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P25924

- CYSG_SALTY

UniProt

P25924 - CYSG_SALTY

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Protein

Siroheme synthase

Gene

cysG

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 PublicationUniRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei225 – 2251S-adenosyl-L-methionine; via carbonyl oxygen
Active sitei248 – 2481Proton acceptorUniRule annotation
Active sitei270 – 2701Proton donorUniRule annotation
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 – 232NAD1 PublicationUniRule annotation
Nucleotide bindingi43 – 442NAD1 PublicationUniRule 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

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 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: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 synthasePRO_0000150380Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP25924.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi99287.STM3477.

Structurei

Secondary structure

1
457
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Beta strandi14 – 185Combined sources
Helixi22 – 3312Combined sources
Beta strandi36 – 449Combined sources
Helixi47 – 537Combined sources
Turni54 – 563Combined sources
Beta strandi59 – 646Combined sources
Helixi67 – 704Combined sources
Beta strandi74 – 785Combined sources
Helixi83 – 9513Combined sources
Beta strandi99 – 1024Combined sources
Beta strandi108 – 1125Combined sources
Beta strandi115 – 1195Combined sources
Beta strandi122 – 1276Combined sources
Helixi133 – 14614Combined sources
Helixi151 – 16818Combined sources
Helixi172 – 18211Combined sources
Helixi186 – 1938Combined sources
Helixi197 – 20812Combined sources
Beta strandi217 – 2226Combined sources
Beta strandi224 – 2263Combined sources
Helixi228 – 2303Combined sources
Helixi233 – 2419Combined sources
Beta strandi243 – 2475Combined sources
Helixi253 – 2564Combined sources
Beta strandi263 – 2675Combined sources
Helixi280 – 29112Combined sources
Beta strandi295 – 3028Combined sources
Turni304 – 3063Combined sources
Beta strandi307 – 3093Combined sources
Helixi310 – 3145Combined sources
Turni315 – 3217Combined sources
Beta strandi324 – 3274Combined sources
Helixi332 – 3398Combined sources
Turni347 – 3493Combined sources
Beta strandi351 – 3566Combined sources
Helixi368 – 3725Combined sources
Beta strandi373 – 38210Combined sources
Beta strandi384 – 3863Combined sources
Helixi387 – 39610Combined sources
Beta strandi404 – 4107Combined sources
Beta strandi417 – 4226Combined sources
Helixi423 – 4253Combined sources
Helixi426 – 4294Combined sources
Turni430 – 4323Combined sources
Beta strandi435 – 4428Combined sources
Helixi443 – 4497Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25924.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4 – 202199Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelataseAdd
BLAST
Regioni216 – 448233Uroporphyrinogen-III C-methyltransferaseAdd
BLAST
Regioni301 – 3033S-adenosyl-L-methionine binding
Regioni331 – 3322S-adenosyl-L-methionine binding

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

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

        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.

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 .
PIRi B39200.
RefSeqi NP_462380.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...
MobiDBi 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: November 26, 2014
This is version 118 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

Dasty 3