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P25924

- CYSG_SALTY

UniProt

P25924 - CYSG_SALTY

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Protein
Siroheme synthase
Gene
cysG, STM3477
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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.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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei225 – 2251S-adenosyl-L-methionine; via carbonyl oxygen
Active sitei248 – 2481Proton acceptor Reviewed prediction
Active sitei270 – 2701Proton donor Reviewed prediction
Binding sitei306 – 3061S-adenosyl-L-methionine; via carbonyl oxygen
Binding sitei382 – 3821S-adenosyl-L-methionine; via amide nitrogen
Binding sitei411 – 4111S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen
Binding sitei437 – 4371S-adenosyl-L-methionine; via carbonyl oxygen

Regions

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

GO - Molecular functioni

  1. NAD binding Source: InterPro
  2. precorrin-2 dehydrogenase activity Source: UniProtKB-HAMAP
  3. sirohydrochlorin ferrochelatase activity Source: UniProtKB-EC
  4. uroporphyrin-III C-methyltransferase activity Source: UniProtKB-HAMAP
Complete GO annotation...

GO - Biological processi

  1. cobalamin biosynthetic process Source: UniProtKB-HAMAP
  2. siroheme biosynthetic process Source: UniProtKB-HAMAP
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.
SENT99287:GCTI-3499-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:STM3477
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi128 – 1281S → A: Abolishes the methyltransferase activity and increases 3 and 4-fold the dehydrogenase and ferrochelatase activities, respectively. 1 Publication
Mutagenesisi128 – 1281S → D: Abolishes the methyltransferase activity and reduces 10 and 5-fold the dehydrogenase and ferrochelatase activities, respectively. 1 Publication
Mutagenesisi250 – 2501L → A: Abolishes the dehydrogenase and ferrochelatase activities and reduces 6-fold the methyltransferase activity. 1 Publication
Mutagenesisi270 – 2701K → I: Abolishes the methyltransferase, dehydrogenase and ferrochelatase activities. 1 Publication
Mutagenesisi385 – 3851N → A: Abolishes the dehydrogenase and ferrochelatase activities and reduces 10-fold the methyltransferase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 457457Siroheme synthaseUniRule annotation
PRO_0000150380Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei128 – 1281Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP25924.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi99287.STM3477.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85
Beta strandi14 – 185
Helixi22 – 3312
Beta strandi36 – 449
Helixi47 – 537
Turni54 – 563
Beta strandi59 – 646
Helixi67 – 704
Beta strandi74 – 785
Helixi83 – 9513
Beta strandi99 – 1024
Beta strandi108 – 1125
Beta strandi115 – 1195
Beta strandi122 – 1276
Helixi133 – 14614
Helixi151 – 16818
Helixi172 – 18211
Helixi186 – 1938
Helixi197 – 20812
Beta strandi217 – 2226
Beta strandi224 – 2263
Helixi228 – 2303
Helixi233 – 2419
Beta strandi243 – 2475
Helixi253 – 2564
Beta strandi263 – 2675
Helixi280 – 29112
Beta strandi295 – 3028
Turni304 – 3063
Beta strandi307 – 3093
Helixi310 – 3145
Turni315 – 3217
Beta strandi324 – 3274
Helixi332 – 3398
Turni347 – 3493
Beta strandi351 – 3566
Helixi368 – 3725
Beta strandi373 – 38210
Beta strandi384 – 3863
Helixi387 – 39610
Beta strandi404 – 4107
Beta strandi417 – 4226
Helixi423 – 4253
Helixi426 – 4294
Turni430 – 4323
Beta strandi435 – 4428
Helixi443 – 4497

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PJQX-ray2.21A/B1-457[»]
1PJSX-ray2.40A/B1-457[»]
1PJTX-ray2.80A/B1-457[»]
ProteinModelPortaliP25924.
SMRiP25924. Positions 1-457.

