Reviewed, UniProtKB/Swiss-Prot A6V4H6 (CYSG_PSEA7)

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:	PSPA7_2597

Organism

Pseudomonas aeruginosa (strain PA7) [Complete proteome] [HAMAP]

Taxonomic identifier

381754 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	465 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 – 465	465	Siroheme synthase HAMAP MF_01646		PRO_0000330534
Regions
	Region	219 – 461	243	Uroporphyrinogen-III C-methyltransferase HAMAP MF_01646

Sequences

	Sequence		Length	Mass (Da)
	A6V4H6-1 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: DB1540256BB2D0B3	FASTA	465	50,297
	10 20 30 40 50 60 MDFLPLFHSL QGRLALVVGG GEVALRKARL LADAGARLRV VAPQIHIELR HLVEQGGGEL 70 80 90 100 110 120 LERDYQDGDQ PGCALIIAAT DDEPLNAEVS RAANARGIPV NVVDAPALCS VIFPAIVDRS 130 140 150 160 170 180 PLVVAVSSGG DAPVLARLIR AKLETWIPSS YGQLAGLASR FRNRVKELLP DLQQRRVFWE 190 200 210 220 230 240 NLFQGEIAER VLAGRPAEAE RLLEERLAGG LAHMATGEVY LVGAGPGDPD LLTFRALRLM 250 260 270 280 290 300 QQADVVLYDR LVAPAILELC RRDAERLYVG KRRAEHAVPQ ERINRLLVEL ASQGKRVLRL 310 320 330 340 350 360 KGGDPFIFGR GGEEIDELAA HGIPFQVVPG ITAASGCAAY AGIPLTHRDH AQSVRFVTGH 370 380 390 400 410 420 LKDGTTDLPW KDLVAPGQTL VFYMGLVGLP VICEQLVAHG RSAQTPAALI QQGTTAQQRV 430 440 450 460 FSGTLENLPQ LVAEHEVHAP TLVIVGEVVQ LRDKLAWFEG AREGA

References

[1]	Dodson R.J., Harkins D., Paulsen I.T. Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000744 Genomic DNA. Translation: ABR83518.1.
RefSeq	YP_001347961.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5356325.
GenomeReviews	Gene locus PSPA7_2597 in contig CP000744_GR.
KEGG	pap:PSPA7_2597.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	A6V4H6. TTVVYMP.
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_PSEA7

Accession

Primary (citable) accession number: A6V4H6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	August 21, 2007
Last modified:	June 16, 2009
This is version 17 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)