Reviewed, UniProtKB/Swiss-Prot Q3ILQ9 (CYSG_PSEHT)

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:	PSHAa0213

Organism

Pseudoalteromonas haloplanktis (strain TAC 125) [Complete proteome] [HAMAP]

Taxonomic identifier

326442 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Pseudoalteromonadaceae › Pseudoalteromonas

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_0000330532
Regions
	Region	217 – 459	243	Uroporphyrinogen-III C-methyltransferase

Sequences

	Sequence		Length	Mass (Da)
	Q3ILQ9-1 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: 64D87C039D7900D3	FASTA	473	51,809
	10 20 30 40 50 60 MQYLPIFTKL DNKPVLVVGG GDVALRKCSA LLKARASITL VAPKFCQQLI ELASENKVTL 70 80 90 100 110 120 IHEYFSEQHL KNMMLVIAAT DLEHVNSQVF ELANAHNIFV NVVDDQPKCT FIFPSIVDRN 130 140 150 160 170 180 PITIAISSAG TAPVLARRLR EKLETLIPQH IGPLATLVGG FRSKVKQRFK HFADRRQFWE 190 200 210 220 230 240 GVFDSSVVSK VQTGDTQAAE QQLEHMLNAK AEPEGEVYVV GAGPGDPELL TLKALQLMQQ 250 260 270 280 290 300 ADVVVYDYLV SDEIMELVRR DADLICVGKR LGDHSVAQQD TNQMLVDLAK QGKKVCRIKG 310 320 330 340 350 360 GDPFIYGRGG EEVQVLAANK VNYQIVPGIT AAAGCSAYAG IPLTHRDHAQ AIQFVTGHCK 370 380 390 400 410 420 KDGQELDWQS LAKPNQTLAI YMGVIKSPHI QAELLKHGRN ANTPVAIIEN GTRKNQRVIT 430 440 450 460 470 GKLGELADLI TRNSVVSPAL LIIGEVASLH QELHWFGAKA QTSSFAQPLT DVA

References

[1]

"Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125." Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N., Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C. , Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A. Genome Res. 15:1325-1335(2005) [PubMed: 16169927] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR954246 Genomic DNA. Translation: CAI85316.1.
RefSeq	YP_338759.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3709414.
GenomeReviews	Gene locus PSHAa0213 in contig CR954246_GR.
KEGG	pha:PSHAa0213.
NMPDR	fig|326442.4.peg.2.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q3ILQ9.
Enzyme and pathway databases
BioCyc	PHAL326442:PSHAA0213-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_PSEHT

Accession

Primary (citable) accession number: Q3ILQ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 29, 2008
Last sequence update:	November 8, 2005
Last modified:	November 25, 2008
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)