Miscellaneous databases

EvolutionaryTraceiP25924.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4 – 202199Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelataseUniRule annotation
Add
BLAST
Regioni216 – 448233Uroporphyrinogen-III C-methyltransferaseUniRule annotation
Add
BLAST
Regioni301 – 3033S-adenosyl-L-methionine bindingUniRule annotation
Regioni331 – 3322S-adenosyl-L-methionine bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000290518.
KOiK02302.
OMAiQASFIMP.
OrthoDBiEOG6DRPFR.
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.
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.

P25924-1 [UniParc]FASTAAdd to Basket

« Hide

MDHLPIFCQL RDRDCLIVGG GDVAERKARL LLEAGARLTV NALTFIPQFT    50
VWANEGMLTL VEGPFDETLL DSCWLAIAAT DDDTVNQRVS DAAESRRIFC 100
NVVDAPKAAS FIMPSIIDRS PLMVAVSSGG TSPVLARLLR EKLESLLPQH 150
LGQVARYAGQ LRARVKKQFA TMGERRRFWE KFFVNDRLAQ SLANADEKAV 200
NATTERLFSE PLDHRGEVVL VGAGPGDAGL LTLKGLQQIQ QADIVVYDRL 250
VSDDIMNLVR RDADRVFVGK RAGYHCVPQE EINQILLREA QKGKRVVRLK 300
GGDPFIFGRG GEELETLCHA GIPFSVVPGI TAASGCSAYS GIPLTHRDYA 350
QSVRLVTGHL KTGGELDWEN LAAEKQTLVF YMGLNQAATI QEKLIAFGMQ 400
ADMPVALVEN GTSVKQRVVH GVLTQLGELA QQVESPALII VGRVVALRDK 450
LNWFSNH 457
Length:457
Mass (Da):50,147
Last modified:May 1, 1992 - v1
Checksum:i359C8CAF4B78092D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64606 Genomic DNA. Translation: AAA27041.1.
AE006468 Genomic DNA. Translation: AAL22339.1.
PIRiB39200.
RefSeqiNP_462380.1. NC_003197.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64606 Genomic DNA. Translation: AAA27041.1 .
AE006468 Genomic DNA. Translation: AAL22339.1 .
PIRi B39200.
RefSeqi NP_462380.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PJQ X-ray 2.21 A/B 1-457 [» ]
1PJS X-ray 2.40 A/B 1-457 [» ]
1PJT X-ray 2.80 A/B 1-457 [» ]
ProteinModelPortali P25924.
SMRi P25924. Positions 1-457.
ModBasei Search...

Protein-protein interaction databases

STRINGi 99287.STM3477.

Proteomic databases

PRIDEi P25924.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL22339 ; AAL22339 ; STM3477 .
GeneIDi 1255000.
KEGGi stm:STM3477.
PATRICi 32385755. VBISalEnt20916_3675.

Phylogenomic databases

HOGENOMi HOG000290518.
KOi K02302.
OMAi QASFIMP.
OrthoDBi EOG6DRPFR.
PhylomeDBi P25924.

Enzyme and pathway databases

UniPathwayi UPA00148 ; UER00211 .
UPA00148 ; UER00222 .
UPA00262 ; UER00211 .
UPA00262 ; UER00222 .
UPA00262 ; UER00376 .
BioCyci MetaCyc:STM3477-MONOMER.
SENT99287:GCTI-3499-MONOMER.

Miscellaneous databases

EvolutionaryTracei P25924.
PROi P25924.

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. "High-level expression of Escherichia coli NADPH-sulfite reductase: requirement for a cloned cysG plasmid to overcome limiting siroheme cofactor."
    Wu J.Y., Siegel L.M., Kredich N.M.
    J. Bacteriol. 173:325-333(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  3. "CysG structure reveals tetrapyrrole-binding features and novel regulation of siroheme biosynthesis."
    Stroupe M.E., Leech H.K., Daniels D.S., Warren M.J., Getzoff E.D.
    Nat. Struct. Biol. 10:1064-1073(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF WILD-TYPE AND OF MUTANT ALA-128 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE AND NAD, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF SER-128; LEU-250; LYS-270 AND ASN-385, ACTIVE SITE, SUBUNIT, PHOSPHORYLATION AT SER-128.

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: July 9, 2014
This is version 116 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

External Data

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