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P0AEA8

- CYSG_ECOLI

UniProt

P0AEA8 - CYSG_ECOLI

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Protein
Siroheme synthase
Gene
cysG, b3368, JW3331
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.5 Publications

Catalytic activityi

S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1.4 Publications
S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2.4 Publications
Precorrin-2 + NAD+ = sirohydrochlorin + NADH.4 Publications
Siroheme + 2 H+ = sirohydrochlorin + Fe2+.4 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei225 – 2251S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Active sitei248 – 2481Proton acceptor Reviewed prediction
Active sitei270 – 2701Proton donor Reviewed prediction
Binding sitei306 – 3061S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding sitei382 – 3821S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding sitei411 – 4111S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi22 – 232NAD By similarity
Nucleotide bindingi43 – 442NAD By similarity

GO - Molecular functioni

  1. NAD binding Source: InterPro
  2. precorrin-2 dehydrogenase activity Source: EcoCyc
  3. sirohydrochlorin ferrochelatase activity Source: EcoCyc
  4. uroporphyrin-III C-methyltransferase activity Source: EcoCyc

GO - Biological processi

  1. cobalamin biosynthetic process Source: UniProtKB-HAMAP
  2. siroheme biosynthetic process Source: EcoCyc
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

BioCyciEcoCyc:SIROHEMESYN-MONOMER.
ECOL316407:JW3331-MONOMER.
MetaCyc:SIROHEMESYN-MONOMER.
UniPathwayiUPA00148; UER00211.
UPA00148; UER00222.
UPA00262; UER00211.
UPA00262; UER00222.
UPA00262; UER00376.

Names & Taxonomyi

Protein namesi
Recommended name:
Siroheme synthase
Including the following 3 domains:
Uroporphyrinogen-III C-methyltransferase (EC:2.1.1.107)
Short name:
Urogen III methylase
Alternative name(s):
SUMT
Uroporphyrinogen III methylase
Short name:
UROM
Precorrin-2 dehydrogenase (EC:1.3.1.76)
Sirohydrochlorin ferrochelatase (EC:4.99.1.4)
Gene namesi
Name:cysG
Ordered Locus Names:b3368, JW3331
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10188. cysG.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi21 – 211G → D: It has methyltransferase and ferrochelatase activities but a greatly reduced dehydrogenase activity. It is able to bind AdoMet. 1 Publication
Mutagenesisi224 – 2241G → A: It abolishes methyltransferase activity, but has dehydrogenase and ferrochelatase activities. It is unable to bind AdoMet. 1 Publication
Mutagenesisi227 – 2271D → A: It has all activities of CysG. 1 Publication
Mutagenesisi248 – 2481D → A: It abolishes methyltransferase activity, but has dehydrogenase and ferrochelatase activities. It is able to bind AdoMet.
Mutagenesisi270 – 2701K → I: It has all activities of CysG. It is able to bind AdoMet. 1 Publication
Mutagenesisi298 – 2981R → L: It abolishes methyltransferase activity, but has dehydrogenase and ferrochelatase activities. It is unable to bind AdoMet. 1 Publication
Mutagenesisi303 – 3031D → A: It has all activities of CysG. It is able to bind AdoMet. 1 Publication
Mutagenesisi309 – 3091R → L: It abolishes methyltransferase activity, but has dehydrogenase and ferrochelatase activities. It is able to bind AdoMet. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 457457Siroheme synthaseUniRule annotation
PRO_0000150378Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei128 – 1281Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP0AEA8.
PRIDEiP0AEA8.

Expressioni

Gene expression databases

GenevestigatoriP0AEA8.

Interactioni

Subunit structurei

Monomer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
nadEP188431EBI-1132623,EBI-548960

Protein-protein interaction databases

IntActiP0AEA8. 1 interaction.
STRINGi511145.b3368.

