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A5W1H7 (CYSG_PSEP1) 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
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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:Pput_1834
OrganismPseudomonas putida (strain F1 / ATCC 700007) [Complete proteome] [HAMAP]
Taxonomic identifier351746 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length463 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 – 463463Siroheme synthase HAMAP-Rule MF_01646
PRO_0000330540

Regions

Nucleotide binding22 – 232NAD By similarity
Nucleotide binding43 – 442NAD By similarity
Region1 – 203203precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase By similarity
Region216 – 463248Uroporphyrinogen-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
A5W1H7 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 7738ABD519697647

FASTA46349,467
        10         20         30         40         50         60 
MDYLPLFHKL QGGRVLVVGG GEIALRKARL LADAGGVLRV VAPDVDGQLA ALAREGGGEV 

        70         80         90        100        110        120 
LVRGYQAADL VGCRLVIAAT DDPGLNAQVS ADAQALSVPV NVVDAPALCT VIFPAIVDRS 

       130        140        150        160        170        180 
PLVIAVSSGG DAPVLARLIR AKLEAWIPSA YGELAGLAAR FRHKVKSLYP DVNQRRGFWE 

       190        200        210        220        230        240 
TVFQGPIAER QLAGQGAEAE RLLQAMVDGA PVQQGGEVYL VGAGPGDPDL LTFRALRLMQ 

       250        260        270        280        290        300 
QADVVLYDRL VAPAIIDMCR RDAERIYVGK RRADHSVPQD QINRLLVDLA RQGKRVLRLK 

       310        320        330        340        350        360 
GGDPFIFGRG GEEIEELAEH GIPFQVVPGI TAASGCSAYG GIPLTHRDYA QSVRFVTGHL 

       370        380        390        400        410        420 
KDGTSNLPWT DLVAPAQTLV FYMGLVGLPT ICAELIRHGR AASTPAALVQ QGTTRNQRVF 

       430        440        450        460 
TGTLADLPDL VAQHEVHAPT LVIVGEVVQL RDKLAWFEGS QNS 

« Hide

References

[1]"Complete sequence of Pseudomonas putida F1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: F1 / ATCC 700007.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000712 Genomic DNA. Translation: ABQ77987.1.
RefSeqYP_001267171.1. NC_009512.1.

3D structure databases

ProteinModelPortalA5W1H7.
SMRA5W1H7. Positions 1-459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351746.Pput_1834.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ77987; ABQ77987; Pput_1834.
GeneID5193098.
KEGGppf:Pput_1834.
PATRIC19919764. VBIPsePut56420_1867.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290518.
KOK02302.
OMAQASFIMP.
OrthoDBEOG6DRPFR.

Enzyme and pathway databases

BioCycPPUT351746:GI26-1880-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_PSEP1
AccessionPrimary (citable) accession number: A5W1H7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: July 10, 2007
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