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Reviewed, UniProtKB/Swiss-Prot Q1H3L5 (CYSG_METFK)

Last modified June 16, 2009. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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: Mfla_0652
OrganismMethylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875) [Complete proteome] [HAMAP]
Taxonomic identifier265072 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaMethylophilalesMethylophilaceaeMethylobacillus

Protein attributes

Sequence length467 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 467467Siroheme synthase HAMAP MF_01646
PRO_0000330521

Regions

Region218 – 460243Uroporphyrinogen-III C-methyltransferase HAMAP MF_01646

Sequences

Sequence LengthMass (Da)Tools
Q1H3L5-1 [UniParc].

Last modified April 29, 2008. Version 2.
Checksum: 9DB793C2313128A4

FASTA46750,652
        10         20         30         40         50         60 
METLPIFMKL RDRPCLVVGG GEIASRKVSL LEKAGASVTV VSPELHPTLA KSLAEGRIRH 

        70         80         90        100        110        120 
LASVFEPAQL DGAVLVIAAT DDAEVNRAVS REAQARNIPV NVVDAPELCT FIVPSIVDRS 

       130        140        150        160        170        180 
PLLVAVSSGG TAPVLARMLR TRIETLIPAT YGRLAAFAAE FREAVKQRFS TGQQRRIFWE 

       190        200        210        220        230        240 
DVFQGVIGEQ VLSGQEEAAR HAMQQVLSGR GELHHGEVYL VGGGPGDPDL LTFRALRLMQ 

       250        260        270        280        290        300 
QADVCVYDKL VSKEVMALVR RDAELIYVGK SRDQHTLPQE DINQLLVRLA KEGKRVLRLK 

       310        320        330        340        350        360 
GGDPFIFGRG GEEIETLMEN GIPFQVVPGI TAANGVSSYA GIPLTHRDYA QSCLFTTGHL 

       370        380        390        400        410        420 
KDGSVNLDWD ALVRPNQTVV IYMGLVGLPE ICRQMVAHGA PENLPIAIVQ QGTTQRQRVV 

       430        440        450        460 
EGTLATLPGL VERAGLRAPC LIIVGQVVRL REKLAWFAPS PEVVSAG 

« Hide

References

[1]"Complete sequence of Methylobacillus flagellatus KT."
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., Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000284 Genomic DNA. Translation: ABE48922.1. Different initiation.
RefSeqYP_544763.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4000719.
GenomeReviewsGene locus Mfla_0652 in contig CP000284_GR.
KEGGmfa:Mfla_0652.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1H3L5.

Enzyme and pathway databases

BioCycMFLA265072:MFLA_0652-MON.

Family and domain databases

HAMAPMF_01646.
[Tree]
InterProIPR000878. 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]
Gene3DG3DSA: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.
PfamPF10414. CysG_dimeriser. 1 hit.
PF00590. TP_methylase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01469. cobA_cysG_Cterm. 1 hit.
TIGR01470. cysG_Nterm. 1 hit.
PROSITEPS00839. SUMT_1. False negative.
PS00840. SUMT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSG_METFK
AccessionPrimary (citable) accession number: Q1H3L5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: April 29, 2008
Last modified: June 16, 2009
This is version 27 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents