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

Q6CZS0 (CYSG2_PECAS) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 67. 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
    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:cysG2
Ordered Locus Names:ECA4081
OrganismPectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia carotovora subsp. atroseptica) [Complete proteome] [HAMAP]
Taxonomic identifier218491 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium

Protein attributes

Sequence length459 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 – 459459Siroheme synthase 2 HAMAP-Rule MF_01646
PRO_0000330506

Regions

Region218 – 457240Uroporphyrinogen-III C-methyltransferase HAMAP-Rule MF_01646

Sequences

Sequence LengthMass (Da)Tools
Q6CZS0 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 0CC2A1827080646F

FASTA45950,607
        10         20         30         40         50         60 
MDYLPIFCQL HDKPCLLVGG GEIAERKARL LLDAGAVITV NALDFNDQFR AWEKDAQLTL 

        70         80         90        100        110        120 
VHSTFDPALL NEVWLVIAAT DNQDVNNHVY ASASERRIFC NVVDSPERAS FIMPSIIDRS 

       130        140        150        160        170        180 
PLMVAVSSGG TAPVLARLLR EKLESILPQN LGKLAAFAGE LRSRVKIRFC KMSARRRFWE 

       190        200        210        220        230        240 
KLFVHDRLAQ ALASEDRERV QQLTELLFSA PLDDRGEVTL VGAGPGDAGL LTLKGLQHLQ 

       250        260        270        280        290        300 
QADIVVYDRL VSKEILNLSR RDAERIFVGK ASGYHSVPQD QINQLLEEKA RAGHRVVRLK 

       310        320        330        340        350        360 
GGDPFIFGRG AEELEYLQQA GVPFSVVPGI TAASGCSAYS GIPLTHRDHS QGVRLITGHV 

       370        380        390        400        410        420 
KHDTDLDWSS LAAEKQTLVF YMGLQQAEHI QNKLIEQQLP ETVPVAIIEN GTSTKQRVLS 

       430        440        450 
GQLSQLGELA QQASSPSLII IGNVVGLREK LSWFSDQTA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX950851 Genomic DNA. Translation: CAG76978.1.
RefSeqYP_052168.1. NC_004547.2.

3D structure databases

ProteinModelPortalQ6CZS0.
SMRQ6CZS0. Positions 1-457.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING218491.ECA4081.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG76978; CAG76978; ECA4081.
GeneID2882115.
KEGGeca:ECA4081.
PATRIC20483609. VBIPecAtr54885_4150.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290518.
KOK02302.
OMAQASFIMP.
OrthoDBEOG6DRPFR.
ProtClustDBPRK10637.

Enzyme and pathway databases

BioCycPATR218491:GJNB-4165-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_PECAS
AccessionPrimary (citable) accession number: Q6CZS0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: August 16, 2004
Last modified: April 16, 2014
This is version 67 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