Uroporphyrinogen-III C-methyltransferase
     (Urogen III methylase)
     (EC 2.1.1.107)
     (SUMT)
     (Uroporphyrinogen III methylase)
     (UROM)
Precorrin-2 dehydrogenase
     (EC 1.3.1.76)
Sirohydrochlorin ferrochelatase
     (EC 4.99.1.4)

Gene name

	Name:	cysG2
	OrderedLocusNames:	ASA_3524

From

Aeromonas salmonicida (strain A449)

[TaxID: 382245]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; Aeromonadaceae; Aeromonas.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Reith M.E., Singh R.K., Curtis B., Boyd J., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J., Johnson S., Brown L.;
"The genome sequence of Aeromonas salmonicida subsp. salmonicida A449.";
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.

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.
CATALYTIC ACTIVITY: S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2.
CATALYTIC ACTIVITY: Precorrin-2 + NAD⁺ = sirohydrochlorin + NADH.
CATALYTIC ACTIVITY: Siroheme + 2 H⁺ = sirohydrochlorin + Fe²⁺.
PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1 .
PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; sirohydrochlorin from precorrin-2: step 1/1 .
PATHWAY: Porphyrin metabolism; siroheme biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1 .
PATHWAY: Porphyrin metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1 .
PATHWAY: Porphyrin metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1 .
SIMILARITY: Belongs to the precorrin methyltransferase family.
SEQUENCE CAUTION:
- Sequence=ABO91492.1; Type=Frameshift; Positions=22;

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CP000644; ABO91492.1; ALT_FRAME; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001143240.1; -.

3D structure databases

ModBase

A4SRH0.

Ontologies

GO:0043115;	Molecular function: precorrin-2 dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0051266;	Molecular function: sirohydrochlorin ferrochelatase activity (inferred from electronic annotation from EC).
GO:0004851;	Molecular function: uroporphyrin-III C-methyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0009236;	Biological process: cobalamin biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0019354;	Biological process: siroheme biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01646; -; 1.
PBIL [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 of domain structure.

Gene3D

G3DSA:3.40.1010.10; 4pyrrole_Mease_sub1; 1.
G3DSA:3.30.950.10; 4pyrrole_Mease_sub2; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF00590; TP_methylase; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR01469; cobA_cysG_Cterm; 1.
TIGR01470; cysG_Nterm; 1.

PROSITE

PS00839; SUMT_1; 1.
PS00840; SUMT_2; 1.

BLOCKS

A4SRH0.

Genome annotation databases

GeneID

4995755; -.

GenomeReviews

CP000644_GR; ASA_3524.

KEGG

asa:ASA_3524; -.

CMR

A4SRH0; ASA_3524.

Other

ProtoNet

A4SRH0.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cobalamin biosynthesis; Complete proteome; Lyase; Methyltransferase; Multifunctional enzyme; NAD; Oxidoreductase; Porphyrin biosynthesis; S-adenosyl-L-methionine; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 480`	`480`	`Siroheme synthase 2.`	`PRO_0000330490`
`REGION`	`216 456`	`241`	`Uroporphyrinogen-III C-methyltransferase.`

Sequence information

Length: 480 AA [This is the length of the unprocessed precursor]

Molecular weight: 51976 Da [This is the MW of the unprocessed precursor]

CRC64: 73EA4371971ABAA8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDYLPMFARL EGRPVLLVGG GEVALRKARL LLAAGARLTL VSPEIEPEFA EFAGRFTHLV 

        70         80         90        100        110        120 
ERFTPAHLAG QLLVVAATDN LEVNALVYQS ANQLGLFVNV VDDPKRSSFI FPSIIDRSPL 

       130        140        150        160        170        180 
MVAVSSGGKA PVLVRLLRER LESLLPRHLG GLTELSGRVR DKAKQVLSSI SDRRRFWERA 

       190        200        210        220        230        240 
FASNTLAGLI EKQDWQSAET WLNDGLDKAQ SEVGEVVLVG AGPGDPGLLT LKALQQIQQA 

       250        260        270        280        290        300 
EVVLYDQLVS PEILDLVRRD ATLVSVGKKA GAHSVPQEET NRLLVEYARA GNRVVRLKGG 

       310        320        330        340        350        360 
DPFMFGCGGE ELEVLAAEGI PFSVVPGITA AAGATAYAGI PLTHRDHAQS AVFITGHCQK 

       370        380        390        400        410        420 
EGKEPDWQQL AVTQQTLVIY MGLMRSEHIQ QQLVSHGRSC TTPIAIIEWG TTARQRVLTG 

       430        440        450        460        470        480 
TLAELAVLAQ QAVSPSLIVI GEVVSLRKQL AWFGEKSGEK RDVQAGTDMN GCDLKLVNLA

A4SRH0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools