Reviewed, UniProtKB/Swiss-Prot Q493N1 (CYSG_BLOPB)

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:	BPEN_166

Organism

Blochmannia pennsylvanicus (strain BPEN) [Complete proteome] [HAMAP]

Taxonomic identifier

291272 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › ant endosymbionts › Candidatus Blochmannia

Protein attributes

Sequence length	474 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 – 474	474	Siroheme synthase HAMAP MF_01646		PRO_0000330495
Regions
	Region	220 – 460	241	Uroporphyrinogen-III C-methyltransferase HAMAP MF_01646

Sequences

	Sequence		Length	Mass (Da)
	Q493N1-1 [UniParc]. Last modified September 13, 2005. Version 1. Checksum: F752193534C6FD69	FASTA	474	52,601
	10 20 30 40 50 60 MEYLPIFIDL KNRPVLVVGG GAVAARKIHM LQRATITIVA PALCTELKKV LIKQNISWIS 70 80 90 100 110 120 KNFQPIMLNK VILVIVATND SKLNTFIYQN AEKHNILINT VDDKNKCSFI FPAIIDRNPV 130 140 150 160 170 180 LIGISSCGKA PILVRILREK LELLLPKSLG FVAKLAGAWR NKVKQHIVDT VLRRQFWEKI 190 200 210 220 230 240 FYNGHVVTLM EKGRPKEANK VLNYALNNSV KNKNNKTGHV TLVGAGPGDI GLLTIRGLQV 250 260 270 280 290 300 IQQADIILYD YLVNSDILDL ARRDADKICV GKHVGNHSIS QKKLNQFIVQ LAQKGNKVVR 310 320 330 340 350 360 LKGGDPFIFG RGGEELQAIS EAGIAFQVVP GITAGIGVAA YSGIPLTHRK YAHSVVFITG 370 380 390 400 410 420 HNTNGDNQFN WNSLSNNQQT LVIYMGKINA ISIRNNLIIH GRNMHTPVAV ISRGTYQDQK 430 440 450 460 470 ILIGTLIELE KLTQMADHPA LLVIGDVVSL HSKINWFGQK ALHYYLINSI INLI

References

[1]	"Genome sequence of Blochmannia pennsylvanicus indicates parallel evolutionary trends among bacterial mutualists of insects." Degnan P.H., Lazarus A.B., Wernegreen J.J. Genome Res. 15:1023-1033(2005) [PubMed: 16077009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000016 Genomic DNA. Translation: AAZ40806.1.
RefSeq	YP_277679.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3563112.
GenomeReviews	Gene locus BPEN_166 in contig CP000016_GR.
KEGG	bpn:BPEN_166.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q493N1.
OMA	Q493N1. DYAQSAV.
Enzyme and pathway databases
BioCyc	CBLO291272:BPEN_166-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_BLOPB

Accession

Primary (citable) accession number: Q493N1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	September 13, 2005
Last modified:	June 16, 2009
This is version 27 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)