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A6V4H6 (CYSG_PSEA7) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. 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:PSPA7_2597
OrganismPseudomonas aeruginosa (strain PA7) [Complete proteome] [HAMAP]
Taxonomic identifier381754 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
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. 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

Belongs to the precorrin methyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 465465Siroheme synthase HAMAP-Rule MF_01646
PRO_0000330534

Regions

Region219 – 461243Uroporphyrinogen-III C-methyltransferase HAMAP-Rule MF_01646

Sequences

Sequence LengthMass (Da)Tools
A6V4H6 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: DB1540256BB2D0B3

FASTA46550,297
        10         20         30         40         50         60 
MDFLPLFHSL QGRLALVVGG GEVALRKARL LADAGARLRV VAPQIHIELR HLVEQGGGEL 

        70         80         90        100        110        120 
LERDYQDGDQ PGCALIIAAT DDEPLNAEVS RAANARGIPV NVVDAPALCS VIFPAIVDRS 

       130        140        150        160        170        180 
PLVVAVSSGG DAPVLARLIR AKLETWIPSS YGQLAGLASR FRNRVKELLP DLQQRRVFWE 

       190        200        210        220        230        240 
NLFQGEIAER VLAGRPAEAE RLLEERLAGG LAHMATGEVY LVGAGPGDPD LLTFRALRLM 

       250        260        270        280        290        300 
QQADVVLYDR LVAPAILELC RRDAERLYVG KRRAEHAVPQ ERINRLLVEL ASQGKRVLRL 

       310        320        330        340        350        360 
KGGDPFIFGR GGEEIDELAA HGIPFQVVPG ITAASGCAAY AGIPLTHRDH AQSVRFVTGH 

       370        380        390        400        410        420 
LKDGTTDLPW KDLVAPGQTL VFYMGLVGLP VICEQLVAHG RSAQTPAALI QQGTTAQQRV 

       430        440        450        460 
FSGTLENLPQ LVAEHEVHAP TLVIVGEVVQ LRDKLAWFEG AREGA 

« Hide

References

[1]Dodson R.J., Harkins D., Paulsen I.T.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PA7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000744 Genomic DNA. Translation: ABR83518.1.
RefSeqYP_001347961.1. NC_009656.1.

3D structure databases

ProteinModelPortalA6V4H6.
SMRA6V4H6. Positions 1-460.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING381754.PSPA7_2597.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR83518; ABR83518; PSPA7_2597.
GeneID5356325.
KEGGpap:PSPA7_2597.
PATRIC19826941. VBIPseAer80442_2488.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290518.
KOK02302.
OMALPVICEQ.
OrthoDBEOG6DRPFR.
ProtClustDBCLSK867405.

Enzyme and pathway databases

BioCycPAER381754:GHMY-2597-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.
PROSITEPS00840. SUMT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSG_PSEA7
AccessionPrimary (citable) accession number: A6V4H6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: August 21, 2007
Last modified: February 19, 2014
This is version 50 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