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B3GZA0 (CYSG_ACTP7) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 49. 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:APP7_1934
OrganismActinobacillus pleuropneumoniae serotype 7 (strain AP76) [Complete proteome] [HAMAP]
Taxonomic identifier537457 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeActinobacillus

Protein attributes

Sequence length486 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 – 486486Siroheme synthase HAMAP-Rule MF_01646
PRO_1000186933

Regions

Nucleotide binding22 – 232NAD By similarity
Nucleotide binding43 – 442NAD By similarity
Region1 – 204204precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase By similarity
Region216 – 486271Uroporphyrinogen-III C-methyltransferase By similarity
Region301 – 3033S-adenosyl-L-methionine binding By similarity
Region331 – 3322S-adenosyl-L-methionine binding By similarity

Sites

Active site2481Proton acceptor By similarity
Active site2701Proton donor By similarity
Binding site2251S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3061S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site3831S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site4121S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Amino acid modifications

Modified residue1281Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
B3GZA0 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: 0DD1062564BB3708

FASTA48653,272
        10         20         30         40         50         60 
MNYLPIFVDL KNRPVLVVGG GHVAVRKIYA LLKADALVKV VAEKLHSSLQ ILVNEGKVEW 

        70         80         90        100        110        120 
LAKAFEASQV TSSYLVIAAT DDNALNQQVF DTAESQQRLV NVVDDQPRCS YIFPSIIDRS 

       130        140        150        160        170        180 
PVQIAISSGG AAPVLIRLLR EKLEALIPHN LGAMADIATR WRSAVKTQFP QLTQRRRFWE 

       190        200        210        220        230        240 
KLFTHQSFQR LTENHQIEQA EALVESELQN NNPVLGEVSL VGAGPGDAGL LTLKGLQTIQ 

       250        260        270        280        290        300 
QADVVLYDAL VSEAVLELVR RDADKVFVGK RAGKHSVKQD DTNQLLVKYA KQGKRVVRLK 

       310        320        330        340        350        360 
GGDPFVFGRG GEELEILKAE NIPFSVVPGI TAALGATAYA GIPLTHRDHA QTAMFITGHL 

       370        380        390        400        410        420 
KPDGNRLKWE TLAQGNQTLV VYMGTIKAAE LSAELQKHGK PSDTPVAIIS NGTLPNQQVQ 

       430        440        450        460        470        480 
TGVLSELAEL AEKAPTPALI VIGEVVKLQK DLAWFGKEAV QFVSTQETLW QKPTLQNKET 


HWKQAA 

« Hide

References

[1]"Genome and proteome analysis of A. pleuropneumoniae serotype 7."
Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N., Tegetmeyer H., Singh M., Gerlach G.F.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AP76.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001091 Genomic DNA. Translation: ACE62586.1.
RefSeqYP_001969728.1. NC_010939.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING537457.APP7_1934.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACE62586; ACE62586; APP7_1934.
GeneID6396544.
KEGGapa:APP7_1934.
PATRIC20757679. VBIActPle116979_1983.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290518.
KOK02302.
OMALHQQLAW.
OrthoDBEOG6DRPFR.

Enzyme and pathway databases

BioCycAPLE537457:GJI0-2010-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.
PROSITEPS00839. SUMT_1. 1 hit.
PS00840. SUMT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCYSG_ACTP7
AccessionPrimary (citable) accession number: B3GZA0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: July 22, 2008
Last modified: June 11, 2014
This is version 49 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