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Protein

Siroheme synthase

Gene

cysG

Organism
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1.UniRule annotation
S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2.UniRule annotation
Precorrin-2 + NAD+ = sirohydrochlorin + NADH.UniRule annotation
Siroheme + 2 H+ = sirohydrochlorin + Fe2+.UniRule annotation

Pathway:iadenosylcobalamin biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes precorrin-2 from uroporphyrinogen III.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Siroheme synthase (cysG)
This subpathway is part of the pathway adenosylcobalamin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes precorrin-2 from uroporphyrinogen III, the pathway adenosylcobalamin biosynthesis and in Cofactor biosynthesis.

Pathway:iadenosylcobalamin biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes sirohydrochlorin from precorrin-2.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Siroheme synthase (cysG)
This subpathway is part of the pathway adenosylcobalamin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes sirohydrochlorin from precorrin-2, the pathway adenosylcobalamin biosynthesis and in Cofactor biosynthesis.

Pathway:isiroheme biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes precorrin-2 from uroporphyrinogen III.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Siroheme synthase (cysG)
This subpathway is part of the pathway siroheme biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes precorrin-2 from uroporphyrinogen III, the pathway siroheme biosynthesis and in Porphyrin-containing compound metabolism.

Pathway:isiroheme biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes siroheme from sirohydrochlorin.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Siroheme synthase (cysG)
This subpathway is part of the pathway siroheme biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes siroheme from sirohydrochlorin, the pathway siroheme biosynthesis and in Porphyrin-containing compound metabolism.

Pathway:isiroheme biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes sirohydrochlorin from precorrin-2.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Siroheme synthase (cysG)
This subpathway is part of the pathway siroheme biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes sirohydrochlorin from precorrin-2, the pathway siroheme biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei225 – 2251S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotation
Active sitei248 – 2481Proton acceptorUniRule annotation
Active sitei270 – 2701Proton donorUniRule annotation
Binding sitei307 – 3071S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotation
Binding sitei384 – 3841S-adenosyl-L-methionine; via amide nitrogenUniRule annotation
Binding sitei413 – 4131S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi22 – 232NADUniRule annotation
Nucleotide bindingi43 – 442NADUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase, Methyltransferase, Oxidoreductase, Transferase

Keywords - Biological processi

Cobalamin biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

NAD, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciBPER257313:BP1055-MONOMER.
UniPathwayiUPA00148; UER00211.
UPA00148; UER00222.
UPA00262; UER00211.
UPA00262; UER00222.
UPA00262; UER00376.

Names & Taxonomyi

Protein namesi
Recommended name:
Siroheme synthaseUniRule annotation
Including the following 3 domains:
Uroporphyrinogen-III C-methyltransferaseUniRule annotation (EC:2.1.1.107UniRule annotation)
Short name:
Urogen III methylaseUniRule annotation
Alternative name(s):
SUMTUniRule annotation
Uroporphyrinogen III methylaseUniRule annotation
Short name:
UROMUniRule annotation
Precorrin-2 dehydrogenaseUniRule annotation (EC:1.3.1.76UniRule annotation)
Sirohydrochlorin ferrochelataseUniRule annotation (EC:4.99.1.4UniRule annotation)
Gene namesi
Name:cysGUniRule annotation
Ordered Locus Names:BP1055
OrganismiBordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Taxonomic identifieri257313 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
ProteomesiUP000002676 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Siroheme synthasePRO_0000330499Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei128 – 1281PhosphoserineUniRule annotation

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

STRINGi257313.BP1055.

Structurei

3D structure databases

ProteinModelPortaliQ7VZ77.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 203203precorrin-2 dehydrogenase / sirohydrochlorin ferrochelataseUniRule annotationAdd
BLAST
Regioni216 – 473258Uroporphyrinogen-III C-methyltransferaseUniRule annotationAdd
BLAST
Regioni302 – 3043S-adenosyl-L-methionine bindingUniRule annotation
Regioni332 – 3332S-adenosyl-L-methionine bindingUniRule annotation

Sequence similaritiesi

In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family.UniRule annotation
In the C-terminal section; belongs to the precorrin methyltransferase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0007.
HOGENOMiHOG000290518.
KOiK02302.
OMAiQASFIMP.
OrthoDBiEOG6DRPFR.