Structurei

3D structure databases

ProteinModelPortaliP0AEA8.
SMRiP0AEA8. Positions 1-457.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4 – 204201Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase By similarity
Add
BLAST
Regioni216 – 448233Uroporphyrinogen-III C-methyltransferase By similarity
Add
BLAST
Regioni301 – 3033S-adenosyl-L-methionine binding By similarity
Regioni331 – 3322S-adenosyl-L-methionine binding By similarity

Sequence similaritiesi

In the C-terminal section; belongs to the precorrin methyltransferase family.

Phylogenomic databases

eggNOGiCOG0007.
HOGENOMiHOG000290518.
KOiK02302.
OMAiQASFIMP.
OrthoDBiEOG6DRPFR.
PhylomeDBiP0AEA8.

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.

P0AEA8-1 [UniParc]FASTAAdd to Basket

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MDHLPIFCQL RDRDCLIVGG GDVAERKARL LLDAGARLTV NALAFIPQFT    50
AWADAGMLTL VEGPFDESLL DTCWLAIAAT DDDALNQRVS EAAEARRIFC 100
NVVDAPKAAS FIMPSIIDRS PLMVAVSSGG TSPVLARLLR EKLESLLPLH 150
LGQVAKYAGQ LRGRVKQQFA TMGERRRFWE KLFVNDRLAQ SLANNDQKAI 200
TETTEQLINE PLDHRGEVVL VGAGPGDAGL LTLKGLQQIQ QADVVVYDRL 250
VSDDIMNLVR RDADRVFVGK RAGYHCVPQE EINQILLREA QKGKRVVRLK 300
GGDPFIFGRG GEELETLCNA GIPFSVVPGI TAASGCSAYS GIPLTHRDYA 350
QSVRLITGHL KTGGELDWEN LAAEKQTLVF YMGLNQAATI QQKLIEHGMP 400
GEMPVAIVEN GTAVTQRVID GTLTQLGELA QQMNSPSLII IGRVVGLRDK 450
LNWFSNH 457
Length:457
Mass (Da):49,951
Last modified:December 6, 2005 - v1
Checksum:iDDDE0DC90C5CF2F4
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261R → P in CAA32419. 1 Publication
Sequence conflicti26 – 261R → P in AAA58165. 1 Publication
Sequence conflicti90 – 912SE → RQ in CAA32419. 1 Publication
Sequence conflicti90 – 912SE → RQ in AAA58165. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X14202 Genomic DNA. Translation: CAA32419.1.
U18997 Genomic DNA. Translation: AAA58165.1.
U00096 Genomic DNA. Translation: AAC76393.1.
AP009048 Genomic DNA. Translation: BAE77922.1.
PIRiC65131.
RefSeqiNP_417827.1. NC_000913.3.
YP_492063.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76393; AAC76393; b3368.
BAE77922; BAE77922; BAE77922.
GeneIDi12933484.
947880.
KEGGiecj:Y75_p3807.
eco:b3368.
PATRICi32122170. VBIEscCol129921_3462.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X14202 Genomic DNA. Translation: CAA32419.1 .
U18997 Genomic DNA. Translation: AAA58165.1 .
U00096 Genomic DNA. Translation: AAC76393.1 .
AP009048 Genomic DNA. Translation: BAE77922.1 .
PIRi C65131.
RefSeqi NP_417827.1. NC_000913.3.
YP_492063.1. NC_007779.1.

3D structure databases

ProteinModelPortali P0AEA8.
SMRi P0AEA8. Positions 1-457.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P0AEA8. 1 interaction.
STRINGi 511145.b3368.

Proteomic databases

PaxDbi P0AEA8.
PRIDEi P0AEA8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76393 ; AAC76393 ; b3368 .
BAE77922 ; BAE77922 ; BAE77922 .
GeneIDi 12933484.
947880.
KEGGi ecj:Y75_p3807.
eco:b3368.
PATRICi 32122170. VBIEscCol129921_3462.

Organism-specific databases

EchoBASEi EB0185.
EcoGenei EG10188. cysG.

