Reviewed, UniProtKB/Swiss-Prot P57500 (CYSG_BUCAI)

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:	BU425

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum symbiotic bacterium) [Complete proteome] [HAMAP]

Taxonomic identifier

118099 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	473 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 – 473	473	Siroheme synthase		PRO_0000150377
Regions
	Region	217 – 457	241	Uroporphyrinogen-III C-methyltransferase

Sequences

	Sequence		Length	Mass (Da)
	P57500-1 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: 4B5781BC2AA565BA	FASTA	473	52,874
	10 20 30 40 50 60 MNYLPIFIDL KSKNVLVIGA GEVGLNKIRI LLRAKAKVNV IAKELCSEVK LLLRDQKINW 70 80 90 100 110 120 LSKNFDLIYL NKIFLVVSAT NDIKLNQYIF KKCNERCVLV NIVDDKLKCS FIFPSIIDRS 130 140 150 160 170 180 PLIVAISSGG TAPVLLRLLR EKIEAILPNK LGDVAKIAGK WRLAIKKHFS NFLERRKFWE 190 200 210 220 230 240 KLFHSIFVEH ILNGNKEQAI NVLKKNMNQN ISLTGEIILV GAGPGDSGLL TLRGLQVLQQ 250 260 270 280 290 300 ADVVLYDYLV SEDILDLIRR DAKRICVGKR VGLKNITQNE IIKLLIFFAQ KGKKVVRLKG 310 320 330 340 350 360 GDPFIFGRGS EEIEAAKDAG IHFQVVPGIT SAIGIAAYTG IPLTHRKYSQ GVIFITGHKC 370 380 390 400 410 420 IDGFLNNWSI LSDPSYTLVV YMGTLKAVYI AQKLITFGRS KLTPIAIIVQ GTTIHQKVIV 430 440 450 460 470 GCLGEIEKII PFAATPSLLI IGDVVHLHKK LAWFQSENIL KKIKNKFSTL TFI

References

[1]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed: 10993077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tokyo 1998.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000003 Genomic DNA. Translation: BAB13123.1.
RefSeq	NP_240237.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1109773.
GenomeReviews	Gene locus BU425 in contig BA000003_GR.
KEGG	buc:BU425.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P57500.
Enzyme and pathway databases
BioCyc	BSP107806:BU425-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. 1 hit. PS00840. SUMT_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CYSG_BUCAI

Accession

Primary (citable) accession number: P57500

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	November 25, 2008
This is version 50 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)