Family and domain databases

Gene3Di1.10.8.210. 1 hit.
3.30.950.10. 1 hit.
3.40.1010.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_01646. Siroheme_synth.
InterProiIPR000878. 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]
PfamiPF10414. CysG_dimeriser. 1 hit.
PF13241. NAD_binding_7. 1 hit.
PF00590. TP_methylase. 1 hit.
[Graphical view]
PIRSFiPIRSF036426. Sirohaem_synth. 1 hit.
SUPFAMiSSF53790. SSF53790. 1 hit.
TIGRFAMsiTIGR01469. cobA_cysG_Cterm. 1 hit.
TIGR01470. cysG_Nterm. 1 hit.
PROSITEiPS00839. SUMT_1. 1 hit.
PS00840. SUMT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7VZ77-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLFPIFADL TGRRVLVVGG GAVAVRKTQA LLQAGAEVVV GAPRLDPALA
60 70 80 90 100
ALAEQGGIAR LDGGFEPAWL AGAWLVVAAT DDRAVNAAVS EAARARRVFC
110 120 130 140 150
NVVDDAELSS FQVPSVVDRS PLIVAISSSG VAPVLARRLR ERIESLFDHS
160 170 180 190 200
LGQLAALAAR YRPRIRAARP DLGQRRRFYD WLLDGPVAAR LRQQQPGLAE
210 220 230 240 250
QELEQALRAP QAAPRGSVVL VGAGPGDPGL LTLKALRALN EADIILYDRL
260 270 280 290 300
VSEGVLALAR RDAERVPVGK LPGKGHDATQ ARIHALMLAQ ARAGRRVVRL
310 320 330 340 350
KGGDAFIFGR GGEELEYLRA HGVPYEVVPG ITAALACAAY AGMPLTHRDH
360 370 380 390 400
AQSVRMVTAH CRADQDTLDW AGLARDQQTL AFYMGVGQLD YVTARLLEHG
410 420 430 440 450
RAPATPFALI ENGSRPEQRV VTGTLADLPE IARRRGVRPP ALLVIGEVAA
460 470
LADTLQWFGQ HQRGLPGPQA LAA
Length:473
Mass (Da):50,524
Last modified:October 1, 2003 - v1
Checksum:iE68DF9621CA27612
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640414 Genomic DNA. Translation: CAE41354.1.
RefSeqiNP_879840.1. NC_002929.2.
WP_010930160.1. NC_002929.2.

Genome annotation databases

EnsemblBacteriaiCAE41354; CAE41354; BP1055.
GeneIDi2664362.
KEGGibpe:BP1055.
PATRICi21155254. VBIBorPer7866_1127.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640414 Genomic DNA. Translation: CAE41354.1.
RefSeqiNP_879840.1. NC_002929.2.
WP_010930160.1. NC_002929.2.

3D structure databases

ProteinModelPortaliQ7VZ77.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi257313.BP1055.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE41354; CAE41354; BP1055.
GeneIDi2664362.
KEGGibpe:BP1055.
PATRICi21155254. VBIBorPer7866_1127.

Phylogenomic databases

eggNOGiCOG0007.
HOGENOMiHOG000290518.
KOiK02302.
OMAiQASFIMP.
OrthoDBiEOG6DRPFR.

Enzyme and pathway databases

UniPathwayiUPA00148; UER00211.
UPA00148; UER00222.
UPA00262; UER00211.
UPA00262; UER00222.
UPA00262; UER00376.
BioCyciBPER257313:BP1055-MONOMER.

Family and domain databases

Gene3Di1.10.8.210. 1 hit.
3.30.950.10. 1 hit.
3.40.1010.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_01646. Siroheme_synth.
InterProiIPR000878. 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]
PfamiPF10414. CysG_dimeriser. 1 hit.
PF13241. NAD_binding_7. 1 hit.
PF00590. TP_methylase. 1 hit.
[Graphical view]
PIRSFiPIRSF036426. Sirohaem_synth. 1 hit.
SUPFAMiSSF53790. SSF53790. 1 hit.
TIGRFAMsiTIGR01469. cobA_cysG_Cterm. 1 hit.
TIGR01470. cysG_Nterm. 1 hit.
PROSITEiPS00839. SUMT_1. 1 hit.
PS00840. SUMT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica."
    Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S.
    , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J.
    Nat. Genet. 35:32-40(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Tohama I / ATCC BAA-589 / NCTC 13251.

Entry informationi

Entry nameiCYSG_BORPE
AccessioniPrimary (citable) accession number: Q7VZ77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: October 1, 2003
Last modified: May 27, 2015
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.