Phylogenomic databases

eggNOGi COG0007.
HOGENOMi HOG000290518.
KOi K02302.
OMAi QASFIMP.
OrthoDBi EOG6DRPFR.
PhylomeDBi P0AEA8.

Enzyme and pathway databases

UniPathwayi UPA00148 ; UER00211 .
UPA00148 ; UER00222 .
UPA00262 ; UER00211 .
UPA00262 ; UER00222 .
UPA00262 ; UER00376 .
BioCyci EcoCyc:SIROHEMESYN-MONOMER.
ECOL316407:JW3331-MONOMER.
MetaCyc:SIROHEMESYN-MONOMER.

Miscellaneous databases

PROi P0AEA8.

Gene expression databases

Genevestigatori P0AEA8.

Family and domain databases

Gene3Di 1.10.8.210. 1 hit.
3.30.950.10. 1 hit.
3.40.1010.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPi MF_01646. Siroheme_synth.
InterProi IPR000878. 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 ]
Pfami PF10414. CysG_dimeriser. 1 hit.
PF13241. NAD_binding_7. 1 hit.
PF00590. TP_methylase. 1 hit.
[Graphical view ]
PIRSFi PIRSF036426. Sirohaem_synth. 1 hit.
SUPFAMi SSF53790. SSF53790. 1 hit.
TIGRFAMsi TIGR01469. cobA_cysG_Cterm. 1 hit.
TIGR01470. cysG_Nterm. 1 hit.
PROSITEi PS00839. SUMT_1. 1 hit.
PS00840. SUMT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of binding sequences for the Escherichia coli transcription activators, FNR and CRP: location of bases involved in discrimination between FNR and CRP."
    Bell A.I., Gaston K.L., Cole J.A., Busby S.J.W.
    Nucleic Acids Res. 17:3865-3874(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Nucleotide sequence, organisation and structural analysis of the products of genes in the nirB-cysG region of the Escherichia coli K-12 chromosome."
    Peakman T., Crouzet J., Mayaux J.F., Busby S.J.W., Mohan S., Harborne N., Wootton J., Nicolson R., Cole J.A.
    Eur. J. Biochem. 191:315-323(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Enzymatic synthesis of dihydrosirohydrochlorin (precorrin-2) and of a novel pyrrocorphin by uroporphyrinogen III methylase."
    Warren M.J., Stolowich N.J., Santander P.J., Roessner C.A., Sowa B.A., Scott A.I.
    FEBS Lett. 261:76-80(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-18, FUNCTION, CATALYTIC ACTIVITY.
  6. "The Escherichia coli cysG gene encodes S-adenosylmethionine-dependent uroporphyrinogen III methylase."
    Warren M.J., Roessner C.A., Santander P.J., Scott A.I.
    Biochem. J. 265:725-729(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A METHYLTRANSFERASE, CATALYTIC ACTIVITY, SUBUNIT.
  7. "The Escherichia coli cysG gene encodes the multifunctional protein, siroheme synthase."
    Spencer J.B., Stolowich N.J., Roessner C.A., Scott A.I.
    FEBS Lett. 335:57-60(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AND CATALYTIC ACTIVITY.
  8. "Evidence for a covalent intermediate in the S-adenosyl-L-methionine-dependent transmethylation reaction catalysed by sirohaem synthase."
    Woodcock S.C., Warren M.J.
    Biochem. J. 313:415-421(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Effect of mutations in the transmethylase and dehydrogenase/chelatase domains of sirohaem synthase (CysG) on sirohaem and cobalamin biosynthesis."
    Woodcock S.C., Raux E., Levillayer F., Thermes C., Rambach A., Warren M.J.
    Biochem. J. 330:121-129(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-21; GLY-224; ASP-227; LYS-270; ARG-298; ASP-303 AND ARG-309.

Entry informationi

Entry nameiCYSG_ECOLI
AccessioniPrimary (citable) accession number: P0AEA8
Secondary accession number(s): P11098, P76685, Q2M734
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: June 11, 2014
This is version 84 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, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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