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Q7VQG9 (CYSG_BLOFL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Bfl161
OrganismBlochmannia floridanus [Complete proteome] [HAMAP]
Taxonomic identifier203907 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeant endosymbiontsCandidatus Blochmannia

Protein attributes

Sequence length461 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 – 461461Siroheme synthase HAMAP-Rule MF_01646
PRO_0000330494

Regions

Nucleotide binding22 – 232NAD By similarity
Nucleotide binding43 – 442NAD By similarity
Region1 – 204204precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase By similarity
Region218 – 461244Uroporphyrinogen-III C-methyltransferase By similarity
Region303 – 3053S-adenosyl-L-methionine binding By similarity

Sites

Active site2501Proton acceptor By similarity
Active site2721Proton donor By similarity
Binding site2271S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3081S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3861S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site4151S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Modified residue1281Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VQG9 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 2C008334D67C27C8

FASTA46151,478
        10         20         30         40         50         60 
MRYLPLFVYL NNKPVLVVGG GIVAFRKVQI LQKTGAIIQI VAKTLCLNLK TTLFKKKIIW 

        70         80         90        100        110        120 
IGKVFQISML DNVFLVIIAT DDTDFNDMVF KYAEKRHILV NTVDDPAKCS FIFPAIIDRS 

       130        140        150        160        170        180 
PILIGISSGG QAPVLIRMLK EKLESLIPMS IGYVASLAGI WRNKIKQHIT DIVYRRFFWE 

       190        200        210        220        230        240 
KLFYNGQISL LVEKGNFRKA NRVIKDAVLN QLHNRKQGSV SLVGAGPGDK GLLTIRGLQV 

       250        260        270        280        290        300 
IQTADIILYD YLVNPDILDL SRKDANKICV GKIAKKHSIS QNNLNHFMIQ LAQQGNNVVR 

       310        320        330        340        350        360 
LKGGDSFIFG RGGEELQAVS KAGIMFQVVP GITSGIGVAA YAGIPLTHRE YAHSVVFMTG 

       370        380        390        400        410        420 
HKRHQGDYKI NWSLLSDNKQ TIVIYMGQLN AVNISKNLIC HGRHIYTPVA IISRGTYLDQ 

       430        440        450        460 
KILIGTLIEL EKLIYMVKKP TLLIIGDVVS LHNEISWFGN G 

« Hide

References

[1]"The genome sequence of Blochmannia floridanus: comparative analysis of reduced genomes."
Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F., Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B., van Ham R.C.H.J., Gross R., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248583 Genomic DNA. Translation: CAD83682.1.
RefSeqNP_878467.1. NC_005061.1.

3D structure databases

ProteinModelPortalQ7VQG9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203907.Bfl161.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD83682; CAD83682; Bfl161.
GeneID1499361.
KEGGbfl:Bfl161.
PATRIC31963915. VBICanBlo38691_0160.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290518.
KOK02302.
OMARVRWHAT.
OrthoDBEOG6DRPFR.

Enzyme and pathway databases

BioCycBFLO203907:GHF7-161-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_BLOFL
AccessionPrimary (citable) accession number: Q7VQG9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: October 1, 2003
Last modified: June 11, 2014
This is version 74 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