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Q6LM67 (CYSG_PHOPR) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Siroheme synthase

Including the following 3 domains:

  1. 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. Precorrin-2 dehydrogenase
    EC=1.3.1.76
  3. 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.
Protein existenceInferred from homology

General annotation (Comments)

Function

Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme By similarity. HAMAP-Rule MF_01646

Catalytic activity

S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1. HAMAP-Rule MF_01646

S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2. HAMAP-Rule MF_01646

Precorrin-2 + NAD+ = sirohydrochlorin + NADH. HAMAP-Rule MF_01646

Siroheme + 2 H+ = sirohydrochlorin + Fe2+. HAMAP-Rule MF_01646

Pathway

Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. HAMAP-Rule MF_01646

Cofactor biosynthesis; adenosylcobalamin biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.

Porphyrin-containing compound metabolism; siroheme biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. HAMAP-Rule MF_01646

Porphyrin-containing compound metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1.

Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.

Sequence similarities

In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family.

In the C-terminal section; belongs to the precorrin methyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 469469Siroheme synthase HAMAP-Rule MF_01646
PRO_0000330529

Regions

Nucleotide binding22 – 232NAD By similarity
Nucleotide binding43 – 442NAD By similarity
Region1 – 203203precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase By similarity
Region214 – 469256Uroporphyrinogen-III C-methyltransferase By similarity
Region299 – 3013S-adenosyl-L-methionine binding By similarity
Region329 – 3302S-adenosyl-L-methionine binding By similarity

Sites

Active site2461Proton acceptor By similarity
Active site2681Proton donor By similarity
Binding site2231S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3041S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3811S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site4101S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Modified residue1281Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6LM67 [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 

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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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SS9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR378673 Genomic DNA. Translation: CAG21610.1.
RefSeqYP_131412.1. NC_006370.1.

3D structure databases

ProteinModelPortalQ6LM67.
SMRQ6LM67. Positions 1-455.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING298386.PBPRA3312.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG21610; CAG21610; PBPRA3312.
GeneID3125518.
KEGGppr:PBPRA3312.
PATRIC22937691. VBIPhoPro109272_3454.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290518.
KOK02302.
OMAEHATAYT.
OrthoDBEOG6DRPFR.

Enzyme and pathway databases

BioCycPPRO298386-WGS:GSSB-3305-MONOMER.
UniPathwayUPA00148; UER00211.
UPA00148; UER00222.
UPA00262; UER00211.
UPA00262; UER00222.
UPA00262; UER00376.

Family and domain databases

Gene3D1.10.8.210. 1 hit.
3.30.950.10. 1 hit.
3.40.1010.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPMF_01646. Siroheme_synth.
InterProIPR000878. 4pyrrol_Mease.
IPR014777. 4pyrrole_Mease_sub1.
IPR014776. 4pyrrole_Mease_sub2.
IPR006366. CobA/CysG_C.
IPR016040. NAD(P)-bd_dom.
IPR012409. Sirohaem_synth.
IPR019478. Sirohaem_synthase_dimer_dom.
IPR006367. Sirohaem_synthase_N.
IPR003043. Uropor_MeTrfase_CS.
[Graphical view]
PfamPF10414. CysG_dimeriser. 1 hit.
PF13241. NAD_binding_7. 1 hit.
PF00590. TP_methylase. 1 hit.
[Graphical view]
PIRSFPIRSF036426. Sirohaem_synth. 1 hit.
SUPFAMSSF53790. SSF53790. 1 hit.
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: July 9, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways