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A1JSB7 (CYSG2_YERE8) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 57. 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 2

Including the following 3 domains:

  1. Uroporphyrinogen-III C-methyltransferase 2
    Short name=Urogen III methylase 2
    EC=2.1.1.107
    Alternative name(s):
    SUMT 2
    Uroporphyrinogen III methylase 2
    Short name=UROM 2
  2. Precorrin-2 dehydrogenase 2
    EC=1.3.1.76
  3. Sirohydrochlorin ferrochelatase 2
    EC=4.99.1.4
Gene names
Name:cysG2
Ordered Locus Names:YE3968
OrganismYersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081) [Complete proteome] [HAMAP]
Taxonomic identifier393305 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length472 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 – 472472Siroheme synthase 2 HAMAP-Rule MF_01646
PRO_0000330571

Regions

Nucleotide binding22 – 232NAD By similarity
Nucleotide binding43 – 442NAD By similarity
Region1 – 204204precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase By similarity
Region216 – 472257Uroporphyrinogen-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
A1JSB7 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 51BE67EF4B78F238

FASTA47251,812
        10         20         30         40         50         60 
MDYFPIFCQL QNKACLLVGG GEVAERKARL LLDAGAAVTV NACEFTEQFH DWAEQGLLSL 

        70         80         90        100        110        120 
VSGEFAPELL AEKWLVIAAT DQVAVNALVY QSANQQRVFC NVVDDPKRTS FIMPSIIDRS 

       130        140        150        160        170        180 
PIMIAISSGG KAPVLARLLR EKLEAMLPQH LGQLAQLAGN LRQRVKQHFA AMTDRRRFWE 

       190        200        210        220        230        240 
KLLTHDRLAQ SLANEDQVQV EQHVEQLFNA PLSDRGEVVL VGAGPGDAGL LTLKGLQQIQ 

       250        260        270        280        290        300 
QADVVVYDRL VSDEVMNLVR RDAERIFVGK ESGRHTVPQD QINQILLQQA QQGKRVVRLK 

       310        320        330        340        350        360 
GGDPFIFGRG GEELETLADY NIPFSVVPGI TAASGCSAYS GIPLTHRDHA QSVRLITGHA 

       370        380        390        400        410        420 
KKDSQLDWAN LAAEKQTLVF YMGLSQAGEI QQQLIRHGMP AATPVALVEN GTSRHQRVVS 

       430        440        450        460        470 
GELSQLALLS QQVSSPSLII VGSVVSLREK LNWFSSAEHG KTGMKEQVER VG 

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References

[1]"The complete genome sequence and comparative genome analysis of the high pathogenicity Yersinia enterocolitica strain 8081."
Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L., Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T., Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S., Sanders M., Whitehead S. expand/collapse author list , Quail M.A., Dougan G., Parkhill J., Prentice M.B.
PLoS Genet. 2:2039-2051(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 13174 / 8081.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM286415 Genomic DNA. Translation: CAL13987.1.
RefSeqYP_001008113.1. NC_008800.1.

3D structure databases

ProteinModelPortalA1JSB7.
SMRA1JSB7. Positions 1-456.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING393305.YE3968.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL13987; CAL13987; YE3968.
GeneID4716180.
KEGGyen:YE3968.
PATRIC18567796. VBIYerEnt11519_4223.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290518.
KOK02302.
OMAQASFIMP.
OrthoDBEOG6DRPFR.

Enzyme and pathway databases

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 nameCYSG2_YERE8
AccessionPrimary (citable) accession number: A1JSB7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: February 6, 2007
Last modified: June 11, 2014
This is version 57 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