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Protein

Siroheme synthase

Gene

cysG

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: 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.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1.1 Publication
S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2.1 Publication
Precorrin-2 + NAD+ = sirohydrochlorin + NADH.1 Publication
Siroheme + 2 H+ = sirohydrochlorin + Fe2+.1 Publication

Pathwayi: adenosylcobalamin 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.

Pathwayi: adenosylcobalamin 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.

Pathwayi: siroheme 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.

Pathwayi: siroheme 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.

Pathwayi: siroheme 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)DescriptionActionsGraphical viewLength
Binding sitei225S-adenosyl-L-methionine; via carbonyl oxygen1 Publication1
Active sitei248Proton acceptor1 Publication1
Active sitei270Proton donor1 Publication1
Binding sitei306S-adenosyl-L-methionine; via carbonyl oxygen1 Publication1
Binding sitei382S-adenosyl-L-methionine; via amide nitrogen1 Publication1
Binding sitei411S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei437S-adenosyl-L-methionine; via carbonyl oxygen1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi22 – 23NAD1 Publication2
Nucleotide bindingi43 – 44NAD1 Publication2

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

BioCyciMetaCyc:STM3477-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:2.1.1.1071 Publication)
Short name:
Urogen III methylaseUniRule annotation
Alternative name(s):
SUMTUniRule annotation
Uroporphyrinogen III methylaseUniRule annotation
Short name:
UROMUniRule annotation
Precorrin-2 dehydrogenaseUniRule annotation (EC:1.3.1.761 Publication)
Sirohydrochlorin ferrochelataseUniRule annotation (EC:4.99.1.41 Publication)
Gene namesi
Name:cysGUniRule annotation
Ordered Locus Names:STM3477
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi128S → A: Abolishes the methyltransferase activity and increases 3 and 4-fold the dehydrogenase and ferrochelatase activities, respectively. 1 Publication1
Mutagenesisi128S → D: Abolishes the methyltransferase activity and reduces 10 and 5-fold the dehydrogenase and ferrochelatase activities, respectively. 1 Publication1
Mutagenesisi250L → A: Abolishes the dehydrogenase and ferrochelatase activities and reduces 6-fold the methyltransferase activity. 1 Publication1
Mutagenesisi270K → I: Abolishes the methyltransferase, dehydrogenase and ferrochelatase activities. 1 Publication1
Mutagenesisi385N → A: Abolishes the dehydrogenase and ferrochelatase activities and reduces 10-fold the methyltransferase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001503801 – 457Siroheme synthaseAdd BLAST457

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei128Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP25924.
PRIDEiP25924.

PTM databases

iPTMnetiP25924.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi99287.STM3477.

Structurei

Secondary structure

1457
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 8Combined sources5
Beta strandi14 – 18Combined sources5
Helixi22 – 33Combined sources12
Beta strandi36 – 44Combined sources9
Helixi47 – 53Combined sources7
Turni54 – 56Combined sources3
Beta strandi59 – 64Combined sources6
Helixi67 – 70Combined sources4
Beta strandi74 – 78Combined sources5
Helixi83 – 95Combined sources13
Beta strandi99 – 102Combined sources4
Beta strandi108 – 112Combined sources5
Beta strandi115 – 119Combined sources5
Beta strandi122 – 127Combined sources6
Helixi133 – 146Combined sources14
Helixi151 – 168Combined sources18
Helixi172 – 182Combined sources11
Helixi186 – 193Combined sources8
Helixi197 – 208Combined sources12
Beta strandi217 – 222Combined sources6
Beta strandi224 – 226Combined sources3
Helixi228 – 230Combined sources3
Helixi233 – 241Combined sources9
Beta strandi243 – 247Combined sources5
Helixi253 – 256Combined sources4
Beta strandi263 – 267Combined sources5
Helixi271 – 273Combined sources3
Helixi280 – 291Combined sources12
Beta strandi295 – 302Combined sources8
Turni304 – 306Combined sources3
Beta strandi307 – 309Combined sources3
Helixi310 – 314Combined sources5
Turni315 – 321Combined sources7
Beta strandi324 – 327Combined sources4
Helixi332 – 339Combined sources8
Turni347 – 349Combined sources3
Beta strandi351 – 356Combined sources6
Beta strandi359 – 361Combined sources3
Helixi368 – 372Combined sources5
Beta strandi373 – 382Combined sources10
Beta strandi384 – 386Combined sources3
Helixi387 – 396Combined sources10
Beta strandi404 – 410Combined sources7
Beta strandi417 – 422Combined sources6
Helixi423 – 425Combined sources3
Helixi426 – 429Combined sources4
Turni430 – 432Combined sources3
Beta strandi435 – 442Combined sources8
Helixi443 – 449Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PJQX-ray2.21A/B1-457[»]
1PJSX-ray2.40A/B1-457[»]
1PJTX-ray2.80A/B1-457[»]
ProteinModelPortaliP25924.
SMRiP25924.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25924.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni4 – 202Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelataseAdd BLAST199
Regioni216 – 448Uroporphyrinogen-III C-methyltransferaseAdd BLAST233
Regioni301 – 303S-adenosyl-L-methionine binding1 Publication3
Regioni331 – 332S-adenosyl-L-methionine binding1 Publication2

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

eggNOGiENOG4105CB8. Bacteria.
COG0007. LUCA.
COG1648. LUCA.
HOGENOMiHOG000290518.
KOiK02302.
OMAiQASFIMP.
PhylomeDBiP25924.

