Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q0ASU7 (Q0ASU7_MARMM) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 62. Feed History...

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

Names and origin

Protein namesSubmitted name:
Uroporphyrin-III C-methyltransferase EMBL ABI64640.1
Gene names
Ordered Locus Names:Mmar10_0347
OrganismMaricaulis maris (strain MCS10) [Complete proteome] [HAMAP] EMBL ABI64640.1
Taxonomic identifier394221 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Hyphomonadaceae › Maricaulis ›

Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Multifunctional enzyme that catalyzes the SAM-dependent methylation of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 and then position C-12 or C-18 to form trimethylpyrrocorphin 2. It also catalyzes the conversion of precorrin-2 into siroheme. This reaction consists of the NAD-dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme By similarity. SAAS SAAS019478

Catalytic activity

Precorrin-2 + NAD+ = sirohydrochlorin + NADH. SAAS SAAS019478

S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2. SAAS SAAS019478

S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1. SAAS SAAS019478

Siroheme + 2 H+ = sirohydrochlorin + Fe2+. SAAS SAAS019478

Pathway

Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. SAAS SAAS019478

Cofactor biosynthesis; adenosylcobalamin biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. SAAS SAAS019478

Porphyrin metabolism; siroheme biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1. SAAS SAAS019478

Porphyrin metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1. SAAS SAAS019478

Porphyrin metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. SAAS SAAS019478

Sequence similarities

Belongs to the precorrin methyltransferase family. RuleBase RU003960

Sequences

Sequence LengthMass (Da)Tools
Q0ASU7 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 5E0A46082AFB64EF

FASTA46448,907
        10         20         30         40         50         60 
MRVFPASIPL DGQTVIVVGQ GPMAEPKARL FASSPARLLW FTGETHDPVA SDIAQYAKII 

        70         80         90        100        110        120 
RRVPTRRDFR GATLIFLAGG EDRALAKLAR WGRSQGALVN IVDSPAASDF QTPAIVDRDG 

       130        140        150        160        170        180 
IVVSIASGGA APVLSVDIRA AIEQILPARI GDIADLARGL RGTVKSVLGK FDDRRAFWER 

       190        200        210        220        230        240 
ALRGKARDLA LSGDKAGARR EMLRELNGET SARAGIVHLV GAGPGDPDLL TLKAARLLRE 

       250        260        270        280        290        300 
ADVIVHDRLV SQGVMDLARR DALRIDVGKT KGHHPVPQEQ IGEILVREAR KGQRVVRIKG 

       310        320        330        340        350        360 
GDPFVFGRGG EELDVVRAAG IKAEVTPGIT AAVACAASAG IPLTHRDHAQ SVTFASGVVK 

       370        380        390        400        410        420 
QDGPDADYRA LSAPNSTTVF YMGVGAAPDI QAKMIEAGRD PATPVALVEN GTLDTERRVF 

       430        440        450        460 
GTLGDLAALV EREAISGPTI MIVGEVAGAA LTSARASAGQ EQFA

« Hide

References

[1]"Complete sequence of Maricaulis maris MCS10."
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., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P., Stephens C., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MCS10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000449 Genomic DNA. Translation: ABI64640.1.
RefSeqYP_755578.1. NC_008347.1.

3D structure databases

ProteinModelPortalQ0ASU7.
ModBaseSearch...

Protein-protein interaction databases

STRING394221.Mmar10_0347.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI64640; ABI64640; Mmar10_0347.
GeneID4285499.
KEGGmmr:Mmar10_0347.
PATRIC22448674. VBIMarMar77530_0347.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290518.
KOK02302.
OMAQASFIMP.
ProtClustDBCLSK2780897.

Enzyme and pathway databases

BioCycMMAR394221:GHNB-401-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.
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. Cor/por_Metransf. 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 nameQ0ASU7_MARMM
AccessionPrimary (citable) accession number: Q0ASU7
Entry history
Integrated into UniProtKB/TrEMBL: October 17, 2006
Last sequence update: October 17, 2006
Last modified: May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info