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Protein

Siroheme synthase

Gene

cysG

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

2 S-adenosyl-L-methionine + uroporphyrinogen III = 2 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

Keywordsi

Molecular functionLyase, Methyltransferase, Multifunctional enzyme, Oxidoreductase, Transferase
Biological processCobalamin biosynthesis, Porphyrin biosynthesis
LigandNAD, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:STM3477-MONOMER
SENT99287:G1FZD-3512-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

Chemistry databases

DrugBankiDB04522 Phosphonoserine
DB01752 S-Adenosyl-L-Homocysteine

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
OMAiFCVRADD
PhylomeDBiP25924

Family and domain databases

CDDicd11642 SUMT, 1 hit
Gene3Di1.10.8.210, 1 hit
3.30.950.10, 1 hit
3.40.1010.10, 1 hit
HAMAPiMF_01646 Siroheme_synth, 1 hit
InterProiView protein in InterPro
IPR000878 4pyrrol_Mease
IPR035996 4pyrrol_Methylase_sf
IPR014777 4pyrrole_Mease_sub1
IPR014776 4pyrrole_Mease_sub2
IPR006366 CobA/CysG_C
IPR036291 NAD(P)-bd_dom_sf
IPR037115 Sirohaem_synt_dimer_dom_sf
IPR012409 Sirohaem_synth
IPR028281 Sirohaem_synthase_central
IPR019478 Sirohaem_synthase_dimer_dom
IPR006367 Sirohaem_synthase_N
IPR003043 Uropor_MeTrfase_CS
PfamiView protein in Pfam
PF10414 CysG_dimeriser, 1 hit
PF14824 Sirohm_synth_M, 1 hit
PF00590 TP_methylase, 1 hit
PIRSFiPIRSF036426 Sirohaem_synth, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
SSF53790 SSF53790, 1 hit
TIGRFAMsiTIGR01469 cobA_cysG_Cterm, 1 hit
TIGR01470 cysG_Nterm, 1 hit
PROSITEiView protein in PROSITE
PS00839 SUMT_1, 1 hit
PS00840 SUMT_2, 1 hit

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_003197.2
WP_000349895.1, NC_003197.2

Genome annotation databases

EnsemblBacteriaiAAL22339; AAL22339; STM3477
GeneIDi1255000
KEGGistm:STM3477
PATRICifig|99287.12.peg.3675

Similar proteinsi

Entry informationi

Entry nameiCYSG_SALTY
AccessioniPrimary (citable) accession number: P25924
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: March 28, 2018
This is version 139 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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