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Q3SG32 (CYSG_THIDA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Siroheme synthase

Including the following 3 domains:

  1. Uroporphyrinogen-III C-methyltransferase
    Short name=Urogen III methylase
    EC=2.1.1.107
    Alternative name(s):
    SUMT
    Uroporphyrinogen III methylase
    Short name=UROM
  2. Precorrin-2 dehydrogenase
    EC=1.3.1.76
  3. Sirohydrochlorin ferrochelatase
    EC=4.99.1.4
Gene names
Name:cysG
Ordered Locus Names:Tbd_2471
OrganismThiobacillus denitrificans (strain ATCC 25259) [Complete proteome] [HAMAP]
Taxonomic identifier292415 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaHydrogenophilalesHydrogenophilaceaeThiobacillus

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_01646

Catalytic activity

S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1. HAMAP-Rule MF_01646

S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2. HAMAP-Rule MF_01646

Precorrin-2 + NAD+ = sirohydrochlorin + NADH. HAMAP-Rule MF_01646

Siroheme + 2 H+ = sirohydrochlorin + Fe2+. HAMAP-Rule MF_01646

Pathway

Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. HAMAP-Rule MF_01646

Cofactor biosynthesis; adenosylcobalamin biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.

Porphyrin-containing compound metabolism; siroheme biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. HAMAP-Rule MF_01646

Porphyrin-containing compound metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1.

Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.

Sequence similarities

In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family.

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 479479Siroheme synthase HAMAP-Rule MF_01646
PRO_0000330565

Regions

Nucleotide binding22 – 232NAD By similarity
Nucleotide binding43 – 442NAD By similarity
Region1 – 202202precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase By similarity
Region217 – 479263Uroporphyrinogen-III C-methyltransferase By similarity
Region302 – 3043S-adenosyl-L-methionine binding By similarity
Region332 – 3332S-adenosyl-L-methionine binding By similarity

Sites

Active site2491Proton acceptor By similarity
Active site2711Proton donor By similarity
Binding site2261S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3071S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3841S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site4131S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Modified residue1281Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3SG32 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 657A2AD46D5B5EC9

FASTA47951,742
        10         20         30         40         50         60 
MNYLPIFLDL RDRHCLVVGG SETAARKAEL LLRAGAHVAV AAPALHAGFE QLPDRQRLTR 

        70         80         90        100        110        120 
VADTFSPALL DGKDAVIVVE DDAAAAQIVA DAARARHLPV NVADKPALCS FILPSIIDRS 

       130        140        150        160        170        180 
PIMVAVSSGG ESPVLARLLR ARLETLIPAA YGRLSALASR YKARVREAIQ PGQRRAFWEK 

       190        200        210        220        230        240 
VFLSSVAEMV FSGRDSEAEA QLEAMIKDSA AHEPARGEVY LVGAGPGNPD LLTFRALRLM 

       250        260        270        280        290        300 
QQADVVVYDR LVSQPILDMC RRDAERIYVG KERDDHAVPQ EEINMMLVRL AKEGKRTLRL 

       310        320        330        340        350        360 
KGGDPFIFGR GGEEIETLVE HGVAFQVVPG ITAAAGVASY AGIPLTHRDY AQSVAFVTGH 

       370        380        390        400        410        420 
LKENTFNMNW EGIARRDQTI VIYMGLKGLP MLCEALIKHG LTADTPAAIV QHGTLPTQRV 

       430        440        450        460        470 
ITGTLATLPT LAVEAGLKAP TLIIVGNVVK LREKLAWYRP QAAGEAAAAT PLEAPDHLA 

« Hide

References

[1]"The genome sequence of the obligately chemolithoautotrophic, facultatively anaerobic bacterium Thiobacillus denitrificans."
Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W., Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.
J. Bacteriol. 188:1473-1488(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25259.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000116 Genomic DNA. Translation: AAZ98424.1.
RefSeqYP_316229.1. NC_007404.1.

3D structure databases

ProteinModelPortalQ3SG32.
SMRQ3SG32. Positions 1-459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292415.Tbd_2471.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ98424; AAZ98424; Tbd_2471.
GeneID3671790.
KEGGtbd:Tbd_2471.
PATRIC23971137. VBIThiDen82923_2455.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290518.
KOK02302.
OMANRVGQAY.
OrthoDBEOG6DRPFR.

Enzyme and pathway databases

BioCycTDEN292415:GHWG-2521-MONOMER.
UniPathwayUPA00148; UER00211.
UPA00148; UER00222.
UPA00262; UER00211.
UPA00262; UER00222.
UPA00262; UER00376.

Family and domain databases

Gene3D1.10.8.210. 1 hit.
3.30.950.10. 1 hit.
3.40.1010.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPMF_01646. Siroheme_synth.
InterProIPR000878. 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.
[Graphical view]
PfamPF10414. CysG_dimeriser. 1 hit.
PF13241. NAD_binding_7. 1 hit.
PF00590. TP_methylase. 1 hit.
[Graphical view]
PIRSFPIRSF036426. Sirohaem_synth. 1 hit.
SUPFAMSSF53790. SSF53790. 1 hit.
TIGRFAMsTIGR01469. cobA_cysG_Cterm. 1 hit.
TIGR01470. cysG_Nterm. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCYSG_THIDA
AccessionPrimary (citable) accession number: Q3SG32
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: October 11, 2005
Last modified: June 11, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways