Reviewed, UniProtKB/Swiss-Prot A9H259 (CYSG_GLUDA)

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:	GDI0165

Organism

Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / PAl5) [Complete proteome] [HAMAP]

Taxonomic identifier

272568 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Gluconacetobacter

Protein attributes

Sequence length	470 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 – 470	470	Siroheme synthase		PRO_0000330513
Regions
	Region	226 – 465	240	Uroporphyrinogen-III C-methyltransferase

Sequences

	Sequence		Length	Mass (Da)
	A9H259-1 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 70D8FF743EA97B96	FASTA	470	50,124
	10 20 30 40 50 60 MSDATDPGWF PLALRLRGAR VVVVGGGGIA LNKVRLLLAH AARIDILAPR LEDTLAAWQA 70 80 90 100 110 120 EGRITHIAGE ATPDRVRALL PGSRLVYAAT DDRAVNRAVA AQADALNIPV CAVDDPEPSS 130 140 150 160 170 180 FITPAQIHRG PVRIAISTGG AAPVLARRLR ERIEAVMPAG LDALARFLQA ERAHVVAACP 190 200 210 220 230 240 DIGRRRRVWE DFLDGPGGEA AQRGEHAAAR QVLDHLLAGA QTGGEVWLVG AGPGDPDLLT 250 260 270 280 290 300 LRALHLMQNA DSVLYDQLLP PALMDRVRRD AERVFVGKQR DRHTMPQDDI NAELIRRARA 310 320 330 340 350 360 GERVLRLKGG DPFIFGRGGE EIEALMAAGI PFQVVPGITA ASGCAAYAGI PLTHRDCAQS 370 380 390 400 410 420 CLFVTGHARR DGTLDLPWDS MARPGQTIAI YMGVTALPDL CTMLVRHGLP PDWPAAVVER 430 440 450 460 470 GTRPDQRVLT GTLADLPALA RAHAVGSPAL VLVGQVVRHR VVTPPPLSGT

References

[1]	"Gluconacetobacter diazotrophicus Pal5 complete genome." Bertalan M., Baldani I.J., Ferreira P. Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM889285 Genomic DNA. Translation: CAP54108.1.
RefSeq	YP_001600455.1. YP_002276605.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5788693. 6975664.
GenomeReviews	Gene locus GDI0165 in contig AM889285_GR.
KEGG	gdi:GDI0165.
Organism-specific databases
CMR	Search...
Family and domain databases
HAMAP	MF_01646. [Tree]
InterPro	IPR014777. 4pyrrole_Mease_sub1. IPR014776. 4pyrrole_Mease_sub2. IPR006366. CobA_cysG_C. IPR006367. CysG_synth_N. IPR016040. NAD(P)-bd. [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.
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_GLUDA

Accession

Primary (citable) accession number: A9H259

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	February 5, 2008
Last modified:	November 25, 2008
This is version 11 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)