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C5BGP8 (CYSG_EDWI9) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 37. 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:NT01EI_3617
OrganismEdwardsiella ictaluri (strain 93-146) [Complete proteome] [HAMAP]
Taxonomic identifier634503 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEdwardsiella

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_1000215846

Regions

Nucleotide binding22 – 232NAD By similarity
Nucleotide binding43 – 442NAD By similarity
Region1 – 204204precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase By similarity
Region216 – 461246Uroporphyrinogen-III C-methyltransferase By similarity
Region301 – 3033S-adenosyl-L-methionine binding By similarity
Region331 – 3322S-adenosyl-L-methionine binding By similarity

Sites

Active site2481Proton acceptor By similarity
Active site2701Proton donor By similarity
Binding site2251S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3061S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3821S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site4111S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Modified residue1281Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
C5BGP8 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: 2C1300882126D4A8

FASTA46149,998
        10         20         30         40         50         60 
MDYFPIFCQL RTKPCLLVGG GEVAERKARL LMEAGAILTV NAGRFTPQFE QWQRDGQLTL 

        70         80         90        100        110        120 
IAGDFDPALL TGKWLAIAAT DDSRVNQQVL AQSEARCIFC NVVDAAQQTG FIMPSIVDRS 

       130        140        150        160        170        180 
PLMVAVSSGG SAPVLARILR EKLEALLPQH LGQVAHMAGH LRQRVKAHFP TLSLRRRFWE 

       190        200        210        220        230        240 
RLFAQDRLAQ SLANGDTTQA QQQVDALFSA APMDRGEVTL VGAGPGDAGL LTLKGLQQIQ 

       250        260        270        280        290        300 
QADVIIYDRL VSDEVMSLVR RDATRIFVGK HAGHHCVPQE EINQTLLDHA REGKRVVRLK 

       310        320        330        340        350        360 
GGDPFIFGRG GEELEALAAA GIAFSVVPGI TAASGCSAYS GIPLTHRDHA QSVRLVTGHT 

       370        380        390        400        410        420 
RQDGQLDWSC LAAAGQTLVF YMGLSQAATI QQRLLQHGML PDTPIALVEN GTTIRQRVVS 

       430        440        450        460 
GTLTQLETLA TRVASPSLII VGDVVTLRPR LNWFRCEAAS A 

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References

[1]"Complete genome sequence of Edwardsiella ictaluri 93-146."
Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C., Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 93-146.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001600 Genomic DNA. Translation: ACR70745.1.
RefSeqYP_002934980.1. NC_012779.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING634503.NT01EI_3617.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR70745; ACR70745; NT01EI_3617.
GeneID7961438.
KEGGeic:NT01EI_3617.
PATRIC21839949. VBIEdwIct114273_3224.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290518.
KOK02302.
OMAQASFIMP.
OrthoDBEOG6DRPFR.

Enzyme and pathway databases

BioCycEICT634503:GCMY-3592-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_EDWI9
AccessionPrimary (citable) accession number: C5BGP8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: June 11, 2014
This is version 37 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