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Reviewed, UniProtKB/Swiss-Prot Q6LM67 (CYSG_PHOPR)

Last modified November 25, 2008. Version 30. 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: PBPRA3312
OrganismPhotobacterium profundum (Photobacterium sp. (strain SS9)) [Complete proteome] [HAMAP]
Taxonomic identifier74109 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaePhotobacterium

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred 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. 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 + Fe(2+). 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 – 469469Siroheme synthase HAMAP MF_01646
PRO_0000330529

Regions

Region216 – 456241Uroporphyrinogen-III C-methyltransferase HAMAP MF_01646

Sequences

Sequence LengthMass (Da)Tools
Q6LM67-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 79177BD9A4116649

FASTA46951,363
        10         20         30         40         50         60 
MDYLPIFTDL KRRPCLVVGG GDVAWRKARM LLKAGADVRV IAPVLNQAFQ QAIEQQQVSH 

        70         80         90        100        110        120 
VADEFESSHL DGIFLAIAAT DRKAVNALVY QSANQRQVLV NVVDDTQRCS FIIPSIIDRS 

       130        140        150        160        170        180 
PIIVAVSSSG KAPVLARLIR EKLEALLPQH LGRMATIAGN FRARLAKTVT SFSARRQFWE 

       190        200        210        220        230        240 
QVFDGRFSDL VACGQEQDAK QELINLTQST SPQGQVALIG SGPGDAGLLT LRALQLMQQA 

       250        260        270        280        290        300 
DVVLYDYLVS DEVMDLVRRD AELVCVGKKA GFHSVPQEET NQLIVKYAQQ GKRVVRLKGG 

       310        320        330        340        350        360 
DPFVFGRGGE ELEVLFDANI LFQVVPGITA AAGATAYAGI PLTHRDYAQT AMFVTGHLKA 

       370        380        390        400        410        420 
ESDQMDWSTL ARGKQTLVIY MGLMKSGHIQ QQLLINGRAG DTPIAIIERG TQKKQKVIKG 

       430        440        450        460 
QLSELEQLAK NAESPSLIVI GEVVNLSEKL HWFGKQEQSL QQSAVVKLA 

« Hide

References

[1]"Life at depth: Photobacterium profundum genome sequence and expression analysis."
Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M., Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C., Bartlett D.H., Valle G.
Science 307:1459-1461(2005) [PubMed: 15746425] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CR378673 Genomic DNA. Translation: CAG21610.1.
RefSeqYP_131412.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3125518.
GenomeReviewsGene locus PBPRA3312 in contig CR354531_GR.
KEGGppr:PBPRA3312.
NMPDRfig|298386.1.peg.5519.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ6LM67.

Enzyme and pathway databases

BioCycPPRO298386:PBPRA3312-MON.

Family and domain databases

HAMAPMF_01646.
[Tree]
InterProIPR000878. 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]
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.
PfamPF00590. TP_methylase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01469. cobA_cysG_Cterm. 1 hit.
TIGR01470. cysG_Nterm. 1 hit.
PROSITEPS00839. SUMT_1. 1 hit.
PS00840. SUMT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSG_PHOPR
AccessionPrimary (citable) accession number: Q6LM67
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: July 5, 2004
Last modified: November 25, 2008
This is version 30 of the entry and version 1 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