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Q7WMM4 (CYSG_BORBR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. 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

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:BB1367
OrganismBordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]
Taxonomic identifier257310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length473 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 – 473473Siroheme synthase HAMAP-Rule MF_01646
PRO_0000330497

Regions

Region218 – 461244Uroporphyrinogen-III C-methyltransferase HAMAP-Rule MF_01646

Sequences

Sequence LengthMass (Da)Tools
Q7WMM4 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 245B36E15E68991E

FASTA47350,648
        10         20         30         40         50         60 
MTLFPIFADL TGRRVLVVGG GAVAVRKTQA LLQAGAEVVV GAPRLDPALA ALAEQGGIAR 

        70         80         90        100        110        120 
LDGGFEPAWL AGAWLVVAAT DDRAVNAAVS EAARARRVFC NVVDDAELSS FQVPSVVDRS 

       130        140        150        160        170        180 
PLIVAISSSG VAPVLARRLR ERIESLFDHS LGQLAALAAR YRPRIRAARP DLGQRRRFYD 

       190        200        210        220        230        240 
WLLDGPVAAR LRQQQPGLAE QELEQALRAP QAAPRGSVVL VGAGPGDPGL LTLKALRALN 

       250        260        270        280        290        300 
EADIILYDRL VSEGVLALAR RDAERVPVGK LPGEDHDATQ ARIHALMLAQ ARAGRRVVRL 

       310        320        330        340        350        360 
KGGDAFIFGR GGEELEYLRA HDVPYEVVPG ITAALACAAY AGIPLTHRDH AQSVRMVTAH 

       370        380        390        400        410        420 
CRADQDTLDW AGLARDQQTL AFYMGVGQLD YVTARLLEHG RAPATPFALI ENGSRPEQRV 

       430        440        450        460        470 
VTGTLAELPE IARRRSVRPP ALLVIGEVAA LADTLQWFGQ HQHGLPGPQA LAA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX640441 Genomic DNA. Translation: CAE31865.1.
RefSeqNP_887913.1. NC_002927.3.

3D structure databases

ProteinModelPortalQ7WMM4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257310.BB1367.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE31865; CAE31865; BB1367.
GeneID2663154.
KEGGbbr:BB1367.
PATRIC21135994. VBIBorBro124907_1387.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290518.
KOK02302.
OMAQASFIMP.
OrthoDBEOG6DRPFR.
ProtClustDBCLSK881271.

Enzyme and pathway databases

BioCycBBRO257310:BB1367-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_BORBR
AccessionPrimary (citable) accession number: Q7WMM4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: October 1, 2003
Last modified: February 19, 2014
This is version 66 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