLIAHGQ RPDMPVALVS KGTTPEQKVV 430 440 450 VGTLSNIASK IAEYQIHAPT LTIIGEVVSL REQLQWL

References

[1]

"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium." Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C. Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR543861 Genomic DNA. Translation: CAG69649.1.
RefSeq	YP_047471.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2878421.
GenomeReviews	Gene locus ACIAD2934 in contig CR543861_GR.
KEGG	aci:ACIAD2934.
NMPDR	fig|62977.3.peg.2664.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6F8G6.
OMA	Q6F8G6. MCRRDAE.
Enzyme and pathway databases
BioCyc	ASP62977:ACIAD2934-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. 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. 1 hit. PS00840. SUMT_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYSG_ACIAD

Accession

Primary (citable) accession number: Q6F8G6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	July 19, 2004
Last modified:	June 16, 2009
This is version 37 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)