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:	cysG
	OrderedLocusNames:	Psyc_1065

From

Psychrobacter arcticus (strain DSM 17307 / 273-4)

[TaxID: 259536]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Moraxellaceae; Psychrobacter.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
NASA Astrobiology Institute;
Ayala-del-Rio H.L., Chain P., Ponder M.A., Di Bartolo G., Ivanova N., Bergholz P.W., Hauser L., Land M., Bakermans C., Rodrigues D., Klappenbach J.A., Zarka D., Larimer F., Richardson P., Thomashow M.F., Tiedje J.M.;
"Complete sequence of Psychrobacter arcticum 273-4.";
Submitted (JUL-2005) 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.

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

CP000082; AAZ18917.1; ALT_INIT; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_264351.1; -.

3D structure databases

ModBase

Q4FSU1.

Enzyme and pathway databases

BioCyc

PARC259536:PSYC_1065-MON; -.

Ontologies

GO:0004325;	Molecular function: ferrochelatase activity (inferred from electronic annotation from HAMAP).
GO:0043115;	Molecular function: precorrin-2 dehydrogenase activity (inferred from electronic annotation from HAMAP).
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; FALSE_NEG.
PS00840; SUMT_2; 1.

BLOCKS

Q4FSU1.

Genome annotation databases

GeneID

3514951; -.

GenomeReviews

CP000082_GR; Psyc_1065.

KEGG

par:Psyc_1065; -.

NMPDR

fig|259536.4.peg.646; -.

Phylogenomic databases

HOGENOM

Q4FSU1; -.

Genome annotation databases

CMR

Q4FSU1; Psyc_1065.

Other

ProtoNet

Q4FSU1.

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`	`1 549`	`549`	`Siroheme synthase.`	`PRO_0000330546`
`REGION`	`249 491`	`243`	`Uroporphyrinogen-III C-methyltransferase.`

Sequence information

Length: 549 AA [This is the length of the unprocessed precursor]

Molecular weight: 59727 Da [This is the MW of the unprocessed precursor]

CRC64: 019AACCDA20937C4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNTFPLFFKL EDRKVLIVGG GDVALRKADL LSRAGACITV LAPSINHEIQ ALLSSSKHEL 

        70         80         90        100        110        120 
IYEHYNKTYM TNSRVIIAAT DDERLNHQIH ADATALNIPV NVVDTPHLCD FIFPAIVDRN 

       130        140        150        160        170        180 
PIVIGISSNG KAPVLARLLR ARLETLIPQG YGKLAKLAGE FRGDVKAKIP TLTGRRQFWE 

       190        200        210        220        230        240 
RAFEGKVSQL MFAGNENEAL AQLQADLDNT AASITAKDAT DDNGLSTAST SAPAIANEFT 

       250        260        270        280        290        300 
AARNTMGEVY IVGAGPGDPE LLTFKALRLM QQADIVYYDA LVSPQVLDLC RRDADKVFVG 

       310        320        330        340        350        360 
KKRRNHAVAQ LGINELLVNS AKEGRRVVRL KGGDPFIFGR GGEEIESLRA HNIPYQVVPG 

       370        380        390        400        410        420 
ITAANAAASY AGIPLTHRDH SQSVRFVTGF LKAGAPNNNF KNFLDTDETV VFYMGLHSLP 

       430        440        450        460        470        480 
RLTEGLIDAG RSAETPIAIV SNASMPNQQV LTGTLASIVE LQEKNQLPTP ALLIMGDVVS 

       490        500        510        520        530        540 
LHHDLAWYNL HNQQHNQNTS ETDNNWLRGG TATTPKSNAQ FNAHQQAHAL SMITNLATED 


GDLEQLIIG

Q4FSU1 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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