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. 1 hit.
InterProiIPR000878. 4pyrrol_Mease.
IPR014777. 4pyrrole_Mease_sub1.
IPR014776. 4pyrrole_Mease_sub2.
IPR006366. CobA/CysG_C.
IPR016040. NAD(P)-bd_dom.
IPR012409. Sirohaem_synth.
IPR028281. Sirohaem_synthase_central.
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.
PF14824. Sirohm_synth_M. 1 hit.
PF00590. TP_methylase. 1 hit.
[Graphical view]
PIRSFiPIRSF036426. Sirohaem_synth. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF53790. 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.

P25924-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDHLPIFCQL RDRDCLIVGG GDVAERKARL LLEAGARLTV NALTFIPQFT
60 70 80 90 100
VWANEGMLTL VEGPFDETLL DSCWLAIAAT DDDTVNQRVS DAAESRRIFC
110 120 130 140 150
NVVDAPKAAS FIMPSIIDRS PLMVAVSSGG TSPVLARLLR EKLESLLPQH
160 170 180 190 200
LGQVARYAGQ LRARVKKQFA TMGERRRFWE KFFVNDRLAQ SLANADEKAV
210 220 230 240 250
NATTERLFSE PLDHRGEVVL VGAGPGDAGL LTLKGLQQIQ QADIVVYDRL
260 270 280 290 300
VSDDIMNLVR RDADRVFVGK RAGYHCVPQE EINQILLREA QKGKRVVRLK
310 320 330 340 350
GGDPFIFGRG GEELETLCHA GIPFSVVPGI TAASGCSAYS GIPLTHRDYA
360 370 380 390 400
QSVRLVTGHL KTGGELDWEN LAAEKQTLVF YMGLNQAATI QEKLIAFGMQ
410 420 430 440 450
ADMPVALVEN GTSVKQRVVH GVLTQLGELA QQVESPALII VGRVVALRDK

LNWFSNH
Length:457
Mass (Da):50,147
Last modified:May 1, 1992 - v1
Checksum:i359C8CAF4B78092D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64606 Genomic DNA. Translation: AAA27041.1.
AE006468 Genomic DNA. Translation: AAL22339.1.
PIRiB39200.
RefSeqiNP_462380.1. NC_003197.1.
WP_000349895.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL22339; AAL22339; STM3477.
GeneIDi1255000.
KEGGistm:STM3477.
PATRICi32385755. VBISalEnt20916_3675.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64606 Genomic DNA. Translation: AAA27041.1.
AE006468 Genomic DNA. Translation: AAL22339.1.
PIRiB39200.
RefSeqiNP_462380.1. NC_003197.1.
WP_000349895.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PJQX-ray2.21A/B1-457[»]
1PJSX-ray2.40A/B1-457[»]
1PJTX-ray2.80A/B1-457[»]
ProteinModelPortaliP25924.
SMRiP25924.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM3477.

PTM databases

iPTMnetiP25924.

Proteomic databases

PaxDbiP25924.
PRIDEiP25924.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL22339; AAL22339; STM3477.
GeneIDi1255000.
KEGGistm:STM3477.
PATRICi32385755. VBISalEnt20916_3675.

Phylogenomic databases

eggNOGiENOG4105CB8. Bacteria.
COG0007. LUCA.
COG1648. LUCA.
HOGENOMiHOG000290518.
KOiK02302.
OMAiQASFIMP.
PhylomeDBiP25924.

Enzyme and pathway databases

UniPathwayiUPA00148; UER00211.
UPA00148; UER00222.
UPA00262; UER00211.
UPA00262; UER00222.
UPA00262; UER00376.
BioCyciMetaCyc:STM3477-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP25924.
PROiP25924.

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. 1 hit.
InterProiIPR000878. 4pyrrol_Mease.
IPR014777. 4pyrrole_Mease_sub1.
IPR014776. 4pyrrole_Mease_sub2.
IPR006366. CobA/CysG_C.
IPR016040. NAD(P)-bd_dom.
IPR012409. Sirohaem_synth.
IPR028281. Sirohaem_synthase_central.
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.
PF14824. Sirohm_synth_M. 1 hit.
PF00590. TP_methylase. 1 hit.
[Graphical view]
PIRSFiPIRSF036426. Sirohaem_synth. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF53790. 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...

Entry informationi

Entry nameiCYSG_SALTY
AccessioniPrimary (citable) accession number: P25924
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 2, 2016
This is version 130 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

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.