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B0U4X0 (CYSG_XYLFM) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Xfasm12_2018
OrganismXylella fastidiosa (strain M12) [Complete proteome] [HAMAP]
Taxonomic identifier405440 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXylella

Protein attributes

Sequence length476 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 – 476476Siroheme synthase HAMAP-Rule MF_01646
PRO_1000186962

Regions

Nucleotide binding25 – 262NAD By similarity
Nucleotide binding46 – 472NAD By similarity
Region1 – 207207precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase By similarity
Region220 – 476257Uroporphyrinogen-III C-methyltransferase By similarity
Region305 – 3073S-adenosyl-L-methionine binding By similarity
Region335 – 3362S-adenosyl-L-methionine binding By similarity

Sites

Active site2521Proton acceptor By similarity
Active site2741Proton donor By similarity
Binding site3101S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3871S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site4161S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Modified residue1321Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
B0U4X0 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 3D5EC31A541DABAD

FASTA47651,691
        10         20         30         40         50         60 
MTANALFPLF ANLHDRAVLV VGGGKVAERK TEALLKVGAL PIIGAPSLTT SLQRWAETGR 

        70         80         90        100        110        120 
ITWRQGTFED SWLQEDIWLV IAATDQPEVN HAAARAAHAQ RLFVNVVDDI ALSNVQVPAV 

       130        140        150        160        170        180 
VERGPLRIAI SSGGGAPMVA RYLRQQLESL IDDSWGRLTT LFAQRRDTIR ARYPNIEARR 

       190        200        210        220        230        240 
RFFETQLAGP LQRLLRKQRH AEAEAVLEAA LAETPLTESG SVTLVGAGAG DAGLLTLNAL 

       250        260        270        280        290        300 
RALNEADIIL YDRLVSDTVL QMARRDAEQI EVGKSATGHS VRQEDIHTLM LQHAHAGQRV 

       310        320        330        340        350        360 
VRLKGGDPFV FGRGGEELEF LRTHGIPYEV IPGITAALAC AAYAGIPLTH RDHAQSLCLI 

       370        380        390        400        410        420 
TAHCQSSLDT LDWAALAQER QTLTFYMGVA GLPTIQQRLC EAGRAETTPF ALIENGARAQ 

       430        440        450        460        470 
QRVLTGTLKT LAHTAQTYAV RPPALLILGE VTALAEHLHW FGTAPLSAPC PPARIL 

« Hide

References

[1]"Whole genome sequences of two Xylella fastidiosa strains (M12 and M23) causing almond leaf scorch disease in California."
Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.
J. Bacteriol. 192:4534-4534(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: M12.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000941 Genomic DNA. Translation: ACA12887.1.
RefSeqYP_001776517.1. NC_010513.1.

3D structure databases

ProteinModelPortalB0U4X0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING405440.Xfasm12_2018.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA12887; ACA12887; Xfasm12_2018.
GeneID6121102.
KEGGxfm:Xfasm12_2018.
PATRIC24140853. VBIXylFas124301_2367.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290518.
KOK02302.
OMAQASFIMP.
OrthoDBEOG6DRPFR.

Enzyme and pathway databases

BioCycXFAS405440:GH0D-2059-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.
IPR003043. Uropor_MeTrfase_CS.
[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.
PROSITEPS00840. SUMT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSG_XYLFM
AccessionPrimary (citable) accession number: B0U4X0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 8, 2008
Last modified: June 11, 2014
This is version 52 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