Reviewed, UniProtKB/Swiss-Prot A1SRP9 (CYSG_PSYIN)

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:	Ping_0298

Organism

Psychromonas ingrahamii (strain 37) [Complete proteome] [HAMAP]

Taxonomic identifier

357804 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Psychromonadaceae › Psychromonas

Protein attributes

Sequence length	472 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 – 472	472	Siroheme synthase HAMAP MF_01646		PRO_0000330549
Regions
	Region	217 – 457	241	Uroporphyrinogen-III C-methyltransferase HAMAP MF_01646

Sequences

	Sequence		Length	Mass (Da)
	A1SRP9-1 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: 1A044E05245FE4AA	FASTA	472	51,193
	10 20 30 40 50 60 MDYLPIFTKL ENRPCLVVGG GSIACRKIHL LLKAGADVTV CALEFNPSLL KQAANKELKI 70 80 90 100 110 120 LEQAFTEELL ENKWLVIAAT NKKQVNEHIA TAAHAKQLLV NVVGQADISS FILPSIVDRS 130 140 150 160 170 180 PLVVAISSGG KAPVLARLIR ERLETLLPMH LGRLAAISAQ FRHRVKEVIK VAPLRRRYWE 190 200 210 220 230 240 KLFGNGMLAN LLQKGQTEKA IALMETSLSE DITQGDVALV GAGPGDPSLL TLKALQLMQQ 250 260 270 280 290 300 ADVVLYDRLV SSDILDLVRR DADLISVGKA AGNHEVEQSR TNQMLVEFAR EGKKVVRLKG 310 320 330 340 350 360 GDSFIFGRGG EELEELVEAG IAFQVVPGIT AASGCSAYAG IPLTHRDFAQ SVTFVTGHRK 370 380 390 400 410 420 TDGEELNWQA LAAPNQTLVV YMGLIQSQEI QTQLLSHGRA PETPVALVNK GTTSDQHVVI 430 440 450 460 470 GQLSELEQLG GGLQGPTLMI IGEVVNLADK LAWYQSDNKP PLSRDPFLVN LA

References

[1]

"Complete sequence of Psychromonas ingrahamii 37." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. , Land M., Hauser L., Kyrpides N., Ivanova N., Staley J., Richardson P. Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000510 Genomic DNA. Translation: ABM02164.1.
RefSeq	YP_941763.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4623717.
GenomeReviews	Gene locus Ping_0298 in contig CP000510_GR.
KEGG	pin:Ping_0298.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	A1SRP9. DYAQSAV.
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_PSYIN

Accession

Primary (citable) accession number: A1SRP9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	February 6, 2007
Last modified:	June 16, 2009
This is version 24 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)