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Q1CCP6 (CYSG2_YERPN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 65. 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 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:YPN_3907
ORF Names:YP516_4437
OrganismYersinia pestis bv. Antiqua (strain Nepal516) [Complete proteome] [HAMAP]
Taxonomic identifier377628 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length470 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 – 470470Siroheme synthase 2 HAMAP-Rule MF_01646
PRO_0000330575

Regions

Nucleotide binding22 – 232NAD By similarity
Nucleotide binding43 – 442NAD By similarity
Region1 – 201201precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase By similarity
Region213 – 470258Uroporphyrinogen-III C-methyltransferase By similarity
Region298 – 3003S-adenosyl-L-methionine binding By similarity
Region328 – 3292S-adenosyl-L-methionine binding By similarity

Sites

Active site2451Proton acceptor By similarity
Active site2671Proton donor By similarity
Binding site2221S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3031S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3791S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site4081S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Modified residue1281Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1CCP6 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: D28E9E9C1182F316

FASTA47051,664
        10         20         30         40         50         60 
MDYFPIFCQL QHKACLLVGG GEIAERKARL LLDAGALVTV NACEFTPQFH HWADQGQLSL 

        70         80         90        100        110        120 
ISGEFVPELL ADKWLVIAAT DQLSVNALVY QSANQQRIFC NVVDDPKRTS FIMPSIIDRS 

       130        140        150        160        170        180 
PIMIAVSSGG KAPVLARLLR EKLEALLPQH LGQLAGNLRQ RVKQHFTVMT ERRRFWEKLL 

       190        200        210        220        230        240 
THDRLAQSLA NNDHVQADQH VEQLFSAPLT DRGEVVLVGA GPGDAGLLTL KGLQQIQQAD 

       250        260        270        280        290        300 
VVVYDRLVSD EVMNLVRRDA ERIFVGKQSG HHCVPQEQIN QILLQQAQSG KRVVRLKGGD 

       310        320        330        340        350        360 
PFIFGRGGEE LEELAGYGIP FSVVPGITAA SGCSAYSGIP LTHRDHAQSV RLVTGHAKKE 

       370        380        390        400        410        420 
GQLDWANLAA EKQTLVFYMG LSQAGEIQQQ LIQHGMPATT QVALVENGTS RHQRVVSGEL 

       430        440        450        460        470 
SQLALLSQQV SSPSLIIVGS VVSLREKLNW FSSRHHDDQP KVTECVAHVG 

« Hide

References

[1]"Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516: evidence of gene reduction in an emerging pathogen."
Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M., Worsham P., Chu M.C., Andersen G.L.
J. Bacteriol. 188:4453-4463(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Nepal516.
[2]"Yersinia pestis Nepal516A whole genome shotgun sequencing project."
Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L., Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R., Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.
Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000305 Genomic DNA. Translation: ABG20234.1.
ACNQ01000019 Genomic DNA. Translation: EEO74827.1.
RefSeqYP_649834.1. NC_008149.1.

3D structure databases

ProteinModelPortalQ1CCP6.
SMRQ1CCP6. Positions 1-453.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING377628.YPN_3907.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG20234; ABG20234; YPN_3907.
EEO74827; EEO74827; YP516_4437.
GeneID4125659.
KEGGypn:YPN_3907.
PATRIC18607949. VBIYerPes46733_4602.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290518.
KOK02302.
OMAQASFIMP.
OrthoDBEOG6DRPFR.

Enzyme and pathway databases

BioCycYPES377628:GIXK-4008-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 nameCYSG2_YERPN
AccessionPrimary (citable) accession number: Q1CCP6
Secondary accession number(s): D1Q2S4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: July 11, 2006
Last modified: June 11, 2014
This is version 65 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