Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A8G9Y3 (CYSG1_SERP5) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 52. 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 1

Including the following 3 domains:

  1. Uroporphyrinogen-III C-methyltransferase 1
    Short name=Urogen III methylase 1
    EC=2.1.1.107
    Alternative name(s):
    SUMT 1
    Uroporphyrinogen III methylase 1
    Short name=UROM 1
  2. Precorrin-2 dehydrogenase 1
    EC=1.3.1.76
  3. Sirohydrochlorin ferrochelatase 1
    EC=4.99.1.4
Gene names
Name:cysG1
Ordered Locus Names:Spro_0817
OrganismSerratia proteamaculans (strain 568) [Complete proteome] [HAMAP]
Taxonomic identifier399741 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

Protein attributes

Sequence length476 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 – 476476Siroheme synthase 1 HAMAP-Rule MF_01646
PRO_0000330557

Regions

Nucleotide binding22 – 232NAD By similarity
Nucleotide binding43 – 442NAD By similarity
Region1 – 203203precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase By similarity
Region219 – 476258Uroporphyrinogen-III C-methyltransferase By similarity
Region304 – 3063S-adenosyl-L-methionine binding By similarity
Region334 – 3352S-adenosyl-L-methionine binding By similarity

Sites

Active site2511Proton acceptor By similarity
Active site2731Proton donor By similarity
Binding site2281S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3091S-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
A8G9Y3 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 2DAB7E09F9A3B2B9

FASTA47651,267
        10         20         30         40         50         60 
MDYLPIFADL KQRPVLVVGG GEVAARKVDL LLRAGAEIRI VAQSLSPILE QLSQQGQIHW 

        70         80         90        100        110        120 
LGQAFAAEQL DEVFLVIAAT DDSALNAEVF SEADKRRVLA NVVDDQPRCS FIFPSIIDRS 

       130        140        150        160        170        180 
PLVVAVSSSG QAPVLARMLR EKLEALLPAS LGQMAEVAGR WRGQVKQRLN AIGERRRFWE 

       190        200        210        220        230        240 
KTFGGRFATL VANGQTAEAQ RQLEQDLEQF AQGSEGTQGE IALVGAGPGD VGLLTLRGLQ 

       250        260        270        280        290        300 
VMQQADVVLY DHLVSDEILD LVRRDAERIC VGKRAGAHSV IQEETNRLLV ELAQQGKRVV 

       310        320        330        340        350        360 
RLKGGDPFIF GRGGEELQVA AAAGIPFQVV PGVTAAAGAT AYAGIPLTHR DHAQSVTFIT 

       370        380        390        400        410        420 
GHCRPDGDGL DWADLARARQ TLAIYMGTMK AADISQRLIA HGRAATTPVA VISRGTRADQ 

       430        440        450        460        470 
LVQTGTLQQL EQLAQQAPLP ALLVIGEVVE LHHQIAWFGH QPQAEGVSRP AVVNLA 

« Hide

References

[1]"Complete sequence of chromosome of Serratia proteamaculans 568."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. expand/collapse author list , Taghavi S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 568.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000826 Genomic DNA. Translation: ABV39923.1.
RefSeqYP_001477051.1. NC_009832.1.

3D structure databases

ProteinModelPortalA8G9Y3.
SMRA8G9Y3. Positions 1-460.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING399741.Spro_0817.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV39923; ABV39923; Spro_0817.
GeneID5603444.
KEGGspe:Spro_0817.
PATRIC32414278. VBISerPro44537_0846.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290518.
KOK02302.
OMALHQQLAW.
OrthoDBEOG6DRPFR.

Enzyme and pathway databases

BioCycSPRO399741:GI55-845-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 nameCYSG1_SERP5
AccessionPrimary (citable) accession number: A8G9Y3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: November 13, 2007
Last modified: June 11, 2014
This is version 52 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